|
Name |
Accession |
Description |
Interval |
E-value |
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-590 |
0e+00 |
|
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: 784.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 28 TKEPAPGSELASALRSCKAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRG 107
Cdd:COG4618 2 SRASAGRSELRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 108 RIMNRIGAELDEAVGGRVFTAVSRLPLyIGQQGDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTT 187
Cdd:COG4618 82 RILVRVGARLDRRLGPRVFDAAFRAAL-RGGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 188 AACGALVLVTLTVATEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGG 267
Cdd:COG4618 161 ALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 268 FGSFARALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRLSKLLARLPQDAQ 347
Cdd:COG4618 241 FSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 348 PMALPVPGSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS 427
Cdd:COG4618 321 RMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 428 SERLGRYIGYLPQDVELFAGTVADNIARFdPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALA 507
Cdd:COG4618 401 REELGRHIGYLPQDVELFDGTIAENIARF-GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 508 RALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLSTLLP 587
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLAR 559
|
...
gi 1555720989 588 APQ 590
Cdd:COG4618 560 PAA 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
41-585 |
0e+00 |
|
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: 672.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 41 LRSCKAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEA 120
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 121 VGGRVFTAVSRLPLYIGQqGDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTV 200
Cdd:TIGR01842 81 LNQPIFAASFSATLRRGS-GDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 201 ATEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQ 280
Cdd:TIGR01842 160 LNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 281 SAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRLSKLLARLPQDAQPMALPVPGSKLTV 360
Cdd:TIGR01842 240 SLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPEPEGHLSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 361 ERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQ 440
Cdd:TIGR01842 320 ENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 DVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLD 520
Cdd:TIGR01842 400 DVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 521 EPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLSTL 585
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-583 |
2.59e-118 |
|
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: 367.24 E-value: 2.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 25 PSSTKEPAPGSELASALRSCKAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDL 104
Cdd:COG2274 135 DKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 105 VRGRIMNRIGAELDEAVGGRVFTAVSRLPL-YIGQQ--GDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLH 181
Cdd:COG2274 215 LRSYLLLRLGQRIDLRLSSRFFRHLLRLPLsFFESRsvGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 182 PTLGTTAACGALVLVTLTVATEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRV 261
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 262 SDIVGGFGSFARALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRLSKLLAR 341
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 342 LP---QDAQPMALPVPGSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKL 418
Cdd:COG2274 455 PPereEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 419 DGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSA 498
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 499 GQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMaLAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTR 578
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEA-IILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
....*
gi 1555720989 579 ESVLS 583
Cdd:COG2274 694 EELLA 698
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
45-335 |
5.55e-103 |
|
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: 313.77 E-value: 5.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGR 124
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 125 VFTAVSRLPLYIGQQGDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTVATEI 204
Cdd:cd18586 81 VFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 205 LTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAML 284
Cdd:cd18586 161 ATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLIL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 285 GVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRL 335
Cdd:cd18586 241 GVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
26-585 |
7.53e-92 |
|
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: 297.55 E-value: 7.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 26 SSTKEPAPGSELASALRSCKAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLV 105
Cdd:TIGR03375 127 DELISPRPKHWFWSTLKESWPLYRDVLIASLLINLLALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 106 RGRIMNRIGAELDEAVGGRVFTAVSRLPL---------YIGQQgdglqpqRDLDNIRTFLSSAGPGTLFDLPWLPFYLAI 176
Cdd:TIGR03375 207 RSYFLDVAGKKADLILSAKLFERVLGLRMearpasvgsFANQL-------REFESVRDFFTSATLTALIDLPFALLFLLV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 177 IWSLHPTLgttaACGALVLVTLTVATEILTRRPMGAAVqssvrRNSLAEASRRNA---EVLQA-------MGMGRRLHdH 246
Cdd:TIGR03375 280 IAIIGGPL----VWVPLVAIPLILLPGLLLQRPLSRLA-----EESMRESAQRNAvlvESLSGletikalNAEGRFQR-R 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 247 WREASRE--HLALQQR-VSDIVGGFGSFARALrlmLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPV-DLA--IA 320
Cdd:TIGR03375 350 WEQTVAAlaRSGLKSRfLSNLATNFAQFIQQL---VSVAIVVVGVYLISDGELTMGGLIACVMLSGRALAPLgQLAglLT 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 321 HWRNFVGARQSWSRLSKLLARLPQDAQPMALPVPGSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSS 400
Cdd:TIGR03375 427 RYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKST 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 401 LVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIG 480
Cdd:TIGR03375 507 LLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 481 LPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKArGGILAIVAHRPNILST 560
Cdd:TIGR03375 587 HPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA-GKTLVLVTHRTSLLDL 665
|
570 580
....*....|....*....|....*
gi 1555720989 561 VDFLLVMKEGQTQMFGTRESVLSTL 585
Cdd:TIGR03375 666 VDRIIVMDNGRIVADGPKDQVLEAL 690
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
37-571 |
3.96e-84 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 274.35 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 37 LASALRSCKAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAE 116
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 117 LDEAVGGRVFTAVSRLPL-YIGQQGDG-----LQpqRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAAC 190
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLsFFDRRRTGdllsrLT--NDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 191 GALVLVTLTVateILTRR--PMGAAVQSSVRR-NSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGG 267
Cdd:COG1132 170 VLPLLLLVLR---LFGRRlrKLFRRVQEALAElNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 268 FGSFARALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRLSKLLA---RLPQ 344
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDeppEIPD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 345 DAQPMALPVPGSKLTVERIAIGAPGAQRIIvQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALD 424
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENVSFSYPGDRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 425 QWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRI 504
Cdd:COG1132 406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 505 ALARALYGDPFLVVLDEPNSNLDAEGEMAlaaailaikarggILA------------IVAHRpniLSTV---DFLLVMKE 569
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEAL-------------IQEalerlmkgrttiVIAHR---LSTIrnaDRILVLDD 549
|
..
gi 1555720989 570 GQ 571
Cdd:COG1132 550 GR 551
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
48-583 |
5.62e-68 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 233.87 E-value: 5.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 48 FAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTL--IAMAILAGALFagQAVIDLVRGRIM----NRIGAELdeav 121
Cdd:TIGR01846 141 FREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLsvLALAMLAVAIF--EPALGGLRTYLFahltSRIDVEL---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 122 GGRVFTAVSRLPL-YIGQQ--GDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLgTTAACGALVL-VT 197
Cdd:TIGR01846 215 GARLYRHLLGLPLgYFESRrvGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTL-TGVVIGSLVCyAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 198 LTVATEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDiVGGFGSFARALRL 277
Cdd:TIGR01846 294 LSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTN-LGNIAGQAIELIQ 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 278 MLQSAM-LGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRLSKLL--ARLPQDAQPMALPVP 354
Cdd:TIGR01846 373 KLTFAIlLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILnsPTEPRSAGLAALPEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 355 GSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY 434
Cdd:TIGR01846 453 RGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDP 514
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNP 612
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 515 FLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:TIGR01846 613 RILIFDEATSALDYESE-ALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
358-571 |
1.25e-63 |
|
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: 207.07 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGY 437
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVELFAGTVADNIarfdpgpdpqaivaaaraagvheliiglpngyetqigeggtaLSAGQRQRIALARALYGDPFLV 517
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1555720989 518 VLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
175-584 |
3.97e-63 |
|
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: 218.10 E-value: 3.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 175 AIIWSLHPTLG-TTAACGALVLVTLTVATEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASRE 253
Cdd:COG4987 148 AFLAFFSPALAlVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEAR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 254 HLALQQRVSdivgGFGSFARALRLMLQS----AMLGVGAWLVIEGeATSGIIIAGSIL----VGRALAPVDLAIAHWRnf 325
Cdd:COG4987 228 LAAAQRRLA----RLSALAQALLQLAAGlavvAVLWLAAPLVAAG-ALSGPLLALLVLaalaLFEALAPLPAAAQHLG-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 326 vGARQSWSRLSKLLARLPQ---DAQPMALPVPGSkLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLV 402
Cdd:COG4987 301 -RVRAAARRLNELLDAPPAvtePAEPAPAPGGPS-LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 403 RGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLP 482
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALP 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 483 NGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTVD 562
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE-QALLADLLEALAGRTVLLITHRLAGLERMD 537
|
410 420
....*....|....*....|..
gi 1555720989 563 FLLVMKEGQTQMFGTRESVLST 584
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQ 559
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
368-571 |
3.15e-53 |
|
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: 181.25 E-value: 3.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 368 PGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAG 447
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03245 93 TLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1555720989 528 AEGEMaLAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03245 173 MNSEE-RLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
37-584 |
8.31e-53 |
|
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: 189.97 E-value: 8.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 37 LASALRSCKAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVL-PSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGA 115
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 116 ELDEAVGGRVFTAVSRL-PLYIGQQGDGLQPQRDLDNI------------RTFLSSAGPGTLfdlpwlpfyLAIIWSLHP 182
Cdd:COG4988 88 RVKRRLRRRLLEKLLALgPAWLRGKSTGELATLLTEGVealdgyfarylpQLFLAALVPLLI---------LVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 183 tlgttaACGALVLVT--LTVATEILTRrpMGAAVQSSVRRNSLAEASRRNAEVLQAM------GMGRRLHDHWREASREH 254
Cdd:COG4988 159 ------LSGLILLVTapLIPLFMILVG--KGAAKASRRQWRALARLSGHFLDRLRGLttlklfGRAKAEAERIAEASEDF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 255 lalqqRVSDIvggfgsfaRALRLMLQSAMlgvgawlVIEGEATSGI----------IIAGSILVGRAL----------AP 314
Cdd:COG4988 231 -----RKRTM--------KVLRVAFLSSA-------VLEFFASLSIalvavyigfrLLGGSLTLFAALfvlllapeffLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 315 VDLAIAHWRNFVGARQSWSRLSKLLARLPQDAQPMALPVP---GSKLTVERIAIGAPGAQRIIvQGVEFSLDAGSVLGII 391
Cdd:COG4988 291 LRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPaagPPSIELEDVSFSYPGGRPAL-DGLSLTIPPGERVALV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 392 GPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARA 471
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 472 AGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIV 551
Cdd:COG4988 450 AGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE-AEILQALRRLAKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|...
gi 1555720989 552 AHRPNILSTVDFLLVMKEGQTQMFGTRESVLST 584
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
371-582 |
2.90e-46 |
|
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: 162.78 E-value: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVA 450
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 531 EmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVL 582
Cdd:cd03254 175 E-KLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
51-335 |
6.47e-46 |
|
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: 163.91 E-value: 6.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 51 VAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVS 130
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 131 RLPL-YIGQQGDGLQPQR--DLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTVATEILTR 207
Cdd:cd18566 87 SLPLsFFEREPSGAHLERlnSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 208 RPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAMLGVG 287
Cdd:cd18566 167 RALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1555720989 288 AWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRL 335
Cdd:cd18566 247 ALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
358-583 |
9.41e-46 |
|
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: 161.63 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGY 437
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLV 517
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 518 VLDEPNSNLDAEGEMAL-AAAILAIKARGGIlaIVAHRpniLSTV---DFLLVMKEGQTQMFGTRESVLS 583
Cdd:cd03251 161 ILDEATSALDTESERLVqAALERLMKNRTTF--VIAHR---LSTIenaDRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
358-583 |
2.53e-44 |
|
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: 158.03 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGY 437
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLV 517
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 518 VLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:cd03252 161 IFDEATSALDYESE-HAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
368-571 |
1.52e-43 |
|
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: 153.31 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 368 PGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAG 447
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIarfdpgpdpqaivaaaraagvheliiglpngyetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03228 91 TIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1555720989 528 AEGEmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03228 129 PETE-ALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
372-583 |
2.16e-43 |
|
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: 155.08 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVAD 451
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGE 531
Cdd:cd03253 94 NIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 532 MaLAAAILAIKARGGILAIVAHRpniLSTV---DFLLVMKEGQTQMFGTRESVLS 583
Cdd:cd03253 174 R-EIQAALRDVSKGRTTIVIAHR---LSTIvnaDKIIVLKDGRIVERGTHEELLA 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
180-531 |
4.14e-42 |
|
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: 159.45 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 180 LHPTLGTTAACGALVLVtltVATEILTRRPMGAAVQSSVR-RNSLAEASR---RNAEVLQAMGMGRRLHDHWREASREHL 255
Cdd:TIGR02868 151 LSVPAALILAAGLLLAG---FVAPLVSLRAARAAEQALARlRGELAAQLTdalDGAAELVASGALPAALAQVEEADRELT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 256 ALQQRvsdivggfGSFARALRLMLQSAMLGVGAW--LVIEGEATSGIIIAGSIL---------VGRALAPVDLAIAHWRN 324
Cdd:TIGR02868 228 RAERR--------AAAATALGAALTLLAAGLAVLgaLWAGGPAVADGRLAPVTLavlvllplaAFEAFAALPAAAQQLTR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 325 FVGARQSWSRL--SKLLARLPQDAQPMALPVPGSKLTVERIAIGAPGAQRIiVQGVEFSLDAGSVLGIIGPSGSGKSSLV 402
Cdd:TIGR02868 300 VRAAAERIVEVldAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 403 RGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLP 482
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALP 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1555720989 483 NGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGE 531
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
338-567 |
7.36e-42 |
|
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: 158.60 E-value: 7.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 338 LLARLPQDAQPMA--LPVPGSKLTVERIAIGAPGAqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGR 415
Cdd:TIGR02857 300 VLDAAPRPLAGKApvTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 416 IKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTA 495
Cdd:TIGR02857 379 IAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 496 LSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVM 567
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE-AEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
373-577 |
2.00e-40 |
|
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: 147.30 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 373 IIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADN 452
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEM 532
Cdd:cd03249 97 IRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1555720989 533 aLAAAILAIKARGGILAIVAHRpniLSTV---DFLLVMKEGQTQMFGT 577
Cdd:cd03249 177 -LVQEALDRAMKGRTTIVIAHR---LSTIrnaDLIAVLQNGQVVEQGT 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
372-571 |
1.17e-36 |
|
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: 136.45 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVAD 451
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGE 531
Cdd:cd03248 107 NIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1555720989 532 MALAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03248 187 QQVQQALYDWPERRTVLVI-AHRLSTVERADQILVLDGGR 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
220-577 |
2.41e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 144.86 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 220 RNSLAEASRRNAEVLQAMGMGRRLH------DHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAMLGVGAWLVIE 293
Cdd:TIGR00958 333 QEAVAKANQVAEEALSGMRTVRSFAaeegeaSRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLT 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 294 GEATSGIIIAGSIL---VGRALAPVDLAIAHWRNFVGARqswSRLSKLLARLPQDAQP---MALPVPGsKLTVERIAIGA 367
Cdd:TIGR00958 413 GKVSSGNLVSFLLYqeqLGEAVRVLSYVYSGMMQAVGAS---EKVFEYLDRKPNIPLTgtlAPLNLEG-LIEFQDVSFSY 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 368 PG-AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFA 446
Cdd:TIGR00958 489 PNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFS 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 GTVADNIAR-FDPGPDPQAIVAAARAaGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:TIGR00958 569 GSVRENIAYgLTDTPDEEIMAAAKAA-NAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 526 LDAEGEmalaAAILAIKARGGILAIV-AHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:TIGR00958 648 LDAECE----QLLQESRSRASRTVLLiAHRLSTVERADQILVLKKGSVVEMGT 696
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
274-571 |
1.71e-35 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 142.19 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 274 ALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRLSKLL---ARLPQDAQPMA 350
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYlvdSEFINKKKRTE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 351 LPVPGSKLTVERIAIGApGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER 430
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 431 LGRYIGYLPQDVELFAGTVADN-IARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARA 509
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENlLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 510 LYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILaiVAHRPNILSTVDFLLVMKEGQ 571
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIF--VAHRLSVAKQSDKIIVLDHGK 685
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
344-583 |
4.06e-34 |
|
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: 136.77 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 344 QDAQPMALPVPGSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAL 423
Cdd:TIGR02203 317 KDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 424 DQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAG-VHELIIGLPNGYETQIGEGGTALSAGQRQ 502
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAyAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 503 RIALARALYGDPFLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRpniLSTV---DFLLVMKEGQTQMFGTRE 579
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESE-RLVQAALERLMQGRTTLVIAHR---LSTIekaDRIVVMDDGRIVERGTHN 552
|
....
gi 1555720989 580 SVLS 583
Cdd:TIGR02203 553 ELLA 556
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
324-571 |
6.80e-34 |
|
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: 136.49 E-value: 6.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 324 NFVGA-----RQSWS---RLSKLLARLP--QDA-QPMALPVPGSKLTVERIAIGApGAQRIIVQGVEFSLDAGSVLGIIG 392
Cdd:COG5265 313 NFLGFvyreiRQALAdmeRMFDLLDQPPevADApDAPPLVVGGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 393 PSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAA 472
Cdd:COG5265 392 PSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 473 GVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMAlaaailaikarggILA--- 549
Cdd:COG5265 472 QIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA-------------IQAalr 538
|
250 260 270
....*....|....*....|....*....|....
gi 1555720989 550 ---------IVAHRpniLSTV---DFLLVMKEGQ 571
Cdd:COG5265 539 evargrttlVIAHR---LSTIvdaDEILVLEAGR 569
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
59-315 |
1.88e-32 |
|
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: 126.78 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 59 NILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVSRLPL---- 134
Cdd:cd18587 15 NLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSRLFERVLGLRLearp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 135 -YIGQQGDGLqpqRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLgttaACGALVLVTLTVATEILTRRPMGAA 213
Cdd:cd18587 95 aSVGSFANNL---REFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPL----ALVPLVAIPLVLLYGLLLQKPLRRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 214 VQSSVRrnslaEASRRNA---------EVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAML 284
Cdd:cd18587 168 VEESMR-----ESAQKNAllveslsglETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIV 242
|
250 260 270
....*....|....*....|....*....|.
gi 1555720989 285 GVGAWLVIEGEATSGIIIAGSILVGRALAPV 315
Cdd:cd18587 243 IVGVYLISDGELTMGGLIACVILSGRALAPL 273
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
358-583 |
1.39e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 123.23 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGY 437
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVEL-FAGTVADNIAR---------FDPGP-DPQAIVAAARAAGVHELIiglpngyETQIGEggtaLSAGQRQRIAL 506
Cdd:COG1120 80 VPQEPPApFGLTVRELVALgryphlglfGRPSAeDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 507 ARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVA-HRPNILSTV-DFLLVMKEGQTQMFGTRESVLS 583
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVlHDLNLAARYaDRLVLLKDGRIVAQGPPEEVLT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
358-529 |
1.81e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.46 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGApgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGY 437
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVELFAGTVADNIAR----FDPGPDPQAivaaaraagVHELI--IGLPNGY-ETQIGEggtaLSAGQRQRIALARAL 510
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFpfqlRERKFDRER---------ALELLerLGLPPDIlDKPVER----LSGGERQRLALIRAL 145
|
170
....*....|....*....
gi 1555720989 511 YGDPFLVVLDEPNSNLDAE 529
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPE 164
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
284-582 |
2.27e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 128.68 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 284 LGVGAWLVIEGEATSGIIIAGSILVGRALAPVdLAIAHWRNFVgARQS--WSRLSKLLARLP--QDAQpMALPVPGSKLT 359
Cdd:PRK10789 239 IGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPM-LALAWMFNIV-ERGSaaYSRIRAMLAEAPvvKDGS-EPVPEGRGELD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 360 VERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLP 439
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 440 QDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVL 519
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 520 DEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVL 582
Cdd:PRK10789 476 DDALSAVDGRTE-HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
375-522 |
1.46e-30 |
|
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: 116.98 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAG-TVADNI 453
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 454 ARfdpGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
380-571 |
8.30e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 124.19 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDAGSVLGIIGPSGSGKSSLVRGLVGaWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPG 459
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 460 PDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEmALAAAIL 539
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE-QLVMQAL 528
|
170 180 190
....*....|....*....|....*....|..
gi 1555720989 540 AIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:PRK11174 529 NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
282-570 |
1.25e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 123.53 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 282 AMLGVGAWLVIEGEATSGIIIA----GSILVGRalapvdlaIAHWRNFV-GARQSWSRLS---KLLARLPQDAQPMALPV 353
Cdd:PRK13657 256 AILVLGAALVQKGQLRVGEVVAfvgfATLLIGR--------LDQVVAFInQVFMAAPKLEeffEVEDAVPDVRDPPGAID 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 354 PGS---KLTVERIAIGAPGaQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER 430
Cdd:PRK13657 328 LGRvkgAVEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 431 LGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARAL 510
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 511 YGDPFLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRpniLSTV---DFLLVMKEG 570
Cdd:PRK13657 487 LKDPPILILDEATSALDVETE-AKVKAALDELMKGRTTFIIAHR---LSTVrnaDRILVFDNG 545
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
45-326 |
4.01e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 117.23 E-value: 4.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGR 124
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 125 VFTAVSRLPLYIGQQ---GDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTva 201
Cdd:cd18555 81 FFEHLLKLPYSFFENrssGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 202 teILTRRPMGAAVQSSVRRNS-----LAEASRrNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALR 276
Cdd:cd18555 159 --LLTRKKIKKLNQEEIVAQTkvqsyLTETLY-GIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1555720989 277 LMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFV 326
Cdd:cd18555 236 FIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
359-576 |
9.44e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 112.91 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 359 TVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYL 438
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 439 PQDVELFagtvadNIARFdpgpdpqaivaaaraagVHELIiglpngyetqigeggTALSAGQRQRIALARALYGDPFLVV 518
Cdd:cd03214 79 PQALELL------GLAHL-----------------ADRPF---------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 519 LDEPNSNLDAEGEMALAAAILAIKARGGILAIVA-HRPNILSTV-DFLLVMKEGQTQMFG 576
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVlHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
374-571 |
2.01e-28 |
|
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: 112.56 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAaldqwsserlgryIGYLPQDVELFAGTVADNI 453
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ---ARFDP------------GPDPQAivaaaraagvheliigLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVV 518
Cdd:cd03250 87 lfgKPFDEeryekvikacalEPDLEI----------------LPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1555720989 519 LDEPNSNLDAE-----------GEMalaaailaIKARGGILaiVAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03250 151 LDDPLSAVDAHvgrhifencilGLL--------LNNKTRIL--VTHQLQLLPHADQIVVLDNGR 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
371-555 |
4.28e-28 |
|
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: 111.80 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQwSSERLGRYIGYLPQDVELFAG-TV 449
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNI---ARFDPGPDPQAIvaaaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:COG4133 93 RENLrfwAALYGLRADREA--------IDEALeaVGLAGLADLPVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|.
gi 1555720989 525 NLDAEGEMALAAAILAIKARGGILAIVAHRP 555
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
360-571 |
7.39e-28 |
|
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: 111.40 E-value: 7.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 360 VERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLP 439
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 440 QDVE--LFAGTVADNIArFdpGPDPQAIVAAARAAGVHE-LIIGLPNGYETQ-IGEggtaLSAGQRQRIALARALYGDPF 515
Cdd:cd03225 82 QNPDdqFFGPTVEEEVA-F--GLENLGLPEEEIEERVEEaLELVGLEGLRDRsPFT----LSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 516 LVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTV-DFLLVMKEGQ 571
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
371-571 |
1.10e-27 |
|
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: 108.87 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQdvelfagtva 450
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 dniarfdpgpdpqaivaaaraagvheliiglpngyetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:cd00267 81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1555720989 531 EMALAAAILAIKARGGILAIVAHRPNILSTV-DFLLVMKEGQ 571
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
45-335 |
1.37e-27 |
|
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: 112.98 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAI--LAGALFagQAVIDLVRGRIM----NRIGAELd 118
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIglLVVALF--EAVLSGLRTYLFshttNRIDAEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 119 eavGGRVFTAVSRLPL-YIG--QQGDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVL 195
Cdd:cd18588 78 ---GARLFRHLLRLPLsYFEsrQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 196 VTLT-VATEILTRR-----PMGAAVQSsvrrnSLAEaSRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFG 269
Cdd:cd18588 155 ALLSlLVTPILRRRleekfQRGAENQS-----FLVE-TVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLAS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 270 SFARALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVdLAIAH-WRNFVGARQSWSRL 335
Cdd:cd18588 229 QIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPV-LRLVQlWQDFQQAKVSVERL 294
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
371-532 |
5.57e-27 |
|
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: 108.77 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAaldqwSSERLGRYIGYLPQDVEL---FAG 447
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSIdrdFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA-RFDPGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:cd03235 86 SVRDVVLmGLYGHKGLFRRLSKADKAKVDEALerVGLSELADRQIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
....*...
gi 1555720989 525 NLDAEGEM 532
Cdd:cd03235 162 GVDPKTQE 169
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
358-583 |
5.62e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 115.00 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRP---LAGRIKLDGAALDQWSSERLGRY 434
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQDVE--LFAGTVADNIARfdpGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARAL 510
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAE---ALENLGLSRAEARARVLELLeaVGLERRLDRYPHQ----LSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 511 YGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGI-LAIVAHRPN-ILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
374-577 |
1.56e-26 |
|
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: 107.58 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNI 453
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ARFDPGPDpQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMA 533
Cdd:cd03244 99 DPFGEYSD-EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1555720989 534 LAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:cd03244 178 IQKTIREAFKDCTVLTI-AHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
180-583 |
2.55e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.38 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 180 LHPTLGTTAaCGALVLVTLTVATeILTR--RPMGAAVQSSVR--RNSLAEASRRNAEvLQAMGMGRRLHDHWREASREHL 255
Cdd:PRK11160 158 FDLTLALTL-GGILLLLLLLLPL-LFYRlgKKPGQDLTHLRAqyRVQLTEWLQGQAE-LTLFGAEDRYRQQLEQTEQQWL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 256 ALQQRVSDIVGgfgsFARALrLMLQSAMLGVGA-WLV---IEGEATSGIIIA-------GSIlvgRALAPVDLAIAHWRN 324
Cdd:PRK11160 235 AAQRRQANLTG----LSQAL-MILANGLTVVLMlWLAaggVGGNAQPGALIAlfvfaalAAF---EALMPVAGAFQHLGQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 325 FVGARQswsRLSKLLARLPQ---DAQPMALPVPGSkLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSL 401
Cdd:PRK11160 307 VIASAR---RINEITEQKPEvtfPTTSTAAADQVS-LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 402 VRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGl 481
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED- 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 482 PNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTV 561
Cdd:PRK11160 462 DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE-RQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
410 420
....*....|....*....|..
gi 1555720989 562 DFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLA 562
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
371-583 |
3.45e-26 |
|
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: 107.03 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVE--LFAGT 448
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIArFdpGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:COG1122 93 VEEDVA-F--GPENLGLPREEIRERVEEALelVGLEHLADRPPHE----LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 527 DAEGEMALAAAILAIKARGGILAIVAHRPN-ILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
374-577 |
3.87e-26 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 106.34 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNI 453
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ARFDPGPDPQAIVAAaraagvheliiglpngyetQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMA 533
Cdd:cd03369 103 DPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1555720989 534 LAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:cd03369 164 IQKTIREEFTNSTILTI-AHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
358-576 |
5.60e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 104.70 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSErLGRYIGY 437
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVELFAGTVADNIarfdpgpdpqaivaaaraagvheliiglpngyetqigegGTALSAGQRQRIALARALYGDPFLV 517
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 518 VLDEPNSNLDAEGEmALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFG 576
Cdd:cd03247 121 LLDEPTVGLDPITE-RQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
372-530 |
7.39e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.30 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyIGYLPQDVELFAG-TVA 450
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNI---ARFDPGPDPQAIVAaaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:COG1131 92 ENLrffARLYGLPRKEARER------IDELLelFGLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
....*
gi 1555720989 526 LDAEG 530
Cdd:COG1131 162 LDPEA 166
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
374-576 |
9.74e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 105.29 E-value: 9.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADN 452
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IArFdpGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:cd03259 93 IA-F--GLKLRGVPKAEIRARVRELLelVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1555720989 531 EMALAAAILAIKARGGILAI-VAHRPN-ILSTVDFLLVMKEGQTQMFG 576
Cdd:cd03259 166 REELREELKELQRELGITTIyVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
374-571 |
1.42e-25 |
|
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: 104.88 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY----IGYLPQDVELFAG-T 448
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSFNLLPDlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIA---RFDPGPDPQAIVAaaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:cd03255 99 ALENVElplLLAGVPKKERRER------AEELLerVGLGDRLNHYPSE----LSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1555720989 524 SNLDAE-GEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03255 169 GNLDSEtGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
371-531 |
4.02e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.40 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALdqwssERLGRYIGYLPQDVEL---FAG 447
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYVPQRAEVdwdFPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA-------RFDPGPDPQAIVAaaraagVHELI--IGLpNGYE-TQIGEggtaLSAGQRQRIALARALYGDPFLV 517
Cdd:COG1121 93 TVRDVVLmgrygrrGLFRRPSRADREA------VDEALerVGL-EDLAdRPIGE----LSGGQQQRVLLARALAQDPDLL 161
|
170
....*....|....
gi 1555720989 518 VLDEPNSNLDAEGE 531
Cdd:COG1121 162 LLDEPFAGVDAATE 175
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
358-528 |
6.75e-25 |
|
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: 103.35 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVE--RIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG---AALDQWSSERLG 432
Cdd:cd03257 2 LEVKnlSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 433 RYIGYLPQDvelfAG-------TVADNIA----RFDPGPDPQAIVAAARAAGVHeliIGLP----NGYETQigeggtaLS 497
Cdd:cd03257 82 KEIQMVFQD----PMsslnprmTIGEQIAeplrIHGKLSKKEARKEAVLLLLVG---VGLPeevlNRYPHE-------LS 147
|
170 180 190
....*....|....*....|....*....|.
gi 1555720989 498 AGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDV 178
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
368-582 |
9.14e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.57 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 368 PGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAG 447
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNI--ARFDPGPDPQAIVAAARAAGVhELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:PRK11176 432 TIANNIayARTEQYSREQIEEAARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 526 LDAEGEMALAAAILAIKARGGILAIvAHRpniLSTV---DFLLVMKEGQTQMFGTRESVL 582
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSLVI-AHR---LSTIekaDEILVVEDGEIVERGTHAELL 566
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
371-530 |
1.83e-24 |
|
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: 100.16 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQwSSERLGRYIGYLPQDVELFAG-TV 449
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIarfdpgpdpqaivaaaraagvheliiglpngyetqigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:cd03230 91 RENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
.
gi 1555720989 530 G 530
Cdd:cd03230 130 S 130
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
374-528 |
2.58e-23 |
|
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: 99.16 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyIGYLPQDVELFAG-TVADN 452
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 I---ARFDPGPDPQAIVAaaraagVHELII--GLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:COG4555 95 IryfAELYGLFDEELKKR------IEELIEllGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
.
gi 1555720989 528 A 528
Cdd:COG4555 165 V 165
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
375-528 |
5.55e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.61 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVR---GLVgawRPLAGRIKLDGAALDQWSSERLgRYIGYLPQDVELFAG-TVA 450
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRiiaGLE---TPDSGRIVLNGRDLFTNLPPRE-RRVGFVFQHYALFPHmTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIArFdpGPDPQAIVAAARAAGVHELII-----GLPNGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:COG1118 94 ENIA-F--GLRVRPPSKAEIRARVEELLElvqleGLADRYPSQ-------LSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
...
gi 1555720989 526 LDA 528
Cdd:COG1118 164 LDA 166
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
51-335 |
6.39e-23 |
|
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: 99.20 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 51 VAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVS 130
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 131 RLPLYIGQQ---GDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLgTTAACGAL-VLVTLTVATEILT 206
Cdd:cd18782 87 RLPLGFFDKrpvGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLL-TLVVLATVpLQLLLTFLFGPIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 207 RRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAMLGV 286
Cdd:cd18782 166 RRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1555720989 287 GAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRL 335
Cdd:cd18782 246 GAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
369-529 |
6.76e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.42 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRI-IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL----GRYIGYLPQDVE 443
Cdd:COG1136 17 GEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 444 LFAG-TVADNI------ARFDPGPDPQAIVAAARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFL 516
Cdd:COG1136 97 LLPElTALENValplllAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKL 165
|
170
....*....|...
gi 1555720989 517 VVLDEPNSNLDAE 529
Cdd:COG1136 166 ILADEPTGNLDSK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
380-573 |
8.87e-23 |
|
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: 96.98 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDA-----GSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAldqWSSERLG-------RYIGYLPQDVELFAG 447
Cdd:cd03297 13 FTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKinlppqqRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 -TVADNIA----RFDPGPDPQAIVAAARAAGVHELIiglpNGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:cd03297 90 lNVRENLAfglkRKRNREDRISVDELLDLLGLDHLL----NRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 523 NSNLDAEGEMALAAAILAIKARGGILAI-VAHRPNILSTV-DFLLVMKEGQTQ 573
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIfVTHDLSEAEYLaDRIVVMEDGRLQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
370-529 |
1.31e-22 |
|
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: 95.33 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER--LGRYIGYLPQDVELFAG 447
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 -TVADNIArfdpgpdpqaivaaaraagvheliiglpngyetqigeggTALSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:cd03229 91 lTVLENIA---------------------------------------LGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
...
gi 1555720989 527 DAE 529
Cdd:cd03229 132 DPI 134
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
374-528 |
1.59e-22 |
|
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: 101.52 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER---LGRYIGYLPQDVE--LFAG- 447
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDPYssLNPRm 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIAR----FDPGPDPQAIVAaaraagVHELI--IGLPNGYETQ-IGEggtaLSAGQRQRIALARALYGDPFLVVLD 520
Cdd:COG1123 360 TVGDIIAEplrlHGLLSRAERRER------VAELLerVGLPPDLADRyPHE----LSGGQRQRVAIARALALEPKLLILD 429
|
....*...
gi 1555720989 521 EPNSNLDA 528
Cdd:COG1123 430 EPTSALDV 437
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
375-592 |
1.78e-22 |
|
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: 96.64 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNI 453
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 A------RFDPGPDPQAIVAAARAAGVHELIIGLPngyetqigeggTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03299 93 AyglkkrKVDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 528 AEGEMALAAAILAIKARGGILAI-VAHR-PNILSTVDFLLVMKEGQTQMFGTRESVLSTllPAPQTV 592
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLhVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFKK--PKNEFV 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
374-522 |
2.55e-22 |
|
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: 95.58 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY-IGYLPQDVELFAG-TVAD 451
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 452 NI-----ARFDPGPDPQAIVaaaraagVHELiigLPNGYETQIGEGGTaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:cd03224 95 NLllgayARRRAKRKARLER-------VYEL---FPRLKERRKQLAGT-LSGGEQQMLAIARALMSRPKLLLLDEP 159
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
374-528 |
3.19e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADN 452
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVFQDYALFPHlTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IA---RFDPGPDPQAIVAaaraagVHELI--IGLPnGYETQ-IGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:COG3842 98 VAfglRMRGVPKAEIRAR------VAELLelVGLE-GLADRyPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
|
..
gi 1555720989 527 DA 528
Cdd:COG3842 167 DA 168
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
363-528 |
8.46e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 94.87 E-value: 8.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 363 IAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDV 442
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 443 ELFA---GTVADNIArfdpgpDP-QAIVAAARAAGVHELI--IGLPNGYETQIGEggtALSAGQRQRIALARALYGDPFL 516
Cdd:COG1124 89 YASLhprHTVDRILA------EPlRIHGLPDREERIAELLeqVGLPPSFLDRYPH---QLSGGQRQRVAIARALILEPEL 159
|
170
....*....|..
gi 1555720989 517 VVLDEPNSNLDA 528
Cdd:COG1124 160 LLLDEPTSALDV 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-527 |
1.77e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVEL-FAGT 448
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIA------RFDPGPDPQAIVAAARAAGVHELiiglpngyetqigeGG---TALSAGQRQRIALARAL------YGD 513
Cdd:PRK13548 93 VEEVVAmgraphGLSRAEDDALVAAALAQVDLAHL--------------AGrdyPQLSGGEQQRVQLARVLaqlwepDGP 158
|
170
....*....|....
gi 1555720989 514 PFLVVLDEPNSNLD 527
Cdd:PRK13548 159 PRWLLLDEPTSALD 172
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
366-528 |
1.96e-21 |
|
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: 92.92 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 366 GAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALdqwssERLGRYIGYLPQDVELF 445
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQQDALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 A-GTVADNIArFdpGPDPQAIVAAARAAGVHELI--IGLP---NGYETQigeggtaLSAGQRQRIALARALYGDPFLVVL 519
Cdd:cd03293 86 PwLTVLDNVA-L--GLELQGVPKAEARERAEELLelVGLSgfeNAYPHQ-------LSGGMRQRVALARALAVDPDVLLL 155
|
....*....
gi 1555720989 520 DEPNSNLDA 528
Cdd:cd03293 156 DEPFSALDA 164
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
358-529 |
2.35e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGApgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRP---LAGRIKLDGAALDQWSSERlgRY 434
Cdd:COG4136 2 LSLENLTITL--GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQDVELFAG-TVADNIArfdpgpdpqaivaaaraagvheliIGLPNGYE------------TQIGEGGTA------ 495
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLA------------------------FALPPTIGraqrrarveqalEEAGLAGFAdrdpat 133
|
170 180 190
....*....|....*....|....*....|....
gi 1555720989 496 LSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
372-527 |
2.40e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 93.34 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE---RLGRYIGYLPQDVELFAG- 447
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIArFdP----GPDPQAIVAAARAAGVHEliIGLPnGYETQI-GEggtaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:cd03261 93 TVFENVA-F-PlrehTRLSEEEIREIVLEKLEA--VGLR-GAEDLYpAE----LSGGMKKRVALARALALDPELLLYDEP 163
|
....*
gi 1555720989 523 NSNLD 527
Cdd:cd03261 164 TAGLD 168
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
366-529 |
3.34e-21 |
|
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: 92.64 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 366 GAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL---GRYIGYLPQDV 442
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 443 ELFAG-TVADNIA---RFDPGPDPQAIVAaaraagVHELI--IGLP---NGYETQigeggtaLSAGQRQRIALARALYGD 513
Cdd:cd03258 92 NLLSSrTVFENVAlplEIAGVPKAEIEER------VLELLelVGLEdkaDAYPAQ-------LSGGQKQRVGIARALANN 158
|
170
....*....|....*.
gi 1555720989 514 PFLVVLDEPNSNLDAE 529
Cdd:cd03258 159 PKVLLCDEATSALDPE 174
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
372-527 |
5.13e-21 |
|
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: 92.35 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE---RLGRYIGYLPQDVELFAG- 447
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIGMLFQGGALFDSl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA---RFDPGPDPQAivaaaraagVHELII------GLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVV 518
Cdd:COG1127 98 TVFENVAfplREHTDLSEAE---------IRELVLeklelvGLPGAADKMPSE----LSGGMRKRVALARALALDPEILL 164
|
....*....
gi 1555720989 519 LDEPNSNLD 527
Cdd:COG1127 165 YDEPTAGLD 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
369-529 |
1.23e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.88 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG---AALDQWSSERLGRYIGYLPQDVELF 445
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLRRRIGVVFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 AG-TVADNIArFdP----GPDPQAIVAAaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVV 518
Cdd:COG2884 92 PDrTVYENVA-L-PlrvtGKSRKEIRRR-----VREVLdlVGLSDKAKALPHE----LSGGEQQRVAIARALVNRPELLL 160
|
170
....*....|.
gi 1555720989 519 LDEPNSNLDAE 529
Cdd:COG2884 161 ADEPTGNLDPE 171
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
375-582 |
1.48e-20 |
|
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: 96.55 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAaldqwsserlgryIGYLPQDVELFAGTVADNIA 454
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 455 RFDPGPDPQAIVAAARAAGVHELIIgLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE--GEM 532
Cdd:TIGR00957 721 FGKALNEKYYQQVLEACALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvgKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1555720989 533 ALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVL 582
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
356-602 |
4.32e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 356 SKLTVERIAIGApGAQRIiVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYI 435
Cdd:PRK11231 1 MTLRTENLTVGY-GTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 436 GYLPQDVELFAG-TVADNIARfdpGPDPQAIVAAARAAGVHELIIGLPNgyETQIGEGG----TALSAGQRQRIALARAL 510
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRELVAY---GRSPWLSLWGRLSAEDNARVNQAME--QTRINHLAdrrlTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 511 YGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILST-VDFLLVMKEGQTQMFGTRESVLSTLLpap 589
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGL--- 230
|
250
....*....|...
gi 1555720989 590 qtvtagLQPVFKL 602
Cdd:PRK11231 231 ------LRTVFDV 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
358-582 |
6.70e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.63 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIG----APGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGR 433
Cdd:PRK10790 336 LQSGRIDIDnvsfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 434 YIGYLPQDVELFAGTVADNIARfdpGPDPQAIVAAARAAGVH--ELIIGLPNGYETQIGEGGTALSAGQRQRIALARALY 511
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTL---GRDISEEQVWQALETVQlaELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1555720989 512 GDPFLVVLDEPNSNLDAEGEMALAAAILAIKARgGILAIVAHRpniLSTV---DFLLVMKEGQTQMFGTRESVL 582
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHR---LSTIveaDTILVLHRGQAVEQGTHQQLL 562
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
374-583 |
8.35e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 94.27 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNI 453
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ARFDPGPDPQAIVAAARAAgVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEmA 533
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAH-IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD-S 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1555720989 534 LAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
354-528 |
8.85e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.38 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 354 PGSKLTVERIAI--GAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVR---GLVgawRPLAGRIKLDGAALdqwss 428
Cdd:COG1116 4 AAPALELRGVSKrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRliaGLE---KPTSGEVLVDGKPV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 429 ERLGRYIGYLPQDVELFA-GTVADNIArFdpGPDPQAIVAAARAAGVHELI--IGLpNGYET----QigeggtaLSAGQR 501
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPwLTVLDNVA-L--GLELRGVPKAERRERARELLelVGL-AGFEDayphQ-------LSGGMR 144
|
170 180
....*....|....*....|....*..
gi 1555720989 502 QRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDA 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
374-527 |
9.63e-20 |
|
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: 88.39 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAW-----RPLAGRIKLDGAALDQWSSERLG--RYIGYLPQDVELFA 446
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElrRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 GTVADNIARfdpGPDPQAIVAAARAAG-VHEL--IIGLPNgyETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:cd03260 95 GSIYDNVAY---GLRLHGIKLKEELDErVEEAlrKAALWD--EVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
....
gi 1555720989 524 SNLD 527
Cdd:cd03260 170 SALD 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
372-527 |
1.09e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 88.37 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS-SERLGRYIGYLPQDVELFAG-TV 449
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 450 ADNI-ARFDPGPDPQAIVAAARAAGVHELIIglpngyETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03218 93 EENIlAVLEIRGLSKKEREEKLEELLEEFHI------THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
375-584 |
1.29e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 88.17 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNI 453
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 A---RFDPGPdpQAIVAAARAAGVHELI-----IGLPNGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:cd03296 96 AfglRVKPRS--ERPPEAEIRAKVHELLklvqlDWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 526 LDAEGEMALAAAILAIKARGGILAI-VAH-RPNILSTVDFLLVMKEGQTQMFGTRESVLST 584
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDELHVTTVfVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
372-555 |
1.34e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGylPQDVELFAGTVAD 451
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NI---ARFDpGPDPQAIVAAARAAGVHeLIIGLPNGYetqigeggtaLSAGQRQRIALARAL-YGDPfLVVLDEPNSNLD 527
Cdd:PRK13539 93 NLefwAAFL-GGEELDIAAALEAVGLA-PLAHLPFGY----------LSAGQKRRVALARLLvSNRP-IWILDEPTAALD 159
|
170 180
....*....|....*....|....*...
gi 1555720989 528 AEGEMALAAAILAIKARGGILAIVAHRP 555
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
374-577 |
1.42e-19 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 89.15 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAaldqwsserlgryIGYLPQDVELFAGTVADNI 453
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ArFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD--AEGE 531
Cdd:cd03291 119 I-FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1555720989 532 MALAAAILAIKARGGILaiVAHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:cd03291 198 IFESCVCKLMANKTRIL--VTSKMEHLKKADKILILHEGSSYFYGT 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
369-592 |
1.59e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAG- 447
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIARFdpgPDPQAIVAAARAAGVHELI--IGLPNG-----YETQigeggtaLSAGQRQRIALARALYGDPFLVVLD 520
Cdd:cd03295 91 TVEENIALV---PKLLKWPKEKIRERADELLalVGLDPAefadrYPHE-------LSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 521 EPNSNLDA------EGEMALAAAILaikarGGILAIVAHRPN-ILSTVDFLLVMKEGQTQMFGTRESVLSTllPAPQTV 592
Cdd:cd03295 161 EPFGALDPitrdqlQEEFKRLQQEL-----GKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS--PANDFV 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
374-522 |
1.78e-19 |
|
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: 87.73 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE---RLGryIGYLPQDVELFAG-TV 449
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriaRLG--IGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 450 ADNI-----ARFDPGPDPQAIVAaaraagVHELiigLPNGYEtQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:COG0410 96 EENLllgayARRDRAEVRADLER------VYEL---FPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
374-577 |
1.86e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.05 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAaldqwsserlgryIGYLPQDVELFAGTVADNI 453
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ArFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD--AEGE 531
Cdd:TIGR01271 508 I-FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1555720989 532 MALAAAILAIKARGGILaiVAHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:TIGR01271 587 IFESCLCKLMSNKTRIL--VTSKLEHLKKADKILLLHEGVCYFYGT 630
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
371-571 |
2.00e-19 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 87.41 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLG----RYIGYLPQDVELFA 446
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 G-TVADNIA------RFDPGPDPQAIVAAARAAGVHELIIGLPngyetqigeggTALSAGQRQRIALARALYGDPFLVVL 519
Cdd:TIGR02211 97 DfTALENVAmplligKKSVKEAKERAYEMLEKVGLEHRINHRP-----------SELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 520 DEPNSNLDAEGEMALAAAILAIKARGGI-LAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
374-529 |
3.30e-19 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 86.53 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER---LGRYIGYLPQDVELF-AGTV 449
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlplLRRRIGVVFQDFRLLpDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIA-----RFDPGPDPQAIvaaaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:TIGR02673 97 YENVAlplevRGKKEREIQRR--------VGAALrqVGLEHKADAFPEQ----LSGGEQQRVAIARAIVNSPPLLLADEP 164
|
....*..
gi 1555720989 523 NSNLDAE 529
Cdd:TIGR02673 165 TGNLDPD 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
375-522 |
6.84e-19 |
|
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: 85.95 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY-IGYLPQDVELFAG-TVADN 452
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 453 IA-------RFDPGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:cd03219 96 VMvaaqartGSGLLLARARREEREARERAEELLerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
385-570 |
7.24e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 85.46 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 385 GSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS---SERLGRY-IGYLPQDVELFAGTVADNIArFDPGP 460
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeaTRSRNRYsVAYAAQKPWLLNATVEENIT-FGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 461 DPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE--GEMALAAAI 538
Cdd:cd03290 106 NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHLMQEGIL 185
|
170 180 190
....*....|....*....|....*....|..
gi 1555720989 539 LAIKARGGILAIVAHRPNILSTVDFLLVMKEG 570
Cdd:cd03290 186 KFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
45-342 |
9.41e-19 |
|
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: 86.83 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGR 124
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 125 VFTAVSRLPLYIGQQ---GDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAacgaLVLVTLTVA 201
Cdd:cd18779 81 FLEHLLRLPYRFFQQrstGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVV----LGLAALQVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 202 TEILTRRPMGAAVQSSVRRNSLAEA----SRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRL 277
Cdd:cd18779 157 LLLATRRRVRELMARELAAQAEAQSylveALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 278 MLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDlaiahwrNFVGARQSWSRLSKLLARL 342
Cdd:cd18779 237 AAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLA-------SLVGTAQQLQLLGSHLERL 294
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
45-315 |
1.35e-18 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 86.42 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGR 124
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 125 VFTAVSRLPL-YIGQQGDGLQPQR--DLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTVA 201
Cdd:cd18783 81 TFDRLLSLPIdFFERTPAGVLTKHmqQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 202 TEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGM-GRRLHDhWREASREHLALQQRVSDIVGGFGSFARALRLMLQ 280
Cdd:cd18783 161 FLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALePRQRRE-WDERVARAIRARFAVGRLSNWPQTLTGPLEKLMT 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1555720989 281 SAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPV 315
Cdd:cd18783 240 VGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPL 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
373-583 |
1.99e-18 |
|
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: 90.00 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 373 IIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADN 452
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IARFDPGPDpQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEM 532
Cdd:TIGR00957 1380 LDPFSQYSD-EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 533 ALAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTI-AHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
358-555 |
2.03e-18 |
|
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: 83.70 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERiaigapgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQ----WSSERLgr 433
Cdd:cd03231 6 LTCER-------DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrdsIARGLL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 434 YIGYLPQDVELFagTVADNIARFDPGPDPQAIVAAARAAGVheliiglpNGYETQIgegGTALSAGQRQRIALARALYGD 513
Cdd:cd03231 77 YLGHAPGIKTTL--SVLENLRFWHADHSDEQVEEALARVGL--------NGFEDRP---VAQLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1555720989 514 PFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRP 555
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
328-529 |
3.20e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 328 ARQSWSRLsKLLARLPQDAQP-------MALPVP---GSK-LTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGS 396
Cdd:COG0488 276 AKQAQSRI-KALEKLEREEPPrrdktveIRFPPPerlGKKvLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 397 GKSSLVRGLVGAWRPLAGRIKLdGAALDqwsserlgryIGYLPQDVELFAG--TVADNIARFDPGPDPQAivaaaraagv 474
Cdd:COG0488 353 GKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFDQHQEELDPdkTVLDELRDGAPGGTEQE---------- 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 475 helIIGL-------PNGYETQIGeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:COG0488 412 ---VRGYlgrflfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
375-529 |
6.81e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.13 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLG---RYIGYLPQDVELFAG-TVA 450
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLSSrTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIA---------------RfdpgpdpqaivaaaraagVHELI--IGLP---NGYETQigeggtaLSAGQRQRIALARAL 510
Cdd:COG1135 101 ENVAlpleiagvpkaeirkR------------------VAELLelVGLSdkaDAYPSQ-------LSGGQKQRVGIARAL 155
|
170
....*....|....*....
gi 1555720989 511 YGDPFLVVLDEPNSNLDAE 529
Cdd:COG1135 156 ANNPKVLLCDEATSALDPE 174
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
365-527 |
9.11e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 365 IGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVEL 444
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 445 FAGTVADNIA-----RFDpGPDPQAIVAAARAagvheliIGLPngyETQIGEGGTALSAGQRQRIALARALYGDPFLVVL 519
Cdd:PRK10247 93 FGDTVYDNLIfpwqiRNQ-QPDPAIFLDDLER-------FALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
....*...
gi 1555720989 520 DEPNSNLD 527
Cdd:PRK10247 162 DEITSALD 169
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
378-528 |
9.28e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 85.15 E-value: 9.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAldqWSSERLG-------RYIGYLPQDVELFAG-TV 449
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGiflpphrRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNI---ARFDPGPDPQAIVAaaraaGVHELIiglpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:COG4148 95 RGNLlygRKRAPRAERRISFD-----EVVELL-----GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
..
gi 1555720989 527 DA 528
Cdd:COG4148 165 DL 166
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
372-529 |
9.77e-18 |
|
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: 82.24 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGsVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGA-ALDQWSSERlgRYIGYLPQDVELFAGTVA 450
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLR--RRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 ----DNIARFDPGPDPQAIVAAAraaGVHELIiGLPNGYETQIGeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:cd03264 90 reflDYIAWLKGIPSKEVKARVD---EVLELV-NLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
...
gi 1555720989 527 DAE 529
Cdd:cd03264 162 DPE 164
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
378-585 |
1.31e-17 |
|
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: 84.78 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALdQWSSERL-----GRYIGYLPQDVELFAG-TVAD 451
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-FDSRKGIflppeKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NI----ARFDPGPDPQAIVAAARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:TIGR02142 95 NLrygmKRARPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 528 --AEGEMALAAAILAIKARGGILaIVAHRPN-ILSTVDFLLVMKEGQTQMFGTRESVLSTL 585
Cdd:TIGR02142 164 dpRKYEILPYLERLHAEFGIPIL-YVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
371-528 |
2.09e-17 |
|
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: 81.15 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TV 449
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIA------RFDPGPDPQAIVAAARAAGVHELIIGLPngyetqigeggTALSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:cd03301 90 YDNIAfglklrKVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
....*
gi 1555720989 524 SNLDA 528
Cdd:cd03301 159 SNLDA 163
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
374-529 |
2.26e-17 |
|
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: 81.04 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE--RLGRYIGYLPQDVELFAG-TVA 450
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARfdpGP-DPQAIVAAARAAGVHELI--IGLP---NGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:cd03262 95 ENITL---APiKVKGMSKAEAEERALELLekVGLAdkaDAYPAQ-------LSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
....*
gi 1555720989 525 NLDAE 529
Cdd:cd03262 165 ALDPE 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
372-597 |
4.27e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.60 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIkldgaaldqWSSerlgRYIGYLPQDVELFAGTVAD 451
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAE----RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIARFDPgPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGE 531
Cdd:PTZ00243 740 NILFFDE-EDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 532 MALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLSTLLPApqTVTAGLQ 597
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYA--TLAAELK 882
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
372-555 |
1.38e-16 |
|
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: 78.55 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGR--YIGYLPQ-DVELfagT 448
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilYLGHLPGlKPEL---S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIARFDPGPDPQAIVAAARAAGVheliiGLpNGYETQIGEggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDALAAV-----GL-TGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 1555720989 529 EGEMALAAAILAIKARGGILAIVAHRP 555
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
370-583 |
1.70e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.63 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLA-GRIKLDGAaldqwsserlgryIGYLPQDVELFAGT 448
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNI---ARFDPgpdPQAIVAAARAAGVHELIIgLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:PLN03130 695 VRDNIlfgSPFDP---ERYERAIDVTALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 526 LDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PLN03130 771 LDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-583 |
1.86e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.06 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 355 GSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY 434
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQ--DVELFAGTVADNIArFdpGPDPQAIVAAARAAGVHELIiglpngyeTQIGEGGTA------LSAGQRQRIAL 506
Cdd:PRK13635 83 VGMVFQnpDNQFVGATVQDDVA-F--GLENIGVPREEMVERVDQAL--------RQVGMEDFLnrephrLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 507 ARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAI-VAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
356-528 |
2.10e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 356 SKLTVERIAI--GAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgr 433
Cdd:COG4525 2 SMLTVRHVSVryPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 434 yiGYLPQDVELFAG-TVADNIA---RFdpgpdpQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALA 507
Cdd:COG4525 79 --GVVFQKDALLPWlNVLDNVAfglRL------RGVPKAERRARAEELLalVGLADFARRRIWQ----LSGGMRQRVGIA 146
|
170 180
....*....|....*....|.
gi 1555720989 508 RALYGDPFLVVLDEPNSNLDA 528
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDA 167
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
377-529 |
2.11e-16 |
|
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: 78.22 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER---LGRYIGYLPQDVELFAG-TVADN 452
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLPDrNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IA-----RFDPGPD-PQAIVAAARAAGVHELIIGLPNGyetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:cd03292 99 VAfalevTGVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
...
gi 1555720989 527 DAE 529
Cdd:cd03292 168 DPD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
355-527 |
3.47e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 82.65 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 355 GSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVgawRPLA--GRIKLDGAALDQWSSERLG 432
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL---RLLSteGEIQIDGVSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 433 RYIGYLPQDVELFAGTVADNIARFDPGPDpQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYG 512
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKNLDPYEQWSD-EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170
....*....|....*
gi 1555720989 513 DPFLVVLDEPNSNLD 527
Cdd:TIGR01271 1371 KAKILLLDEPSAHLD 1385
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
375-527 |
4.18e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.78 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyigyLPQDVEL-----FAG-- 447
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRMQMvfqdpYASln 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 ---TVADNIA------RFDPGPDPQAIvaaaraagVHELI--IGLP----NGYETQigeggtaLSAGQRQRIALARALYG 512
Cdd:COG4608 110 prmTVGDIIAeplrihGLASKAERRER--------VAELLelVGLRpehaDRYPHE-------FSGGQRQRIGIARALAL 174
|
170
....*....|....*
gi 1555720989 513 DPFLVVLDEPNSNLD 527
Cdd:COG4608 175 NPKLIVCDEPVSALD 189
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
358-527 |
4.91e-16 |
|
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: 77.99 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLG---RY 434
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQDVELFAG-TVADNI--------------ARFDPGPDPQAIVAAARAAGVHELiiglpngYETQIGEggtaLSAG 499
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVlsgrlgrrstwrslFGLFPKEEKQRALAALERVGLLDK-------AYQRADQ----LSGG 148
|
170 180
....*....|....*....|....*...
gi 1555720989 500 QRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
390-527 |
7.26e-16 |
|
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: 79.07 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 390 IIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNIA---RFDPGPDPQAI 465
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHmTVEENVAfglKMRKVPRAEIK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 466 VAAARAAGVheliiglpngyeTQIGEGG----TALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:TIGR01187 79 PRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
374-529 |
7.78e-16 |
|
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: 77.09 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL----GRYIGYLPQDVELFAG-T 448
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLPTlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIA---RFDPGPDPQAIVAAA-RAAGVHELIIGLPNGyetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:COG4181 107 ALENVMlplELAGRRDARARARALlERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTG 175
|
....*
gi 1555720989 525 NLDAE 529
Cdd:COG4181 176 NLDAA 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
380-527 |
8.16e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.10 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNIA-RFD 457
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLFPHlTVAQNIGlGLR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 458 PG-----PDPQAIVAAARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:COG3840 98 PGlkltaEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
374-583 |
1.14e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.94 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNI 453
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ARFDPGPDPQAIVAAARAAgVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAeGEMA 533
Cdd:PLN03130 1334 DPFNEHNDADLWESLERAH-LKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV-RTDA 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1555720989 534 LAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
358-531 |
1.86e-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: 74.11 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWrplagrikldgaaldQWSSERLGRYIG- 436
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW---------------PWGSGRIGMPEGe 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 437 ---YLPQDVELFAGTVADNIARfdpgpdPQaivaaaraagvheliiglpngyetqigegGTALSAGQRQRIALARALYGD 513
Cdd:cd03223 65 dllFLPQRPYLPLGTLREQLIY------PW-----------------------------DDVLSGGEQQRLAFARLLLHK 109
|
170
....*....|....*...
gi 1555720989 514 PFLVVLDEPNSNLDAEGE 531
Cdd:cd03223 110 PKFVFLDEATSALDEESE 127
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
375-591 |
1.89e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 76.80 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVE------LFAGT 448
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPNtslnprLNIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIARFDPGPDPQAIvaaaraagvHELII------GL-PNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:COG4167 109 ILEEPLRLNTDLTAEER---------EERIFatlrlvGLlPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 522 PNSNLDAEGEMALAAAILAIKARGGILAI-VAHRPNILSTV-DFLLVMKEGQTQMFGTRESVLStllpAPQT 591
Cdd:COG4167 176 ALAALDMSVRSQIINLMLELQEKLGISYIyVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFA----NPQH 243
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
375-528 |
1.89e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 77.79 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVR---GLVGAWRPLAGRIKLDGAALDQWSSERL----GRYIGYLPQD------ 441
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARailGLLPPPGITSGEILFDGEDLLKLSEKELrkirGREIQMIFQDpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 442 -VElfagTVADNIArfdpgpDPQAIVAAARAAGVHELII------GLPNGYET------QigeggtaLSAGQRQRIALAR 508
Cdd:COG0444 101 pVM----TVGDQIA------EPLRIHGGLSKAEARERAIellervGLPDPERRldryphE-------LSGGMRQRVMIAR 163
|
170 180
....*....|....*....|
gi 1555720989 509 ALYGDPFLVVLDEPNSNLDA 528
Cdd:COG0444 164 ALALEPKLLIADEPTTALDV 183
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
373-577 |
2.75e-15 |
|
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: 75.35 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 373 IIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVAD 451
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIArFdpGPDPQAIVAAARAAGVHELI--IGLpNGYETQIGEggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:cd03300 92 NIA-F--GLRLKKLPKAEIKERVAEALdlVQL-EGYANRKPS---QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1555720989 530 GEMALAAAILAIKARGGILAI-VAH-RPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVfVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
374-527 |
2.81e-15 |
|
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: 75.01 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgryIGYLPQDVELFAG-TVADN 452
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 ---IARFDpGPDPQAIVAAaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03269 91 lvyLAQLK-GLKKEEARRR-----IDEWLerLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
372-522 |
3.89e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG---AALDQWSSERLGryIGYLPQDVELFAG- 447
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTHLPMHKRARLG--IGYLPQEASIFRKl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIArfdpgpdpqaivaaaraaGVHELiIGLPNGYETQIGEG--------------GTALSAGQRQRIALARALYGD 513
Cdd:COG1137 94 TVEDNIL------------------AVLEL-RKLSKKEREERLEElleefgithlrkskAYSLSGGERRRVEIARALATN 154
|
....*....
gi 1555720989 514 PFLVVLDEP 522
Cdd:COG1137 155 PKFILLDEP 163
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
375-522 |
3.90e-15 |
|
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: 75.46 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY-IGYLPQDVELFAG-TVADN 452
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 I-----ARFDPGPDPQAIVAAARAAGVHEL---------IIGLpngyETQIGEGGTALSAGQRQRIALARALYGDPFLVV 518
Cdd:COG0411 100 VlvaahARLGRGLLAALLRLPRARREEREAreraeelleRVGL----ADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
....
gi 1555720989 519 LDEP 522
Cdd:COG0411 176 LDEP 179
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
371-572 |
6.27e-15 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 73.79 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAlDQWSSERLGRyIGYLPQDVELFAG-TV 449
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRR-IGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIarfdpgpdpqaivaaaraaGVHELIIGLPNGYETQI----GEGGTA------LSAGQRQRIALARALYGDPFLVVL 519
Cdd:cd03268 90 RENL-------------------RLLARLLGIRKKRIDEVldvvGLKDSAkkkvkgFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 520 DEPNSNLDAEGEMALAAAILAIKARGGILAIVAHrpnILS----TVDFLLVMKEGQT 572
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSH---LLSeiqkVADRIGIINKGKL 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
358-530 |
9.49e-15 |
|
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: 71.71 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAldqwsserlgrYIGY 437
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQdvelfagtvadniarfdpgpdpqaivaaaraagvheliiglpngyetqigeggtaLSAGQRQRIALARALYGDPFLV 517
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170
....*....|...
gi 1555720989 518 VLDEPNSNLDAEG 530
Cdd:cd03221 93 LLDEPTNHLDLES 105
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
377-531 |
1.02e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.87 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE--RLGRYIGYLPQDVELFAG-TVADNI 453
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGMVFQQFNLFPHlTVLENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ARfdpGPdpqaivaaARAAGV---------HELI--IGLP---NGYETQigeggtaLSAGQRQRIALARALYGDPFLVVL 519
Cdd:COG1126 99 TL---AP--------IKVKKMskaeaeeraMELLerVGLAdkaDAYPAQ-------LSGGQQQRVAIARALAMEPKVMLF 160
|
170
....*....|....
gi 1555720989 520 DEPNSNLDAE--GE 531
Cdd:COG1126 161 DEPTSALDPElvGE 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
372-530 |
1.07e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAldqwsseRlgryIGYLPQDVELFAG-TVA 450
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------R----IGYLPQEPPLDDDlTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNI-----------ARF--------DPGPDPQAIVAAARAAG----------VHELIIGL---PNGYETQIGEggtaLSA 498
Cdd:COG0488 80 DTVldgdaelraleAELeeleaklaEPDEDLERLAELQEEFEalggweaearAEEILSGLgfpEEDLDRPVSE----LSG 155
|
170 180 190
....*....|....*....|....*....|..
gi 1555720989 499 GQRQRIALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
374-527 |
1.31e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVEL-FAGTVADN 452
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 I--------ARFDPGPDPQAIVAAARAAGVheliiglpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:PRK09536 98 VemgrtphrSRFDTWTETDRAAVERAMERT---------GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
...
gi 1555720989 525 NLD 527
Cdd:PRK09536 169 SLD 171
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
180-577 |
1.61e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 180 LHPTLGTTAACGALVLVTLTVATEILT---RRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLA 256
Cdd:PLN03232 435 LYQQLGVASLFGSLILFLLIPLQTLIVrkmRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELS 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 257 LQqRVSDIVGGFGSFaralrlMLQS-----AMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQS 331
Cdd:PLN03232 515 WF-RKAQLLSAFNSF------ILNSipvvvTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVS 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 332 WSRLSKLLarlpqdaqpmalpvpgskLTVERIAIG----APGAQRIIVQGVEFSLDA----------------GSVLGII 391
Cdd:PLN03232 588 LQRIEELL------------------LSEERILAQnpplQPGAPAISIKNGYFSWDSktskptlsdinleipvGSLVAIV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 392 GPSGSGKSSLVRGLVGAWRPLagrikldgaaldQWSSERLGRYIGYLPQDVELFAGTVADNIArFDPGPDPQAIVAAARA 471
Cdd:PLN03232 650 GGTGEGKTSLISAMLGELSHA------------ETSSVVIRGSVAYVPQVSWIFNATVRENIL-FGSDFESERYWRAIDV 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 472 AGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIV 551
Cdd:PLN03232 717 TALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLV 796
|
410 420
....*....|....*....|....*.
gi 1555720989 552 AHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:PLN03232 797 TNQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
372-562 |
1.63e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGaaldqwsserlGRYIGYLPQDVEL---FAGT 448
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIA--RFDP-GP-------DPQAIVAAARAAGVHELIiglpngyETQIGEggtaLSAGQRQRIALARALYGDPFLVV 518
Cdd:NF040873 74 VRDLVAmgRWARrGLwrrltrdDRAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1555720989 519 LDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVD 562
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRAD 186
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
380-527 |
2.53e-14 |
|
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: 72.58 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAaldqwSSERLGRYIGYLPQDVEL-------FAGTVADN 452
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRHEFawdfpisVAHTVMSG 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 453 IARFdPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:TIGR03771 76 RTGH-IGWLRRPCVADFAAVRDALRRVGLTELADRPVGE----LSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
377-528 |
3.12e-14 |
|
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: 70.54 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS---SERLGryIGYLPQdvelfagtvadni 453
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASprdARRAG--IAMVYQ------------- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 454 arfdpgpdpqaivaaaraagvheliiglpngyetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
371-527 |
3.15e-14 |
|
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: 73.06 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL----GRYIGYLPQDVELFA 446
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 G-TVADNIARfdpGPDPQAIVAAARAAGVHELI--IGLpNGYETQ-IGEggtaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:cd03294 116 HrTVLENVAF---GLEVQGVPRAEREERAAEALelVGL-EGWEHKyPDE----LSGGMQQRVGLARALAVDPDILLMDEA 187
|
....*
gi 1555720989 523 NSNLD 527
Cdd:cd03294 188 FSALD 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
375-589 |
3.17e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQ--DVELFAGTVADN 452
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IARfdpGPDPQAIVAAARAAGVHELIIGLpNGYETQIGEGGTaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEG-- 530
Cdd:PRK13642 103 VAF---GMENQGIPREEMIKRVDEALLAV-NMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGrq 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 531 EMALAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQ-------TQMFGTRESVLSTLLPAP 589
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSI-THDLDEAASSDRILVMKAGEiikeaapSELFATSEDMVEIGLDVP 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
366-529 |
3.20e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.07 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 366 GAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLG---RYIGYLPQDV 442
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 443 ELFAG-TVADNIA---RFDPGPDPQAIVAaaraagVHEL--IIGLP---NGYETQigeggtaLSAGQRQRIALARALYGD 513
Cdd:PRK11153 92 NLLSSrTVFDNVAlplELAGTPKAEIKAR------VTELleLVGLSdkaDRYPAQ-------LSGGQKQRVAIARALASN 158
|
170
....*....|....*.
gi 1555720989 514 PFLVVLDEPNSNLDAE 529
Cdd:PRK11153 159 PKVLLCDEATSALDPA 174
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
374-527 |
3.23e-14 |
|
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: 73.35 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVgawRPLA--GRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVAD 451
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL---RLLNteGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 452 NIARFDPGPDpQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03289 96 NLDPYGKWSD-EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
358-522 |
3.91e-14 |
|
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: 70.92 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPgaqriiVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS-SERLGRYIG 436
Cdd:cd03215 5 LEVRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 437 YLPQD---VELFAG-TVADNIArfdpgpdpqaivaaaraagvheliigLPNGyetqigeggtaLSAGQRQRIALARALYG 512
Cdd:cd03215 79 YVPEDrkrEGLVLDlSVAENIA--------------------------LSSL-----------LSGGNQQKVVLARWLAR 121
|
170
....*....|
gi 1555720989 513 DPFLVVLDEP 522
Cdd:cd03215 122 DPRVLILDEP 131
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
374-528 |
4.37e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.95 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELF-AGTVADN 452
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQSYALYpHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IA-----RFDPGPDPQAIvaaaraagVHEL--IIGL-------PngyetqigeggTALSAGQRQRIALARALYGDPFLVV 518
Cdd:COG3839 96 IAfplklRKVPKAEIDRR--------VREAaeLLGLedlldrkP-----------KQLSGGQRQRVALGRALVREPKVFL 156
|
170
....*....|
gi 1555720989 519 LDEPNSNLDA 528
Cdd:COG3839 157 LDEPLSNLDA 166
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
55-335 |
4.78e-14 |
|
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: 72.98 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 55 SGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVSRLPL 134
Cdd:cd18568 11 SLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 135 YI---GQQGDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTVATEILTRRPMG 211
Cdd:cd18568 91 SFfasRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 212 AAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAMLGVGAWLV 291
Cdd:cd18568 171 EIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1555720989 292 IEGEATSGIIIAGSILVGRALAPVDLAIAHWRNFVGARQSWSRL 335
Cdd:cd18568 251 ISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
355-583 |
4.89e-14 |
|
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: 72.25 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 355 GSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRY 434
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQDVELFAGTVadniaRFDPGPDPQ----AIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARAL 510
Cdd:cd03288 97 LSIILQDPILFSGSI-----RFNLDPECKctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 511 YGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI-AHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
358-527 |
5.88e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS-SERLGRYIG 436
Cdd:PRK10895 4 LTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 437 YLPQDVELFAG-TVADNIA-----RFDPGPDPQAIVAAARAAGVHelIIGLPNGYetqigegGTALSAGQRQRIALARAL 510
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMavlqiRDDLSAEQREDRANELMEEFH--IEHLRDSM-------GQSLSGGERRRVEIARAL 152
|
170
....*....|....*..
gi 1555720989 511 YGDPFLVVLDEPNSNLD 527
Cdd:PRK10895 153 AANPKFILLDEPFAGVD 169
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
374-529 |
7.77e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.70 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALD--------QWSSERLGRYIGYLPQDVELF 445
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqqKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 AG-TVADNIARfdpGP-----DPQAIVAAARaagvHELI--IGLpNGYETQIGEggtALSAGQRQRIALARALYGDPFLV 517
Cdd:PRK11264 98 PHrTVLENIIE---GPvivkgEPKEEATARA----RELLakVGL-AGKETSYPR---RLSGGQQQRVAIARALAMRPEVI 166
|
170
....*....|..
gi 1555720989 518 VLDEPNSNLDAE 529
Cdd:PRK11264 167 LFDEPTSALDPE 178
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
356-530 |
7.78e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 356 SKLTVERiaigapgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAL----DQWSSERL 431
Cdd:PRK13538 5 RNLACER-------DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrDEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 432 grYIGYLPQ-DVELfagTVADNIARFDPGPDPQAIVAAARAAGvheliiglpngyetQIGEGGTA------LSAGQRQRI 504
Cdd:PRK13538 78 --YLGHQPGiKTEL---TALENLRFYQRLHGPGDDEALWEALA--------------QVGLAGFEdvpvrqLSAGQQRRV 138
|
170 180
....*....|....*....|....*.
gi 1555720989 505 ALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:PRK13538 139 ALARLWLTRAPLWILDEPFTAIDKQG 164
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
375-527 |
9.72e-14 |
|
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: 73.95 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAwRPLAGRIKLDGAALDQWSSERLGRyigyLPQDVEL-----FAG-- 447
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRP----LRRRMQVvfqdpFGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 ---TVADNIAR----FDPGPDPQAivaaaraagVHELII------GLP----NGYETQigeggtaLSAGQRQRIALARAL 510
Cdd:COG4172 377 prmTVGQIIAEglrvHGPGLSAAE---------RRARVAealeevGLDpaarHRYPHE-------FSGGQRQRIAIARAL 440
|
170
....*....|....*..
gi 1555720989 511 YGDPFLVVLDEPNSNLD 527
Cdd:COG4172 441 ILEPKLLVLDEPTSALD 457
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
358-528 |
9.80e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgryiGY 437
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVELFA-GTVADNIARfdpGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDP 514
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVAF---GLQLAGVEKMQRLEIAHQMLkkVGLEGAEKRYIWQ----LSGGQRQRVGIARALAANP 147
|
170
....*....|....
gi 1555720989 515 FLVVLDEPNSNLDA 528
Cdd:PRK11248 148 QLLLLDEPFGALDA 161
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
369-576 |
1.06e-13 |
|
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: 69.89 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLA--GRIKLDGAALDQwssERLGRYIGYLPQDVELFA 446
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDK---RSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 G-TVADNIArfdpgpdpqaivaaaraagVHELIIGlpngyetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:cd03213 96 TlTVRETLM-------------------FAAKLRG---------------LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 526 LDAEGEMALAAAILAIKARGGILAIVAHRP--NILSTVDFLLVMKEGQTQMFG 576
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
379-529 |
1.23e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 379 EFSLD--AGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNIAr 455
Cdd:PRK10851 20 DISLDipSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDNIA- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 456 FdpG----PDPQAIVAAARAAGVHEL--IIGLP---NGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:PRK10851 97 F--GltvlPRRERPNAAAIKAKVTQLleMVQLAhlaDRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
...
gi 1555720989 527 DAE 529
Cdd:PRK10851 168 DAQ 170
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
375-527 |
1.24e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNI 453
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1555720989 454 ARfdpGPDPQAIVAAARAAGVHELIiGLPNGYETQiGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK11607 113 AF---GLKQDKLPKAEIASRVNEML-GLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
252-531 |
1.35e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 252 REHLALQQRVSDIVGGFGSFARA-LRLML------QSAM---LGVGAWLVIEGEATSGIIIAGSILVGR---ALA-PVD- 316
Cdd:COG4178 242 AERRRLRRRFDAVIANWRRLIRRqRNLTFfttgygQLAVifpILVAAPRYFAGEITLGGLMQAASAFGQvqgALSwFVDn 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 317 -LAIAHWRNFVgarqswSRLSKLLARL-----PQDAQPMALPVPGSKLTVERIAIGAPgAQRIIVQGVEFSLDAGSVLGI 390
Cdd:COG4178 322 yQSLAEWRATV------DRLAGFEEALeaadaLPEAASRIETSEDGALALEDLTLRTP-DGRPLLEDLSLSLKPGERLLI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 391 IGPSGSGKSSLVRGLVGAWRPLAGRIKL--DGAALdqwsserlgryigYLPQDVELFAGTVADNIARfdPGPDPQAIVaa 468
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVL-------------FLPQRPYLPLGTLREALLY--PATAEAFSD-- 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 469 araagvHELI-----IGLPNgYETQIGEG---GTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGE 531
Cdd:COG4178 458 ------AELRealeaVGLGH-LAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
48-315 |
1.48e-13 |
|
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: 71.43 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 48 FAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFT 127
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 128 AVSRLPL-YIGQQGDG-----LQpqRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLgttaACGALVLVTLTVA 201
Cdd:cd07346 81 HLQRLSLsFFDRNRTGdlmsrLT--SDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKL----TLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 202 TEILTRRPMGAAvqSSVRRNSLAEASRRNAEVL------QAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARAL 275
Cdd:cd07346 155 ILRYFRRRIRKA--SREVRESLAELSAFLQESLsgirvvKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1555720989 276 RLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPV 315
Cdd:cd07346 233 TALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPI 272
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
360-532 |
1.48e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 360 VERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLP 439
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 440 Q--DVELFAGTVADNIA------RFDPGPDPQAIVAAARAAGVHELIiglpnGYETQigeggtALSAGQRQRIALARALY 511
Cdd:PRK13632 90 QnpDNQFIGATVEDDIAfglenkKVPPKKMKDIIDDLAKKVGMEDYL-----DKEPQ------NLSGGQKQRVAIASVLA 158
|
170 180
....*....|....*....|.
gi 1555720989 512 GDPFLVVLDEPNSNLDAEGEM 532
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKR 179
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
368-570 |
1.52e-13 |
|
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: 70.38 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 368 PGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSL---VRGLVGAWRPLAGRIKLDGAAL--DQWSSErlgryIGYLPQDV 442
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRkpDQFQKC-----VAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 443 ELFAG-TVADNIA--------RFDPGPDPQAIVAAARAAGVHELIIGlpngyetqiGEGGTALSAGQRQRIALARALYGD 513
Cdd:cd03234 91 ILLPGlTVRETLTytailrlpRKSSDAIRKKRVEDVLLRDLALTRIG---------GNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 514 PFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAH--RPNILSTVDFLLVMKEG 570
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSG 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
374-573 |
1.53e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSS----ERLGRYIGYLPQDVELFAG-T 448
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIAR--FDPGPDPQAIVAAAraagvHELIIGLpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:PRK11629 104 ALENVAMplLIGKKKPAEINSRA-----LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 527 DAE---------GEMalaaailaIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQ 573
Cdd:PRK11629 177 DARnadsifqllGEL--------NRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
322-527 |
2.30e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.79 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 322 WRNFVGARQSWSRLSKLLARLPQDAQPMALPVPGSKLTVeriaigapgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSL 401
Cdd:PRK13536 13 RLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSY---------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 402 VRGLVGAWRPLAGRIKLDGAALDqwSSERLGRY-IGYLPQ----DVELfagTVADNIARFDPGPDPQAIVAAARAAGVHE 476
Cdd:PRK13536 84 ARMILGMTSPDAGKITVLGVPVP--ARARLARArIGVVPQfdnlDLEF---TVRENLLVFGRYFGMSTREIEAVIPSLLE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 477 LiIGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK13536 159 F-ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
371-532 |
2.31e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGaaldqwsserlGRYIGYLPQDVELFAgTVA 450
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQKLYLDT-TLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARFdpgpdpqaivaAARAAGVHELIIgLPNGYETQIGEGGTA----LSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:PRK09544 84 LTVNRF-----------LRLRPGTKKEDI-LPALKRVQAGHLIDApmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
....*.
gi 1555720989 527 DAEGEM 532
Cdd:PRK09544 152 DVNGQV 157
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
376-583 |
2.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 376 QGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAL--DQWSSERLGRYIGYLPQ--DVELFAGTVAD 451
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQnpDDQLFAPTVEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIArFDPgpdpqaivaaaraagvheLIIGLP-----------------NGYETQIGEggtALSAGQRQRIALARALYGDP 514
Cdd:PRK13639 99 DVA-FGP------------------LNLGLSkeevekrvkealkavgmEGFENKPPH---HLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 515 FLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILST-VDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
375-598 |
2.84e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSS-ERLGRYIGYLPQDVEL-FAG-TVAD 451
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETqFVGrTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIARfdpGPD----PQAIVAAARAAGVHELiiglpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK13644 98 DLAF---GPEnlclPPIEIRKRVDRALAEI------GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 528 AEGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLSTllpaPQTVTAGLQP 598
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD----VSLQTLGLTP 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
374-583 |
3.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.53 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQ--DVELFAGTVAD 451
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQnpDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIArFdpGPDPQAIVAAARAAGVHEL--IIGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:PRK13650 102 DVA-F--GLENKGIPHEEMKERVNEAleLVGMQDFKEREPAR----LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 530 GEMALAAAILAIKARGGILAI-VAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
379-527 |
3.96e-13 |
|
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: 68.73 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 379 EFSL--DAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAalDQWSSERLGRYIGYLPQDVELFAG-TVADNIAR 455
Cdd:TIGR01277 16 EFDLnvADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHlTVRQNIGL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 456 -FDPG-----PDPQAIVAAARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:TIGR01277 94 gLHPGlklnaEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
413-583 |
3.99e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 413 AGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADNIARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEG 492
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPY 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 493 GTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAI-VAHRPNILSTVDFLLVM---- 567
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIItIAHRIASIKRSDKIVVFnnpd 1435
|
170
....*....|....*..
gi 1555720989 568 KEGQ-TQMFGTRESVLS 583
Cdd:PTZ00265 1436 RTGSfVQAHGTHEELLS 1452
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
384-527 |
5.61e-13 |
|
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: 68.29 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 384 AGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGaaLDQWSSERLGRYIGYLPQDVELFAG-TVADNIA-RFDPG-- 459
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQENNLFAHlTVEQNVGlGLSPGlk 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 460 ---PDPQAIVAAARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03298 101 ltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
376-529 |
6.50e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 376 QGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS---SERLGryIGYLPQDVELFAG-TVAD 451
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAAG--IAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NI-------------------------ARFDPGPDPqaivaaaraagvheliiglpngyETQIGEggtaLSAGQRQRIAL 506
Cdd:COG1129 99 NIflgreprrgglidwramrrrarellARLGLDIDP-----------------------DTPVGD----LSVAQQQLVEI 151
|
170 180
....*....|....*....|...
gi 1555720989 507 ARALYGDPFLVVLDEPNSNLDAE 529
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTER 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
375-527 |
1.01e-12 |
|
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: 67.78 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyIGYLPQDVELFAG-TVADNI 453
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 454 ARFDP--GPDPQAIVAAaraagVHELIIGLpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:cd03266 100 EYFAGlyGLKGDELTAR-----LEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
46-521 |
1.13e-12 |
|
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: 70.60 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 46 AAFAGVAvfSGVSNILMLT----GAMFMLEVYDRVLPSRSVPTLIAMAILAGALFA----GQAVIDLVRGRIMNRI-GAE 116
Cdd:COG4615 18 ALLLGLL--SGLANAGLIAlinqALNATGAALARLLLLFAGLLVLLLLSRLASQLLltrlGQHAVARLRLRLSRRIlAAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 117 LD--EAVGG-RVFTAVSRlplyigqqgdglqpqrDLDNIrTFLSSAGPGTLFDLPWLPF---YLAiiwslhpTLGTTAAC 190
Cdd:COG4615 96 LErlERIGAaRLLAALTE----------------DVRTI-SQAFVRLPELLQSVALVLGclaYLA-------WLSPPLFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 191 GALVLVTLTVAT-EILTRRPMGAAVQSSVRRNSLAEAsrrnaevLQAMGMGR---RLHDHWREASREHlALQQRVSDI-- 264
Cdd:COG4615 152 LTLVLLGLGVAGyRLLVRRARRHLRRAREAEDRLFKH-------FRALLEGFkelKLNRRRRRAFFDE-DLQPTAERYrd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 265 --VGGFGSFARALRL--MLQSAMLGV-----GAWLVIEGEATSGIIIAGSILVGralaPVDLAIAHWRNFVGARQSWSRL 335
Cdd:COG4615 224 lrIRADTIFALANNWgnLLFFALIGLilfllPALGWADPAVLSGFVLVLLFLRG----PLSQLVGALPTLSRANVALRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 336 SKLLARLPQDAQPMALPVPgskltveriAIGAPGAQRIIVQGVEF------------------SLDAGSVLGIIGPSGSG 397
Cdd:COG4615 300 EELELALAAAEPAAADAAA---------PPAPADFQTLELRGVTYrypgedgdegftlgpidlTIRRGELVFIVGGNGSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 398 KSSLVRGLVGAWRPLAGRIKLDGAALDqwsSERLGRY---IGYLPQDVELFagtvaDNIARFDPGPDPQAivaaaraagV 474
Cdd:COG4615 371 KSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYrqlFSAVFSDFHLF-----DRLLGLDGEADPAR---------A 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 475 HELIIGLPNGYETQIGEGG---TALSAGQRQRIALARALYGD-PFLvVLDE 521
Cdd:COG4615 434 RELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDrPIL-VFDE 483
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
374-529 |
1.28e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG-AALDQWSSERLGRY-IGYLPQDVELFAG-TVA 450
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQeAGMVFQQFYLFPHlTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIArFDP----GPDPQAIVAAAraagvHELI--IGLP---NGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:PRK09493 96 ENVM-FGPlrvrGASKEEAEKQA-----RELLakVGLAeraHHYPSE-------LSGGQQQRVAIARALAVKPKLMLFDE 162
|
....*...
gi 1555720989 522 PNSNLDAE 529
Cdd:PRK09493 163 PTSALDPE 170
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
371-527 |
1.97e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.29 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyIGYLPQDVELFAG-TV 449
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFDNLDPDfTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 450 ADNIARFDPGPDPQAIVAAARAAGVHELIiGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAARALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
374-563 |
2.61e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRI------KLDGAALDQWSSErlgryIGYLPQDVELFAG 447
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWRSK-----IGVVSQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNI---------------------------------ARFDPGPDPQAIVAAARAAG--------------------- 473
Cdd:PTZ00265 475 SIKNNIkyslyslkdlealsnyynedgndsqenknkrnsCRAKCAGDLNDMSNTTDSNEliemrknyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 474 ---VHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGE-MALAAAILAIKARGGILA 549
Cdd:PTZ00265 555 kvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEyLVQKTINNLKGNENRITI 634
|
250
....*....|....
gi 1555720989 550 IVAHRpniLSTVDF 563
Cdd:PTZ00265 635 IIAHR---LSTIRY 645
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
377-579 |
2.67e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDV--ELFAGTVADNIA 454
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 455 rFdpGPDPQAIVAAARAAGVHELIIGLpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMAL 534
Cdd:PRK13647 103 -F--GPVNMGLDKDEVERRVEEALKAV--RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1555720989 535 AAAILAIKARGGILAIVAHRPNI-LSTVDFLLVMKEGQTQMFGTRE 579
Cdd:PRK13647 178 MEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
378-590 |
2.77e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGaaLDQWSSE----RLGRYIGYLPQ--DVELFAGTVAD 451
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKvklsDIRKKVGLVFQypEYQLFEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIArFdpGPDPQAIVAAARAAGVHEL--IIGLPngYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:PRK13637 104 DIA-F--GPINLGLSEEEIENRVKRAmnIVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 530 GemalaaailaikaRGGILA--------------IVAHR-PNILSTVDFLLVMKEGQTQMFGTRESV---LSTL----LP 587
Cdd:PRK13637 179 G-------------RDEILNkikelhkeynmtiiLVSHSmEDVAKLADRIIVMNKGKCELQGTPREVfkeVETLesigLA 245
|
...
gi 1555720989 588 APQ 590
Cdd:PRK13637 246 VPQ 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
352-527 |
3.44e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 352 PVPGSKLTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL 431
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 432 GRYIGYLPQDVELFAG-TVADNIA-----------RFDpGPDPQAIVAAARAAGVHELIIGLPNgyetqigeggtALSAG 499
Cdd:PRK10575 84 ARKVAYLPQQLPAAEGmTVRELVAigrypwhgalgRFG-AADREKVEEAISLVGLKPLAHRLVD-----------SLSGG 151
|
170 180
....*....|....*....|....*...
gi 1555720989 500 QRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
373-584 |
4.08e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 373 IIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVADN 452
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IARFDPGpDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALY--GDPFlVVLDEPNSNLDAEG 530
Cdd:PTZ00243 1404 VDPFLEA-SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkkGSGF-ILMDEATANIDPAL 1481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 531 EMALAAAILAIKARGGILAIvAHRPNILSTVDFLLVMKEGQ-TQMFGTRESVLST 584
Cdd:PTZ00243 1482 DRQIQATVMSAFSAYTVITI-AHRLHTVAQYDKIIVMDHGAvAEMGSPRELVMNR 1535
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
375-526 |
4.09e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGR-YIGYLPQDVELFAG-TVADN 452
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1555720989 453 IARFDPGPDPQAIVAAARAagVHELiigLPNGYETQIGEGGTaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:PRK11614 101 LAMGGFFAERDQFQERIKW--VYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
379-529 |
4.71e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.28 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 379 EFSLDA-------GSVLGIIGPSGSGKSSLVRglvgawrPLAGRIKLDGAaldqwSSERLGRYIGYLPQDVEL-FAGTVA 450
Cdd:cd03237 12 EFTLEVeggsiseSEVIGILGPNGIGKTTFIK-------MLAGVLKPDEG-----DIEIELDTVSYKPQYIKAdYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARFDP--GPDPQAIVAAARAAGVHELiiglpngYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:cd03237 80 DLLSSITKdfYTHPYFKTEIAKPLQIEQI-------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
.
gi 1555720989 529 E 529
Cdd:cd03237 149 E 149
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
380-527 |
5.78e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAalDQWSSERLGRYIGYLPQDVELFAG-TVADNIAR-FD 457
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLgLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 458 PG-----PDPQAIVAAARAAGVHELIIGLPngyetqigeggTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK10771 98 PGlklnaAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-584 |
6.22e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLvGAWRPLAGRIKLDGAA--LDQWSSER------LGRYIGYLPQDVELF 445
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVefFNQNIYERrvnlnrLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 AGTVADNIARFDP--GPDPQAIVAAARAAGVHEliIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:PRK14258 101 PMSVYDNVAYGVKivGWRPKLEIDDIVESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 524 SNLDAEGEMALAAAILAIKARGGI-LAIVAHR-PNILSTVDFLLVMKEGQ---TQM--FGTRESVLST 584
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELtMVIVSHNlHQVSRLSDFTAFFKGNEnriGQLveFGLTKKIFNS 246
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
45-303 |
8.15e-12 |
|
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: 66.33 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGR 124
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 125 VFTAVSRLPL------YIGqqgdglqpqrD-------LDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACG 191
Cdd:cd18567 81 LFRHLLRLPLsyfekrHLG----------DivsrfgsLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 192 ALVLVTLTVATEILTRRPMGAAVQSSVRRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSF 271
Cdd:cd18567 151 VALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAA 230
|
250 260 270
....*....|....*....|....*....|..
gi 1555720989 272 ARALRLMLQSAMLGVGAWLVIEGEATSGIIIA 303
Cdd:cd18567 231 NGLLFGLENILVIYLGALLVLDGEFTVGMLFA 262
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
371-604 |
8.43e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLvgawrplAGRIK---LDGAAL--DQWSSERLGRYIGYLPQDVELF 445
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILanNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 AG-TVADNIARFDPGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEGGT-ALSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:PLN03211 153 PHlTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 522 PNSNLDAEGEMALAAAILAIKARGGILAIVAHRPN--ILSTVDFLLVMKEGQTQMFGTRESVLSTLlpapqtVTAGLQPV 599
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSsrVYQMFDSVLVLSEGRCLFFGKGSDAMAYF------ESVGFSPS 306
|
....*
gi 1555720989 600 FKLTP 604
Cdd:PLN03211 307 FPMNP 311
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
376-526 |
8.96e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 376 QGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE---RLGryIGYLPQDVELFAG-TVAD 451
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALG--IGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NIARFDPGPDPQAIVAAARAAGVHELI--IGL---PNGYetqIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAARARIRELSerYGLdvdPDAK---VED----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
375-527 |
9.09e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAwRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVE-LFAGTVADNI 453
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ARFDPGPDPQAIVAAARAAGVHELiiGLPNGYETQIgeggTALSAGQRQRIALARALY-------GDPFLVVLDEPNSNL 526
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSL 164
|
.
gi 1555720989 527 D 527
Cdd:COG4138 165 D 165
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
375-522 |
1.12e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS-SERLGRYIGYLPQD--VE-LFAG-TV 449
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkGEgLVLDlSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNI-----ARFDPGP--DPQAIVAAaraagVHELIIGL---PNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVL 519
Cdd:COG1129 348 RENItlaslDRLSRGGllDRRRERAL-----AEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLIL 418
|
...
gi 1555720989 520 DEP 522
Cdd:COG1129 419 DEP 421
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
375-583 |
1.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.59 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQ--DVELFAGTVADN 452
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IArFDP---GPDPQAIV----AAARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:PRK13652 100 IA-FGPinlGLDEETVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 526 LDAEGEMALAAAILAIKARGGILAIVA--HRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSthQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
356-527 |
1.32e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 356 SKLTVERIAIGApgAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYI 435
Cdd:PRK10253 6 ARLRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 436 GYLPQDVELFAG-TVADNIA--RFDPGP--------DPQAIVAAARAAGVHELiiglpngyetqIGEGGTALSAGQRQRI 504
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVArgRYPHQPlftrwrkeDEEAVTKAMQATGITHL-----------ADQSVDTLSGGQRQRA 152
|
170 180
....*....|....*....|...
gi 1555720989 505 ALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLD 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
374-528 |
1.44e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADN 452
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IARfdpGPDPQAIVAAARAAGVHELI-----IGLPNGYETQIgeggtalSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK11432 99 VGY---GLKMLGVPKEERKQRVKEALelvdlAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
.
gi 1555720989 528 A 528
Cdd:PRK11432 169 A 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
359-527 |
1.65e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 359 TVERIAIGApgaqriiVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAalDQW---------SSE 429
Cdd:TIGR03269 291 SVDRGVVKA-------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVG--DEWvdmtkpgpdGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 430 RLGRYIGYLPQDVELFA-GTVADNIARFDPGPDPQAIVAAAraaGVHEL-IIGLPNGYETQIGEGGT-ALSAGQRQRIAL 506
Cdd:TIGR03269 362 RAKRYIGILHQEYDLYPhRTVLDNLTEAIGLELPDELARMK---AVITLkMVGFDEEKAEEILDKYPdELSEGERHRVAL 438
|
170 180
....*....|....*....|.
gi 1555720989 507 ARALYGDPFLVVLDEPNSNLD 527
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMD 459
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
372-527 |
1.96e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.13 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgryIGYLPQDVELFAG-TVA 450
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IGYLPEERGLYPKmKVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARF------DPGPDPQAivaaaraagVHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:COG4152 90 EQLVYLarlkglSKAEAKRR---------ADEWLerLGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEP 156
|
....*
gi 1555720989 523 NSNLD 527
Cdd:COG4152 157 FSGLD 161
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
378-530 |
2.08e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLP---QDVelfagTVADNIA 454
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPglkADL-----STLENLH 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 455 RFDP--GPDPQAIVAAARAagvhelIIGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:PRK13543 105 FLCGlhGRRAKQMPGSALA------IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
374-577 |
2.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.26 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLD----GAALDQWSS------------ERLGRYIGY 437
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELitnpyskkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQ--DVELFAGTVADNIArFDPGPDPQAIVAAARAAGVHELIIGLPNGYetqIGEGGTALSAGQRQRIALARALYGDPF 515
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIM-FGPVALGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 516 LVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHR-PNILSTVDFLLVMKEGQTQMFGT 577
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILKTGT 259
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-527 |
2.28e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVelFAGT-- 448
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDP--MMGTap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 ---VADNIA---------RFDPGPDPQAIVAaaraagVHELI----IGLPNGYETQIGeggtALSAGQRQRIALARALYG 512
Cdd:COG1101 96 smtIEENLAlayrrgkrrGLRRGLTKKRREL------FRELLatlgLGLENRLDTKVG----LLSGGQRQALSLLMATLT 165
|
170
....*....|....*
gi 1555720989 513 DPFLVVLDEPNSNLD 527
Cdd:COG1101 166 KPKLLLLDEHTAALD 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
371-577 |
2.79e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRP---LAGRIKLDGAALDQWSSERLGRYIgylpQDVELFAG 447
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYV----QQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 --TVADNI---ARFDPgpdPQAIVAAARAAGVHELI--IGLPNGYETQIGEGGT--ALSAGQRQRIALARALYGDPFLVV 518
Cdd:TIGR00955 113 tlTVREHLmfqAHLRM---PRRVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 519 LDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPN--ILSTVDFLLVMKEGQTQMFGT 577
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSseLFELFDKIILMAEGRVAYLGS 250
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
48-316 |
2.83e-11 |
|
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: 64.82 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 48 FAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFT 127
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 128 AVSRLPL-YIGQQGDGLQPQR---DLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAAcgaLVLVTLTVATE 203
Cdd:cd18546 81 HLQRLSLdFHERETSGRIMTRmtsDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVAL---AALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 204 ILTRRpmgAAVQSSVRRNSLAEASRRNAE------VLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRL 277
Cdd:cd18546 158 WFRRR---SSRAYRRARERIAAVNADLQEtlagirVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGN 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 1555720989 278 MLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVD 316
Cdd:cd18546 235 LATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQ 273
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
374-571 |
3.23e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 64.06 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG---AALDQWSSERLGRYIGYLPQD--------- 441
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlYQLDRKQRRAFRRDVQLVFQDspsavnprm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 442 -VELFAGTVADNIARFDpgpdpqaivAAARAAGVHELI--IGLPNGYETQIGEggtALSAGQRQRIALARALYGDPFLVV 518
Cdd:TIGR02769 106 tVRQIIGEPLRHLTSLD---------ESEQKARIAELLdmVGLRSEDADKLPR---QLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 519 LDEPNSNLDAEGEMALAAAILAIKARGGI--LAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
375-590 |
3.63e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.10 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDqWSSE---RLGRYIGYLPQ--DVELFAGTV 449
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQdpDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIArFDPgpdpqaIVAAARAAGVHELI--IGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK13636 101 YQDVS-FGA------VNLKLPEDEVRKRVdnALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 528 AEGEMALAAAILAIKARGGILAIVA-HRPNILST-VDFLLVMKEGQ-------TQMFGTRESVLSTLLPAPQ 590
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIAtHDIDIVPLyCDNVFVMKEGRvilqgnpKEVFAEKEMLRKVNLRLPR 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
374-527 |
4.86e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.52 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGL-------VGAWrpLAGRIKLDGAAL--DQWSSERLGRYIGYLPQDVEL 444
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 445 FAGTVADNIArfdpgpdpqaivaaaraagvheliIGLP-NGY----------ET-------------QIGEGGTALSAGQ 500
Cdd:COG1117 104 FPKSIYDNVA------------------------YGLRlHGIkskseldeivEEslrkaalwdevkdRLKKSALGLSGGQ 159
|
170 180
....*....|....*....|....*..
gi 1555720989 501 RQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
45-315 |
5.16e-11 |
|
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: 64.00 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 45 KAAFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGR 124
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 125 VFTAVSRLPL-YIG--QQGDGLQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTva 201
Cdd:cd18570 81 YFKHLLKLPLsFFEtrKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 202 teILTRRPMGAAVQSSVRRNSLAEA----SRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRL 277
Cdd:cd18570 159 --LLFNKPFKKKNREVMESNAELNSylieSLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISL 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1555720989 278 MLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPV 315
Cdd:cd18570 237 IGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPI 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
325-527 |
5.92e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 325 FVGARQSWSRlsKLLARLPQDaQPMALPVPGSK-LTVERIAIGAPGAQRI---------IVQGVEFSLDAGSVLGIIGPS 394
Cdd:PRK15134 245 FSAPTHPYTQ--KLLNSEPSG-DPVPLPEPASPlLDVEQLQVAFPIRKGIlkrtvdhnvVVKNISFTLRPGETLGLVGES 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 395 GSGKSSLVRGLVgawRPLA--GRIKLDGAALDQWSSERL---GRYIGYLPQDvelfagtvaDNIARfdpgpDPQAIVAAA 469
Cdd:PRK15134 322 GSGKSTTGLALL---RLINsqGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQD---------PNSSL-----NPRLNVLQI 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 470 RAAG--VHELIIGLPNGYETQIG---EGG----------TALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK15134 385 IEEGlrVHQPTLSAAQREQQVIAvmeEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
372-584 |
5.98e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALD------QWSSERLGRYIGYLPQDVELF 445
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 AG-TVADNIARfdPGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:PRK14246 103 PHlSIYDNIAY--PLKSHGIKEKREIKKIVEECLrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 523 NSNLDAEGEMALAAAILAIKARGGILaIVAHRPNILSTV-DFLLVMKEGQTQMFGTRESVLST 584
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIV-IVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
375-527 |
7.71e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAL-----DQWSSERlgRYIGYLPQDVelFAG-- 447
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWRAVR--SDIQMIFQDP--LASln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 ---TVADNIAR----FDPGPDPQAIVAAaraagVHELI--IGL-PNgyetQIGEGGTALSAGQRQRIALARALYGDPFLV 517
Cdd:PRK15079 113 prmTIGEIIAEplrtYHPKLSRQEVKDR-----VKAMMlkVGLlPN----LINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170
....*....|
gi 1555720989 518 VLDEPNSNLD 527
Cdd:PRK15079 184 ICDEPVSALD 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
380-527 |
1.27e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDA--GSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERlgRYIGYLPQDVELFAG-TVADNIA-- 454
Cdd:PRK09452 33 LDLTInnGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYALFPHmTVFENVAfg 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 455 -RFDPGPDPQAIVAaaraagVHELI--IGLpngyETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK09452 111 lRMQKTPAAEITPR------VMEALrmVQL----EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
361-567 |
1.47e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.00 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 361 ERIAIGAPGAQrIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDgaaldqwsseRLGRyIGYLPQ 440
Cdd:TIGR00954 455 ENIPLVTPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----------AKGK-LFYVPQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 DVELFAGTVADNIARFDPGPDPQaivaaARAAGVHELIIGLPNGYETQI--GEGG--------TALSAGQRQRIALARAL 510
Cdd:TIGR00954 523 RPYMTLGTLRDQIIYPDSSEDMK-----RRGLSDKDLEQILDNVQLTHIleREGGwsavqdwmDVLSGGEKQRIAMARLF 597
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 511 YGDPFLVVLDEPNS--NLDAEGEMalaaaiLAIKARGGI-LAIVAHRPNILSTVDFLLVM 567
Cdd:TIGR00954 598 YHKPQFAILDECTSavSVDVEGYM------YRLCREFGItLFSVSHRKSLWKYHEYLLYM 651
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
374-579 |
1.54e-10 |
|
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: 61.00 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVG--AWRPLAGRIKLDGAALDQWS-SERLGRYIGYLPQDVELFAG-TV 449
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPpEERARLGIFLAFQYPPEIPGvKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIaRFdpgpdpqaivaaaraagvheliiglpngyetqIGEGgtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:cd03217 95 ADFL-RY--------------------------------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 530 G-EMALAAAILAIKARGGILaIVAHRPNILSTV--DFLLVMKEGQTQMFGTRE 579
Cdd:cd03217 139 AlRLVAEVINKLREEGKSVL-IITHYQRLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
370-528 |
2.05e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSE-RLgryigyLPQDVELFA-G 447
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDtRL------MFQDARLLPwK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA---RFDPGPDPQAIVAAAraagvheliiglpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:PRK11247 97 KVIDNVGlglKGQWRDAALQALAAV--------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
....
gi 1555720989 525 NLDA 528
Cdd:PRK11247 163 ALDA 166
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
369-529 |
2.16e-10 |
|
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: 60.91 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRI-------KLDGAALDQWSSERLGRY-IGYLPQ 440
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 -----------DV---ELFAGTVADNIARfdpgpdpQAIVAAARAAGVHELIIGLPNgyetqigeggTALSAGQRQRIAL 506
Cdd:COG4778 101 flrviprvsalDVvaePLLERGVDREEAR-------ARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 1555720989 507 ARALYGDPFLVVLDEPNSNLDAE 529
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
367-582 |
2.25e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 367 APGAQRIIVQgVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER----LGRYIGYLPQ-- 440
Cdd:PRK13643 15 SPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 DVELFAGTVADNIArFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQigeGGTALSAGQRQRIALARALYGDPFLVVLD 520
Cdd:PRK13643 94 ESQLFEETVLKDVA-FGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 521 EPNSNLDAEGEMALAAAILAIKARGGILAIVAH-RPNILSTVDFLLVMKEGQTQMFGTRESVL 582
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
379-529 |
2.36e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 379 EFSLDA-------GSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDgaaLDqwsserlgryIGYLPQDVEL-FAGTVA 450
Cdd:PRK13409 352 DFSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LK----------ISYKPQYIKPdYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARFDPGPDPQAIVaaaraagvHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:PRK13409 419 DLLRSITDDLGSSYYK--------SEIIkpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
.
gi 1555720989 529 E 529
Cdd:PRK13409 487 E 487
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
366-527 |
2.43e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.63 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 366 GAPGAQRIiVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYigylPQDVELf 445
Cdd:PRK10419 20 GKHQHQTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF----RRDIQM- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 agTVADNIARFDPGPDpqaivaaaraagVHElIIGLPNGYETQIGEGGTA-----------------------LSAGQRQ 502
Cdd:PRK10419 94 --VFQDSISAVNPRKT------------VRE-IIREPLRHLLSLDKAERLarasemlravdlddsvldkrppqLSGGQLQ 158
|
170 180
....*....|....*....|....*
gi 1555720989 503 RIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLD 183
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
365-571 |
2.53e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.77 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 365 IGAPGA--QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSS----ERLGRYIGYL 438
Cdd:PRK13641 11 IYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 439 PQ--DVELFAGTVADNIaRFdpGPDPQAIVAAARAAGVHELI--IGLPngyETQIGEGGTALSAGQRQRIALARALYGDP 514
Cdd:PRK13641 91 FQfpEAQLFENTVLKDV-EF--GPKNFGFSEDEAKEKALKWLkkVGLS---EDLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 515 FLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHR-PNILSTVDFLLVMKEGQ 571
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGK 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
372-529 |
3.54e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.27 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER---LGRYIGYLPQDVELFAG- 447
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA--RFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:PRK10908 95 TVYDNVAipLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
....
gi 1555720989 526 LDAE 529
Cdd:PRK10908 168 LDDA 171
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
358-530 |
4.39e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLA---GRIKLDGAALDQ---WS-SER 430
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAktvWDiREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 431 LGryIGYLPQDVELFAGTVADNIA-----RFDPGPDPQAIvaaaraagVHELI--IGLPNGYETQigegGTALSAGQRQR 503
Cdd:PRK13640 86 VG--IVFQNPDNQFVGATVGDDVAfglenRAVPRPEMIKI--------VRDVLadVGMLDYIDSE----PANLSGGQKQR 151
|
170 180
....*....|....*....|....*..
gi 1555720989 504 IALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAG 178
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
365-576 |
4.84e-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: 59.18 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 365 IGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLvgAWRPLAGRIK----LDGAALDqwssERLGRYIGYLPQ 440
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTAGVITgeilINGRPLD----KNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 -DVELFAGTVADNIaRFdpgpdpqaivaaaraagvHELIIGLpngyetqigeggtalSAGQRQRIALARALYGDPFLVVL 519
Cdd:cd03232 87 qDVHSPNLTVREAL-RF------------------SALLRGL---------------SVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 520 DEPNSNLDAEGEMALAAAILAIKARGgiLAIVA--HRPN--ILSTVDFLLVMKE-GQTQMFG 576
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSG--QAILCtiHQPSasIFEKFDRLLLLKRgGKTVYFG 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
358-527 |
6.11e-10 |
|
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: 62.01 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVE--RIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKS----SLVRGLVGAWRPLAGRIKLDGAALDQWSSERL 431
Cdd:COG4172 7 LSVEdlSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 432 ----GRYIGYLPQdvE-------LFagTVADNIA---RFDPGPDPQAIVAAaraagVHELI--IGLPNGyETQIGEGGTA 495
Cdd:COG4172 87 rrirGNRIAMIFQ--EpmtslnpLH--TIGKQIAevlRLHRGLSGAAARAR-----ALELLerVGIPDP-ERRLDAYPHQ 156
|
170 180 190
....*....|....*....|....*....|..
gi 1555720989 496 LSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
371-559 |
6.23e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGA--WRPLAGRIKLDGaalDQWSSERlgryigylpqdvelfagT 448
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPD---NQFGREA-----------------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIARFDPGPDpqaivaaaraagVHELI--IGL--PNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:COG2401 102 LIDAIGRKGDFKD------------AVELLnaVGLsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1555720989 525 NLDAEGEMALAAAILAIKARGGILAIVA-HRPNILS 559
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVAtHHYDVID 201
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
371-583 |
6.42e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.42 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG----AALDQWSSERLGRYIGYLPQDVE--L 444
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNKKLKPLRKKVGIVFQFPEhqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 445 FAGTVADNIArFdpGPDPQAIVAAARAAGVHELI--IGLPNGYETQigeGGTALSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:PRK13634 99 FEETVEKDIC-F--GPMNFGVSEEDAKQKAREMIelVGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 523 NSNLDAEGemalaaailaikaRGGILAIVA--HRPNILSTV-------------DFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13634 173 TAGLDPKG-------------RKEMMEMFYklHKEKGLTTVlvthsmedaaryaDQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
369-529 |
7.29e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGrikldgaalDQWSSErlGRYIGYLPQD------- 441
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG---------EARPQP--GIKVGYLPQEpqldptk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 442 -----VELFAGTVADNIARFDP------GPDPQAIVAAARAAGVHELI------------------IGLPNGyETQIgeg 492
Cdd:TIGR03719 84 tvrenVEEGVAEIKDALDRFNEisakyaEPDADFDKLAAEQAELQEIIdaadawdldsqleiamdaLRCPPW-DADV--- 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1555720989 493 gTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:TIGR03719 160 -TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
53-303 |
8.51e-10 |
|
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: 59.96 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 53 VFSGVSNILMLTGAMFMLEVYDRVLPSRSVPT--LIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVS 130
Cdd:pfam00664 6 LLAILSGAISPAFPLVLGRILDVLLPDGDPETqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 131 RLPL-YIGQQGDGLQPQR---DLDNIRTFLSSAgPGTLFDLPWLPFYL-AIIWSLHPTLgttAACGALVLVTLTVATEIL 205
Cdd:pfam00664 86 RQPMsFFDTNSVGELLSRltnDTSKIRDGLGEK-LGLLFQSLATIVGGiIVMFYYGWKL---TLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 206 TRRPMGAAVQSSV---RRNSLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSA 282
Cdd:pfam00664 162 AKILRKLSRKEQKavaKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260
....*....|....*....|.
gi 1555720989 283 MLGVGAWLVIEGEATSGIIIA 303
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVA 262
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
378-527 |
1.00e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAL-DQWSSERLG---RYIGYLPQDVELFA------- 446
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfDAEKGICLPpekRRIGYVFQDARLFPhykvrgn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 ---GTVADNIARFDpgpdpqaivAAARAAGVHELIIGLPngyetqigeggTALSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:PRK11144 97 lryGMAKSMVAQFD---------KIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
....
gi 1555720989 524 SNLD 527
Cdd:PRK11144 157 ASLD 160
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
379-529 |
1.05e-09 |
|
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: 61.34 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 379 EFSLDA-------GSVLGIIGPSGSGKSSLVRglvgawrPLAGRIKLDGAALDqwSSERlgryIGYLPQDVE-LFAGTVA 450
Cdd:COG1245 353 GFSLEVeggeireGEVLGIVGPNGIGKTTFAK-------ILAGVLKPDEGEVD--EDLK----ISYKPQYISpDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARFDPGPDPQAIVAaaraagvHELI--IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:COG1245 420 EFLRSANTDDFGSSYYK-------TEIIkpLGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
.
gi 1555720989 529 E 529
Cdd:COG1245 489 E 489
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
358-529 |
1.43e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKldgaaldqWSSerlGRYIGY 437
Cdd:PRK15064 320 LEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSE---NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 438 LPQDVEL-FAG--TVADNIARF-DPGPDPQAIVAaaraagvhelIIG--LPNGYEtqIGEGGTALSAGQRQRIALARALY 511
Cdd:PRK15064 387 YAQDHAYdFENdlTLFDWMSQWrQEGDDEQAVRG----------TLGrlLFSQDD--IKKSVKVLSGGEKGRMLFGKLMM 454
|
170
....*....|....*...
gi 1555720989 512 GDPFLVVLDEPNSNLDAE 529
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDME 472
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
375-527 |
1.85e-09 |
|
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: 58.15 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSErLGRYIGYLPQDVELFAG-TVADNI 453
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 454 ArfdpgpdpqaivaaaraagVHELIIGLPNGYETQ----------IGEGGTAL----SAGQRQRIALARALYGDPFLVVL 519
Cdd:cd03265 95 Y-------------------IHARLYGVPGAERREridelldfvgLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFL 155
|
....*...
gi 1555720989 520 DEPNSNLD 527
Cdd:cd03265 156 DEPTIGLD 163
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
378-530 |
2.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVE-LFAGTvadnIARF 456
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVGS----IVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 457 DP--GPDPQAIVAAARAAGVHELI--IGLPN--GYETQigeggtALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEG 530
Cdd:PRK13648 104 DVafGLENHAVPYDEMHRRVSEALkqVDMLEraDYEPN------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
374-586 |
2.81e-09 |
|
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: 59.82 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVG--AWRPLAGRI----------------------------KLDGAAL 423
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcpvcggTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 424 DQWSSE-----RLGRYIGYLPQdvELFA----GTVADNIARFDPGPDPQAIVAAARAAGVHELIiglpnGYETQIGEGGT 494
Cdd:TIGR03269 95 DFWNLSdklrrRIRKRIAIMLQ--RTFAlygdDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV-----QLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 495 ALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE-GEMALAAAILAIKARGGILAIVAHRPNILSTV-DFLLVMKEGQT 572
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtAKLVHNALEEAVKASGISMVLTSHWPEVIEDLsDKAIWLENGEI 247
|
250
....*....|....
gi 1555720989 573 QMFGTRESVLSTLL 586
Cdd:TIGR03269 248 KEEGTPDEVVAVFM 261
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
375-527 |
2.91e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyigyLPQDVEL-----FAG-- 447
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL----LRQKIQIvfqnpYGSln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 ---TVADNIArfDPGPDPQAIVAAARAAGVHELI--IGL-PNGYetqiGEGGTALSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:PRK11308 107 prkKVGQILE--EPLLINTSLSAAERREKALAMMakVGLrPEHY----DRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
....*.
gi 1555720989 522 PNSNLD 527
Cdd:PRK11308 181 PVSALD 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
380-527 |
6.31e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDAGSVLGIIGPSGSGKSSLVRGLVGAWrPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVE-LFAGTVADNIARFdp 458
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLTLH-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 459 gpDPQAIVAAARAAGVHELI--IGLPNGYETQIGeggtALSAGQRQRIALARALY-----GDPF--LVVLDEPNSNLD 527
Cdd:PRK03695 94 --QPDKTRTEAVASALNEVAeaLGLDDKLGRSVN----QLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
375-527 |
8.95e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.54 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRyIGYLP--QDVELFAG-TVAD 451
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 NI---------ARFDPG----PDPQAIVAAARAAGVHEL-IIGLpngyeTQIG--EGGTaLSAGQRQRIALARALYGDPF 515
Cdd:PRK11300 100 NLlvaqhqqlkTGLFSGllktPAFRRAESEALDRAATWLeRVGL-----LEHAnrQAGN-LAYGQQRRLEIARCMVTQPE 173
|
170
....*....|..
gi 1555720989 516 LVVLDEPNSNLD 527
Cdd:PRK11300 174 ILMLDEPAAGLN 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
319-575 |
1.16e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 319 IAHWRNFVG--------ARQSWSRLsKLLARLPQDA-------------QPMALPVPgsKLTVERIAIGApgAQRIIVQG 377
Cdd:PRK10636 256 VAHLQSYIDrfrakatkAKQAQSRI-KMLERMELIApahvdnpfhfsfrAPESLPNP--LLKMEKVSAGY--GDRIILDS 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKL-DGAALDQWSSERLgryiGYLPQDvelfaGTVADNIARF 456
Cdd:PRK10636 331 IKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQL----EFLRAD-----ESPLQHLARL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 457 DPGPDPQAIVAAARAAGVHeliiglpngyETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAegEMALAA 536
Cdd:PRK10636 402 APQELEQKLRDYLGGFGFQ----------GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL--DMRQAL 469
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1555720989 537 AILAIKARGGiLAIVAH-RPNILSTVDFLLVMKEGQTQMF 575
Cdd:PRK10636 470 TEALIDFEGA-LVVVSHdRHLLRSTTDDLYLVHDGKVEPF 508
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
390-583 |
1.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 390 IIGPSGSGKSSLVR---GLV--GAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQ--DVELFAGTVADNIArFDP---G 459
Cdd:PRK13645 42 VIGTTGSGKSTMIQltnGLIisETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQETIEKDIA-FGPvnlG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 460 PDPQAIVAAaraagVHELI--IGLPNGYetqIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMALAAA 537
Cdd:PRK13645 121 ENKQEAYKK-----VPELLklVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1555720989 538 ILAIKARGG--ILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13645 193 FERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-573 |
1.65e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWR-PLAGRIKLDGAALDQWSSERLGRY-IGYLPQD------VELFA 446
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAgIAMVPEDrkrhgiVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 gtVADNI-----------ARFDPGPDPQAIVAAARAAGVHELIIGLPNGyetqigeggtALSAGQRQRIALARALYGDPF 515
Cdd:TIGR02633 356 --VGKNItlsvlksfcfkMRIDAAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 516 LVVLDEPNSNLDAEGEMALAAAILAIKARG-GILAIVAHRPNILSTVDFLLVMKEGQTQ 573
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
374-573 |
2.36e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.17 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLG----RYIGYLPQ--------- 440
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklraKHVGFVFQsfmliptln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 ---DVELFA--GTVADNIARfdpgpdpQAIVAAARAAGVHELIIGLPngyetqigeggTALSAGQRQRIALARALYGDPF 515
Cdd:PRK10584 105 aleNVELPAllRGESSRQSR-------NGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 516 LVVLDEPNSNLDAE-GEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQ 573
Cdd:PRK10584 167 VLFADEPTGNLDRQtGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
375-527 |
2.38e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALD----QWSSERLgRYIGYLPQ---------- 440
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRI-RMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 ---DVELFAGTVADNIARfdpgpdPQAIVAAARAAGVheliigLPN--GYETQigeggtALSAGQRQRIALARALYGDPF 515
Cdd:PRK15112 108 qilDFPLRLNTDLEPEQR------EKQIIETLRQVGL------LPDhaSYYPH------MLAPGQKQRLGLARALILRPK 169
|
170
....*....|..
gi 1555720989 516 LVVLDEPNSNLD 527
Cdd:PRK15112 170 VIIADEALASLD 181
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
375-527 |
2.63e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVR------GLVGAWRpLAGRIKLDGAAL--DQWSSERLGRYIGYLPQDVELFA 446
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlnDLIPGFR-VEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 447 GTVADNIARfdpGPdpqaiVAAARAAGVHELI------IGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLD 520
Cdd:PRK14243 105 KSIYDNIAY---GA-----RINGYKGDMDELVerslrqAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
....*..
gi 1555720989 521 EPNSNLD 527
Cdd:PRK14243 177 EPCSALD 183
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
380-531 |
2.75e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 380 FSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLgryIGYLPQDVEL---FAGTVADNIA-- 454
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVdwsFPVLVEDVVMmg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 455 --------RFDPGPDPQAIVAAARAAGVHELiiglpngYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNL 526
Cdd:PRK15056 105 ryghmgwlRRAKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
....*
gi 1555720989 527 DAEGE 531
Cdd:PRK15056 174 DVKTE 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
375-565 |
2.92e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVR---GLVGAWRPLAGRIKLDGAALDQwsSERLGRYI-------GYLPQDVEL 444
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQR--EGRLARDIrksrantGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 445 FAG-TVADNIARFDPGPDP------QAIVAAARAAGVHELI-IGLPNGYETQIgeggTALSAGQRQRIALARALYGDPFL 516
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTrVGMVHFAHQRV----STLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1555720989 517 VVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAhrpniLSTVDFLL 565
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVT-----LHQVDYAL 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
374-527 |
3.12e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.09 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKS---SLVRGLVGawrPLAGRIKLDGAALDQWSSERLGRYIGYLPQD--------V 442
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKStllSMISRLLP---PDSGEVLVDGLDVATTPSRELAKRLAILRQEnhinsrltV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 443 -ELFA-G---------TVADN------IARFDPGPdpqaivaaaraagvheliigLPNGYetqIGEggtaLSAGQRQRIA 505
Cdd:COG4604 93 rELVAfGrfpyskgrlTAEDReiideaIAYLDLED--------------------LADRY---LDE----LSGGQRQRAF 145
|
170 180
....*....|....*....|..
gi 1555720989 506 LARALYGDPFLVVLDEPNSNLD 527
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLD 167
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
372-529 |
3.61e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLdGAALDqwsserlgryIGYLPQDVELFAG--TV 449
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQSRDALDPnkTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIArfdpgpdpqaivaaaraAGVHELIIGlpnGYETQ------------------IGEggtaLSAGQRQRIALARALY 511
Cdd:TIGR03719 404 WEEIS-----------------GGLDIIKLG---KREIPsrayvgrfnfkgsdqqkkVGQ----LSGGERNRVHLAKTLK 459
|
170
....*....|....*...
gi 1555720989 512 GDPFLVVLDEPNSNLDAE 529
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE 477
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
372-584 |
3.88e-08 |
|
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: 54.71 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAG-RIKLDGAALDQWSSERLGRYIGYlpqdvelFAGTVA 450
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL-------VSPALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIARFDPgpdpqaivaaaraagVHELI-------IGLPNGYE-----------TQIGEGGTA------LSAGQRQRIAL 506
Cdd:COG1119 89 LRFPRDET---------------VLDVVlsgffdsIGLYREPTdeqrerarellELLGLAHLAdrpfgtLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 507 ARALYGDPFLVVLDEPNSNLDAEGeMALAAAILAIKARGGILAI--VAHRPN-ILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGA-RELLLALLDKLAAEGAPTLvlVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
.
gi 1555720989 584 T 584
Cdd:COG1119 233 S 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
374-580 |
3.99e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAL-------------DQWSSERLGRYIGYLPQ 440
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 DVELFAG-TVADNIARfdpGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVL 519
Cdd:PRK10619 100 HFNLWSHmTVLENVME---APIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 520 DEPNSNLDAEGEMALAAAILAIKARGGILAIVAHR----PNILSTVDFL---LVMKEGQ-TQMFGTRES 580
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEmgfaRHVSSHVIFLhqgKIEEEGApEQLFGNPQS 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-527 |
4.13e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.10 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGL------VGAWRpLAGRIKLDGAALDQWSSE-RLGRYIGYLPQDV 442
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYR-YSGDVLLGGRSIFNYRDVlEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 443 ELFAGTVADNIArfdPGPDPQAIVAAARAAGVHE---LIIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVL 519
Cdd:PRK14271 111 NPFPMSIMDNVL---AGVRAHKLVPRKEFRGVAQarlTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
....*...
gi 1555720989 520 DEPNSNLD 527
Cdd:PRK14271 188 DEPTSALD 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
375-528 |
4.14e-08 |
|
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: 54.26 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGaaLDQWS-SERLGRYIGY-LPQDVELFAG-TVAD 451
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKrRKKFLRRIGVvFGQKTQLWWDlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 452 N------IARFDPGPDPQAIVAAARAAGVHELIiglpngyETQIgeggTALSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:cd03267 115 SfyllaaIYDLPPARFKKRLDELSELLDLEELL-------DTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
...
gi 1555720989 526 LDA 528
Cdd:cd03267 184 LDV 186
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
375-571 |
4.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYI----GYLPQ--DVELFAGT 448
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVrkriGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIArFdpGPDPQAIVAAARAAGVHELIIGLpnGYETQIGEGGT-ALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK13646 103 VEREII-F--GPKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1555720989 528 AEGE---MALAAAILAIKARGGILaiVAHRPN-ILSTVDFLLVMKEGQ 571
Cdd:PRK13646 178 PQSKrqvMRLLKSLQTDENKTIIL--VSHDMNeVARYADEVIVMKEGS 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
375-527 |
4.94e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGL--VGAWRP---LAGRIKLDGAALDQWSSE--RLGRYIGYLPQDVELFAG 447
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA---RFDPGPDPQAIVAAaraagVHELIIG--LPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEA-----VEKSLKGasIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
....*
gi 1555720989 523 NSNLD 527
Cdd:PRK14239 176 TSALD 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
377-571 |
5.78e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.71 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRI--------KLDGAALDQWSSER----------------LG 432
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEKEKVLEKlviqktrfkkikkikeIR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 433 RYIGYLPQDVE--LFAGTVADNIArFDP---GPDPQAIVAAARaagvhELI--IGLPNGYetqIGEGGTALSAGQRQRIA 505
Cdd:PRK13651 105 RRVGVVFQFAEyqLFEQTIEKDII-FGPvsmGVSKEEAKKRAA-----KYIelVGLDESY---LQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 506 LARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHR-PNILSTVDFLLVMKEGQ 571
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGK 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
375-522 |
6.13e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS-SERLGRYIGYLPQD------VELFag 447
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDrlgrglVPDM-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIA--RFDPGP-------DPQAIVAAaraagVHELI----IgLPNGYETQIGeggtALSAGQRQRIALARALYGDP 514
Cdd:COG3845 352 SVAENLIlgRYRRPPfsrggflDRKAIRAF-----AEELIeefdV-RTPGPDTPAR----SLSGGNQQKVILARELSRDP 421
|
....*...
gi 1555720989 515 FLVVLDEP 522
Cdd:COG3845 422 KLLIAAQP 429
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
374-571 |
7.07e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG---AALDQWSSERLGR-YIGYLPQDVELFAG-T 448
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvATLDADALAQLRReHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNI---ARFDPGPDPQAIVAAaraagvHELIIGLpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:PRK10535 103 AAQNVevpAVYAGLERKQRLLRA------QELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1555720989 526 LDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
374-576 |
8.49e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.86 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQwsSER----LGRYIGYLPQDVE--LFAG 447
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRgllaLRQQVATVFQDPEqqIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIArfdpgpdpqaivAAARAAGVHE----------LIIGLPNGYETQIGEggtALSAGQRQRIALARALYGDPFLV 517
Cdd:PRK13638 94 DIDSDIA------------FSLRNLGVPEaeitrrvdeaLTLVDAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 518 VLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTV-DFLLVMKEGQTQMFG 576
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHG 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
371-522 |
1.13e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 371 QRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL---GRYIGYLPQDVELFAG 447
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 -TVADNIARfdpgpdPQAIVAAARAAGVHELI------IGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLD 520
Cdd:PRK11831 99 mNVFDNVAY------PLREHTQLPAPLLHSTVmmkleaVGLRGAAKLMPSE----LSGGMARRAALARAIALEPDLIMFD 168
|
..
gi 1555720989 521 EP 522
Cdd:PRK11831 169 EP 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
375-581 |
1.13e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSS-ERLGRYIGYLPQ---DVELFAG-TV 449
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIArfdpgpdpqaiVAAARAAGVHELIIGLPNGYETQ----------------IGEGGTALSAGQRQRIALARALYGD 513
Cdd:PRK09700 359 AQNMA-----------ISRSLKDGGYKGAMGLFHEVDEQrtaenqrellalkchsVNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 514 PFLVVLDEPNSNLDAEGEMALAAAILAIKARG-GILAIVAHRPNILSTVDFLLVMKEGQ-TQMFGTRESV 581
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITVCDRIAVFCEGRlTQILTNRDDM 497
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
369-583 |
3.40e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGaaLDQWSSERL---GRYIGYLPQ--DVE 443
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLwdiRNKAGMVFQnpDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 444 LFAGTVADNIArFDP---GPDPQAIVA----AARAAGVHELIIGLPNgyetqigeggtALSAGQRQRIALARALYGDPFL 516
Cdd:PRK13633 98 IVATIVEEDVA-FGPenlGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 517 VVLDEPNSNLDAEGEMALAAAILAIKARGGILAI-VAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIIlITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
363-528 |
3.77e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 363 IAIGAPGAQRIivQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG---------AALDQ-------- 425
Cdd:PRK11288 10 IGKTFPGVKAL--DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfasttAALAAgvaiiyqe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 426 -------WSSERLgrYIGYLPQ-----DVELFAGTVADNIARFDPGPDPQaivaaaraagvheliiglpngyeTQIGEgg 493
Cdd:PRK11288 88 lhlvpemTVAENL--YLGQLPHkggivNRRLLNYEAREQLEHLGVDIDPD-----------------------TPLKY-- 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1555720989 494 taLSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:PRK11288 141 --LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-529 |
4.02e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.45 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVR---GLVGAWRP--LAGRIKLDGAALDQWSSERLGR---YIGYLPQDVELF 445
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnRLIELYPEarVSGEVYLDGQDIFKMDVIELRRrvqMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 agTVADNIArFDPGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:PRK14247 98 --SIFENVA-LGLKLNRLVKSKKELQERVRWALekAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
....*.
gi 1555720989 524 SNLDAE 529
Cdd:PRK14247 175 ANLDPE 180
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
495-528 |
4.72e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 4.72e-07
10 20 30
....*....|....*....|....*....|....
gi 1555720989 495 ALSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
375-583 |
4.73e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.34 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERL----GRYIGYLPQDVELFAG-TV 449
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIA-RFDPGPDPQAIVAAARAAGVHEliIGLPN---GYETQigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSN 525
Cdd:PRK10070 124 LDNTAfGMELAGINAEERREKALDALRQ--VGLENyahSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 526 LDA--EGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFGTRESVLS 583
Cdd:PRK10070 195 LDPliRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
377-581 |
5.01e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.67 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSER----LGRYIGYLPQ--DVELFAGTVA 450
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqIRKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNIArFDP---GPDP----QAIVAAARAAGVHELIIGlPNGYEtqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPN 523
Cdd:PRK13649 105 KDVA-FGPqnfGVSQeeaeALAREKLALVGISESLFE-KNPFE---------LSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 524 SNLDAEGEMALAAAILAIKARGGILAIVAH-RPNILSTVDFLLVMKEGQTQMFGTRESV 581
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
48-316 |
6.06e-07 |
|
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: 51.33 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 48 FAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFT 127
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 128 AVSRLPLyiGQQgDGLQPQR-------DLDNIRTFLSsAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVTLTV 200
Cdd:cd18543 81 HLQRLDG--AFH-DRWQSGQllsratsDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 201 ateiLTRRPMGAAVQSSVRRN----SLAEASRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALR 276
Cdd:cd18543 157 ----RFRRRYFPASRRAQDQAgdlaTVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1555720989 277 LMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPVD 316
Cdd:cd18543 233 ELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVR 272
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
364-575 |
7.43e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 364 AIGAPGAQrIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRI----KLDGAALDQWSSERLGryigyLP 439
Cdd:PLN03073 515 SFGYPGGP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFSQHHVDGLD-----LS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 440 QDVELFagtvadnIARFDPGPDPQAIVAAARAAGVHElIIGLPNGYetqigeggtALSAGQRQRIALARALYGDPFLVVL 519
Cdd:PLN03073 589 SNPLLY-------MMRCFPGVPEQKLRAHLGSFGVTG-NLALQPMY---------TLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 520 DEPNSNLDAEGemALAAAILAIKARGGILaIVAHRPNILS-TVDFLLVMKEGQTQMF 575
Cdd:PLN03073 652 DEPSNHLDLDA--VEALIQGLVLFQGGVL-MVSHDEHLISgSVDELWVVSEGKVTPF 705
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-571 |
8.39e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWR-PLAGRIKLDGAALDQWSSERLGRY-IGYLPQD------VE 443
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQgIAMVPEDrkrdgiVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 444 LFAgtVADNIA-----RF-DPGPDPQAIVAAARAAGVHELIIGLPNGyETQIGEggtaLSAGQRQRIALARALYGDPFLV 517
Cdd:PRK13549 355 VMG--VGKNITlaaldRFtGGSRIDDAAELKTILESIQRLKVKTASP-ELAIAR----LSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 518 VLDEPNSNLDAEGEMALAAAILAIKARG-GILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
355-420 |
1.27e-06 |
|
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: 49.84 E-value: 1.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1555720989 355 GSKLTVERIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG 420
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
369-529 |
1.38e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGrikldgaalDQWSSErlGRYIGYLPQD------- 441
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------EARPAP--GIKVGYLPQEpqldpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 442 -----VELFAGTVADNIARFD------PGPDPQAIVAAARAAGVHELI------------------IGLPNGyETQIgeg 492
Cdd:PRK11819 86 tvrenVEEGVAEVKAALDRFNeiyaayAEPDADFDALAAEQGELQEIIdaadawdldsqleiamdaLRCPPW-DAKV--- 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1555720989 493 gTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:PRK11819 162 -TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
375-571 |
1.79e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS-SERLGRYIGYLPQDVE---LFAG-TV 449
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRKrdgLVLGmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIA------------RFDPGPDPQAivaaaraagVHELI----IGLPNgYETQIGEggtaLSAGQRQRIALARALYGD 513
Cdd:PRK10762 348 KENMSltalryfsraggSLKHADEQQA---------VSDFIrlfnIKTPS-MEQAIGL----LSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1555720989 514 PFLVVLDEPNSNLD---------------AEGEmalaaailaikargGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:PRK10762 414 PKVLILDEPTRGVDvgakkeiyqlinqfkAEGL--------------SIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
370-527 |
2.25e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIK--------LDGAALDQWSSERLGRY-IGYLPQ 440
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlRDLYALSEAERRRLLRTeWGFVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 D------VELFAG--------------------TVADNIARFDPGPDpqaivaaaraagvheliiglpngyetQIGEGGT 494
Cdd:PRK11701 97 HprdglrMQVSAGgnigerlmavgarhygdiraTAGDWLERVEIDAA--------------------------RIDDLPT 150
|
170 180 190
....*....|....*....|....*....|...
gi 1555720989 495 ALSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
365-576 |
2.32e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 365 IGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLvgAWRPLAGRIKLD-----GAALDqwssERLGRYIGYLP 439
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVITGGdrlvnGRPLD----SSFQRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 440 Q-DVELFAGTVADNI---ARFDpgpDPQAIVAAARAAGVHELI--IGLPNGYETQIGEGGTALSAGQRQRIALARALYGD 513
Cdd:TIGR00956 843 QqDLHLPTSTVRESLrfsAYLR---QPKSVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 514 PFLVV-LDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDF---LLVMKEGQTQMFG 576
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFdrlLLLQKGGQTVYFG 986
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
374-423 |
2.57e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.92 E-value: 2.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG--AAL 423
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSAL 92
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
385-527 |
2.94e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 385 GSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGA---ALDQWSSERLGRYIGYL----------PQDVEL----FAG 447
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdeILDEFRGSELQNYFTKLlegdvkvivkPQYVDLipkaVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 TVADNIARFDpgpdpqaivaaarAAGVHELII---GLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:cd03236 106 KVGELLKKKD-------------ERGKLDELVdqlELRHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPSS 168
|
...
gi 1555720989 525 NLD 527
Cdd:cd03236 169 YLD 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
378-570 |
3.22e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAA---LDQWSSERLGryIGYLPQDV----ELfagTVA 450
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLG--IGIIYQELsvidEL---TVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 451 DNI------ARFDPGPDPQAIVAAARAAGVHELIIGLPNGYETQIGEggtaLSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:PRK09700 99 ENLyigrhlTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1555720989 525 NL-DAEGEMALAAAILAIKARGGILAIvAHRPN-ILSTVDFLLVMKEG 570
Cdd:PRK09700 175 SLtNKEVDYLFLIMNQLRKEGTAIVYI-SHKLAeIRRICDRYTVMKDG 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
372-563 |
3.45e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQwsseRLGRYigylpQDVELFAG---- 447
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTY-----QKQLCFVGhrsg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 -----TVADNiARFDpgpdpqaIVAAARAAGVHELIIGLPNGYETQIGEGgtALSAGQRQRIALARALYGDPFLVVLDEP 522
Cdd:PRK13540 85 inpylTLREN-CLYD-------IHFSPGAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1555720989 523 NSNLDAEGEMALAAAILAIKARGGILAIVAHRPNILSTVDF 563
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADY 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
370-529 |
4.01e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 370 AQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRI----KLDGAALDQWSSErlgryigylpQDVElf 445
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLEVAYFDQHRAE----------LDPE-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 aGTVADNIARfdpgpdpqaivaaaraaGVHELIIglpNGYETQI-----------GEGGT---ALSAGQRQRIALARALY 511
Cdd:PRK11147 398 -KTVMDNLAE-----------------GKQEVMV---NGRPRHVlgylqdflfhpKRAMTpvkALSGGERNRLLLARLFL 456
|
170
....*....|....*...
gi 1555720989 512 GDPFLVVLDEPNSNLDAE 529
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVE 474
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
374-528 |
4.24e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.07 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQwsSERLGRYIGYLPQDVELFAG-TVADN 452
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIAMVFQNYALYPHmSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 453 IArfdpgpdpqaivaaaraagvHEL-IIGLPNG-YETQIGEGGT-------------ALSAGQRQRIALARALYGDPFLV 517
Cdd:PRK11650 97 MA--------------------YGLkIRGMPKAeIEERVAEAARileleplldrkprELSGGQRQRVAMGRAIVREPAVF 156
|
170
....*....|.
gi 1555720989 518 VLDEPNSNLDA 528
Cdd:PRK11650 157 LFDEPLSNLDA 167
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
378-527 |
4.31e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSS-ERLGRYIGYLPQDVELfAGTVADNIARF 456
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLARGLVYLPEDRQS-SGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 457 DpgpdpqaivaaARAAGVHELIIGLPNGYETQIGEGGTA---------------LSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:PRK15439 361 N-----------VCALTHNRRGFWIKPARENAVLERYRRalnikfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
....*.
gi 1555720989 522 PNSNLD 527
Cdd:PRK15439 430 PTRGVD 435
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
378-521 |
8.44e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIGYLPQDVELFAGTVadniarfd 457
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL-------- 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 458 pGPDPQAIVAAARAAGVHELiiGLPNGYETQIGE-GGTALSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:PRK10522 414 -GPEGKPANPALVEKWLERL--KMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
478-570 |
9.16e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 478 IIGLPngyetqigeGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARGGILAIVAHRP-- 555
Cdd:PLN03140 1011 IVGLP---------GVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPsi 1081
|
90
....*....|....*
gi 1555720989 556 NILSTVDFLLVMKEG 570
Cdd:PLN03140 1082 DIFEAFDELLLMKRG 1096
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
375-571 |
9.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSS-------------ERlgRYIG-YLPQ 440
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvteER--RSTGiYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 441 DVElFAGTVAdNIARF----------DPGPDPQAIvaaaraagVHELIIGLPnGYETQIGeggtALSAGQRQRIALARAL 510
Cdd:PRK10982 342 DIG-FNSLIS-NIRNYknkvglldnsRMKSDTQWV--------IDSMRVKTP-GHRTQIG----SLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1555720989 511 YGDPFLVVLDEPNSNLDAEGEMALAAAILAIKARG-GILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
367-571 |
1.09e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 367 APGAQRIIVQGVE---------FSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS---SERLGry 434
Cdd:PRK11288 252 PLGEVRLRLDGLKgpglrepisFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdAIRAG-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 435 IGYLPQDVE---LFAG-TVADNI---AR---------FDPGPDPQAIVAAaraagVHELIIGLPNGyETQIGeggtALSA 498
Cdd:PRK11288 330 IMLCPEDRKaegIIPVhSVADNInisARrhhlragclINNRWEAENADRF-----IRSLNIKTPSR-EQLIM----NLSG 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1555720989 499 GQRQRIALARALYGDPFLVVLDEPNSNLD--AEGEMalaAAILAIKARGGILAIVAHR--PNILSTVDFLLVMKEGQ 571
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHEI---YNVIYELAAQGVAVLFVSSdlPEVLGVADRIVVMREGR 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
374-576 |
1.35e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWS---SERLGRYIgyLPQDVELFAG-TV 449
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLGIYL--VPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIARFDPGPdpqaivaAARAAGVHELIIGLpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLD-A 528
Cdd:PRK15439 104 KENILFGLPKR-------QASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1555720989 529 EGEMALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQTQMFG 576
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
369-577 |
1.41e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 369 GAQRIIVQGVEFSldAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAAldqwsserlgryIGYLPQDVELfagt 448
Cdd:cd03222 11 GVFFLLVELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT------------PVYKPQYIDL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 vadniarfdpgpdpqaivaaaraagvheliiglpngyetqigeggtalSAGQRQRIALARALYGDPFLVVLDEPNSNLDA 528
Cdd:cd03222 73 ------------------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1555720989 529 EGEMALAAAILAIKARGGILA-IVAHRPNILSTVDFLLVMKEGQTQMFGT 577
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKKTAlVVEHDLAVLDYLSDRIHVFEGEPGVYGI 154
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
372-418 |
1.63e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 1.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKL 418
Cdd:PRK11819 337 RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
378-529 |
1.71e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.55 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDqWSSE-------RLGRYIGYLPQDVELFAG-TV 449
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTpsdkairELRRNVGMVFQQYNLWPHlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIARfDP----GPDPQAIVAAARaagvhELIIGLpngyetQIGEGGTA----LSAGQRQRIALARALYGDPFLVVLDE 521
Cdd:PRK11124 100 QQNLIE-APcrvlGLSKDQALARAE-----KLLERL------RLKPYADRfplhLSGGQQQRVAIARALMMEPQVLLFDE 167
|
....*...
gi 1555720989 522 PNSNLDAE 529
Cdd:PRK11124 168 PTAALDPE 175
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-530 |
1.78e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.76 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGL-----VGAWRPLAGRIKLDGAALdqWSSE----RLGRYIGYLPQDVEL 444
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNI--YSPDvdpiEVRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 445 FAG-TVADNIA---RFDPGPDPQAIVAAARAAGVHEliIGLPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLD 520
Cdd:PRK14267 97 FPHlTIYDNVAigvKLNGLVKSKKELDERVEWALKK--AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170
....*....|
gi 1555720989 521 EPNSNLDAEG 530
Cdd:PRK14267 175 EPTANIDPVG 184
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
82-315 |
2.03e-05 |
|
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: 46.70 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 82 VPTLIAMAILAGAlfagQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVSRLPLYIGQQ---GDGLQPQRDLDNIRTFLSS 158
Cdd:cd18569 42 RPLLLGMALTALL----QGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQryaGDIASRVQSNDRVANLLSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 159 AGPGTLFDLPWLPFYLAIIWSLHPTLgtTAACGALVLVTLTVATEILTRRPMGAAV--QSSVRRNSLAEASRRNAEVLQA 236
Cdd:cd18569 118 QLATTVLNLVMAVFYALLMLQYDVPL--TLIGIAIALLNLLVLRLVSRKRVDLNRRllQDSGKLTGTTMSGLQMIETLKA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 237 MGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFARALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPV 315
Cdd:cd18569 196 SGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPV 274
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
362-440 |
2.08e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 2.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 362 RIAIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAwrpLAGRIKLDGAALDQwsserlGRYIGYLPQ 440
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL---LAANGRIGGSATFN------GREILNLPE 88
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
47-315 |
5.46e-05 |
|
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: 45.54 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 47 AFAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIG----AELDEavg 122
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGqrilYDLRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 123 gRVFTAVSRLPL-YIGQQGDG---LQPQRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLgttaACGALVLVTL 198
Cdd:cd18545 78 -DLFSHLQKLSFsFFDSRPVGkilSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRL----ALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 199 TVATEILTRRPMGAAVQSSVRRNS-----LAEaSRRNAEVLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFGSFAR 273
Cdd:cd18545 153 LVLVVFLLRRRARKAWQRVRKKISnlnayLHE-SISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1555720989 274 ALRLMLQSAMLGVGAWLVIEGEATSGIIIAGSILVGRALAPV 315
Cdd:cd18545 232 LISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPI 273
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
375-527 |
5.82e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLG---RYIGYLPQDVelFAG---- 447
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDP--YASldpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 448 -TVADNIarFDPGPDPQAIVAAARAAGVHELI--IGLPNGYETQIGEggtALSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:PRK10261 418 qTVGDSI--MEPLRVHGLLPGKAAAARVAWLLerVGLLPEHAWRYPH---EFSGGQRQRICIARALALNPKVIIADEAVS 492
|
...
gi 1555720989 525 NLD 527
Cdd:PRK10261 493 ALD 495
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
84-318 |
6.09e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 45.20 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 84 TLIAMAILAgaLFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVSRLPL-YIGQQ--GDGLQpqR---DLDNIRTFLS 157
Cdd:cd18564 54 LLAAAALVG--IALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLsFHDRRrtGDLLS--RltgDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 158 SAGPGTLFDLPWLPFYLAIIWSLHPTLGTTAACGALVLVtltVATEILTRRpMGAAVQSSVRRN----SLAEASRRNAEV 233
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLL---LAARRFSRR-IKEASREQRRREgalaSVAQESLSAIRV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 234 LQAMGMGRRLHDHWREASREHL----------ALQQRVSDIVGGFGSfaralrlmlqSAMLGVGAWLVIEGEATSGIIIA 303
Cdd:cd18564 206 VQAFGREEHEERRFARENRKSLraglraarlqALLSPVVDVLVAVGT----------ALVLWFGAWLVLAGRLTPGDLLV 275
|
250
....*....|....*.
gi 1555720989 304 GSILVGRALAPV-DLA 318
Cdd:cd18564 276 FLAYLKNLYKPVrDLA 291
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
356-528 |
6.61e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.69 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 356 SKLTVERIAIGAPgaqRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRP----LAGRIKLDGAALDqwSSERL 431
Cdd:PRK10418 3 QQIELRNIALQAA---QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA--PCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 432 GRYIGYLPQD-------VELFAGTVADNI-ARFDPGPDPQAIVAAARaagvheliIGLPNGyETQIGEGGTALSAGQRQR 503
Cdd:PRK10418 78 GRKIATIMQNprsafnpLHTMHTHARETClALGKPADDATLTAALEA--------VGLENA-ARVLKLYPFEMSGGMLQR 148
|
170 180
....*....|....*....|....*.
gi 1555720989 504 IALARALYGD-PFLVVlDEPNSNLDA 528
Cdd:PRK10418 149 MMIALALLCEaPFIIA-DEPTTDLDV 173
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
375-571 |
1.18e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVrglvgawrplagrikldgaaLDQWSSERLGRYIGYLPqdvelfagtvadnia 454
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--------------------NEGLYASGKARLISFLP--------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 455 RFDPGPdpqaivaaARAAGVHELIIGLPNGYETqIGEGGTALSAGQRQRIALARALYGDPF--LVVLDEPNSNLDAEGEM 532
Cdd:cd03238 56 KFSRNK--------LIFIDQLQFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 1555720989 533 ALAAAILAIKARGGILAIVAHRPNILSTVDFLLVMKEGQ 571
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
372-557 |
1.58e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.05 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 372 RIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVG----AWRP----LAGRIKLDGAALDQWSSERLGRYIGYLPQDVE 443
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPrgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 444 LFAGTVADNIARFDPGPDPQAIVAAARAAG-VHELIIGLPnGYETQIGEGGTALSAGQRQRIALARAL---------YGD 513
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGeIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1555720989 514 PFLVVLDEPNSNLDA--EGEMALAAAILAIKARGGILAIVaHRPNI 557
Cdd:PRK13547 173 PRYLLLDEPTAALDLahQHRLLDTVRRLARDWNLGVLAIV-HDPNL 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
385-532 |
1.96e-04 |
|
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: 41.98 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 385 GSVLGIIGPSGSGKSSLVRglvgawrplagrikldgaaldqwsseRLGRYIGYLPQDVELFAGTVADNIARFDpgpdpqa 464
Cdd:smart00382 2 GEVILIVGPPGSGKTTLAR--------------------------ALARELGPPGGGVIYIDGEDILEEVLDQ------- 48
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1555720989 465 ivaaaraagvheliiglpnGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAEGEM 532
Cdd:smart00382 49 -------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
477-527 |
2.27e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 2.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1555720989 477 LIIGLPNGYETQIGEGGTaLSAGQRQRIALARALYGDPFLVVLDEPNSNLD 527
Cdd:PLN03073 327 ILAGLSFTPEMQVKATKT-FSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
375-420 |
3.20e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 3.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDG 420
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
374-437 |
3.33e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.71 E-value: 3.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1555720989 374 IVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVG--AWRPLAGRIKLDGAALDQWSSE---RLGRYIGY 437
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEeraHLGIFLAF 90
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
379-588 |
4.17e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 379 EFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQWSSERLGRYIG---------YLPQDVELFAGTV 449
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 450 ADNIArfDPGPDPQAIVAAARAAGVHELIiGLPNGYetqigeggtaLSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:PRK10938 103 AEIIQ--DEVKDPARCEQLAQQFGITALL-DRRFKY----------LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 530 GEMALAAAILAIKARGGILAIVAHRPN-ILSTVDFLLVMKEGQTQMFGTRESVLSTLLPA 588
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLVLNRFDeIPDFVQFAGVLADCTLAETGEREEILQQALVA 229
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
358-441 |
5.31e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.59 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVEriaIGAPGAQRIIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGA----WRPLAGRIKLDGAALDQWSS-ER-- 430
Cdd:COG4170 9 LTIE---IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnWHVTADRFRWNGIDLLKLSPrERrk 85
|
90
....*....|..
gi 1555720989 431 -LGRYIGYLPQD 441
Cdd:COG4170 86 iIGREIAMIFQE 97
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
48-303 |
5.42e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 42.50 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 48 FAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPTLIAMA-ILAGALFA---GQAVIDLVRGRIMNRIGAELDEAVGG 123
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLlLLVLGLAGayvLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 124 RVFTAVSRLPL-YIGQQgdglQP-------QRDLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLgttaACGALVL 195
Cdd:cd18563 81 DLYEHLQRLSLsFFDKR----QTgslmsrvTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKL----ALLVLIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 196 VTLTVATEILTRRPMGAAVQSSVRRNSlaEASRRNAEVLQ------AMGMGRRLHDHWREASREHLALQQRVSDIVGGFG 269
Cdd:cd18563 153 VPLVVWGSYFFWKKIRRLFHRQWRRWS--RLNSVLNDTLPgirvvkAFGQEKREIKRFDEANQELLDANIRAEKLWATFF 230
|
250 260 270
....*....|....*....|....*....|....
gi 1555720989 270 SFARALRLMLQSAMLGVGAWLVIEGEATSGIIIA 303
Cdd:cd18563 231 PLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVA 264
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
366-527 |
8.77e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 366 GAPGAQRIIVQGVEFSLDAgsvlgIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAALDQwSSERLGRYIGYLPQDVELF 445
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITA-----FLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 446 AG-TVADNIARFDPGPDPQAIVAAARAAGVHEliiglPNGYETQIGEGGTALSAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:TIGR01257 1016 HHlTVAEHILFYAQLKGRSWEEAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
...
gi 1555720989 525 NLD 527
Cdd:TIGR01257 1091 GVD 1093
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
377-440 |
1.23e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1555720989 377 GVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIK-LDGAALDQWSSERLGRYIGYLPQ 440
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVCPRIAYMPQ 83
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
494-529 |
1.40e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1555720989 494 TALSAGQRQRIALARALYGDPFLVVLDEPNSNLDAE 529
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-571 |
1.70e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.35 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 375 VQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWR--PLAGRIKLDGAALDQWS---SERLGryIGYLPQDVELFAG-T 448
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNirdTERAG--IVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 449 VADNIARFDPGPDP-QAIVAAARAAGVHELI--IGLPNGYETQ-IGEGGtalsAGQRQRIALARALYGDPFLVVLDEPNS 524
Cdd:TIGR02633 95 VAENIFLGNEITLPgGRMAYNAMYLRAKNLLreLQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1555720989 525 NLdAEGEMALAAAILAIKARGGILAI-VAHRPNILSTV-DFLLVMKEGQ 571
Cdd:TIGR02633 171 SL-TEKETEILLDIIRDLKAHGVACVyISHKLNEVKAVcDTICVIRDGQ 218
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-303 |
2.10e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 40.60 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 71 EVYDRVL-PSRSVPTLIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAVGGRVFTAVSRLPL-YIGQQGDGLQPQR- 147
Cdd:cd18778 24 ELVDLVTiGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLrYFDDRQTGDLMSRv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 148 --DLDNIRTFLSSAGPGTLFDLPWLPFYLAIIWSLHPTLGttaacgALVLVT---LTVATEILTRRPMGAAVQSsvrRNS 222
Cdd:cd18778 104 inDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLA------LLTLIPipfLALGAWLYSKKVRPRYRKV---REA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 223 LAEASRRNAE------VLQAMGMGRRLHDHWREASREHLALQQRVSDIVGGFG---SFARALRLMLqsaMLGVGAWLVIE 293
Cdd:cd18778 175 LGELNALLQDnlsgirEIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHplmEFLTSLGTVL---VLGFGGRLVLA 251
|
250
....*....|
gi 1555720989 294 GEATSGIIIA 303
Cdd:cd18778 252 GELTIGDLVA 261
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
378-422 |
2.77e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1555720989 378 VEFSLDAGSVLGIIGPSGSGKSSLVRGLVGAWRPLAGRIKLDGAA 422
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA 87
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
48-157 |
3.80e-03 |
|
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: 39.69 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 48 FAGVAVFSGVSNILMLTGAMFMLEVYDRVLPSRSVPT------LIAMAILAGALFAGQAVIDLVRGRIMNRIGAELDEAV 121
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1555720989 122 GGRVFTAVSRLPL-YIGQQ--GDGLQpqR---DLDNIRTFLS 157
Cdd:cd18547 81 RKDLFEKLQRLPLsYFDTHshGDIMS--RvtnDVDNISQALS 120
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
358-437 |
5.14e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1555720989 358 LTVERIAIGAPGAqriIVQGVEFSLDAGSVLGIIGPSGSGKSSLVRGLVGA----WRPLAGRIKLDGAALDQWSSERLGR 433
Cdd:PRK15093 9 LTIEFKTSDGWVK---AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRK 85
|
....
gi 1555720989 434 YIGY 437
Cdd:PRK15093 86 LVGH 89
|
|
| |
