|
Name |
Accession |
Description |
Interval |
E-value |
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-558 |
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: 830.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 16 LAASRGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQ 95
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 96 LHGRIYAAAFERNLRAGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALAWF 175
Cdd:TIGR01842 81 LNQPIFAASFSATLRRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 176 NERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLDQQSLASERAARINALSKYLRIALQS 255
Cdd:TIGR01842 161 NNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 256 LVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSGLLDEFPARERRMELPEPRGHLLLE 335
Cdd:TIGR01842 241 LVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPEPEGHLSVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 336 SLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQD 415
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAGTVAENIARFGE-VQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:TIGR01842 401 VELFPGTVAENIARFGEnADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 495 PNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAAL 558
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-564 |
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: 825.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 1 MARLgSSVTNEIKQALAASRGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEAL 80
Cdd:COG4618 1 MSRA-SAGRSELRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 81 RSFVLVRVSERFDGQLHGRIYAAAFERNLRAGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGL 160
Cdd:COG4618 80 RSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 161 LSLVGALALMALAWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLDQQSLASERAA 240
Cdd:COG4618 160 LALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 241 RINALSKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSGLLDEFPARE 320
Cdd:COG4618 240 GFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 321 RRMELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY 400
Cdd:COG4618 320 ERMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 401 ERETLGPRIGYLPQDIELFAGTVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALA 480
Cdd:COG4618 400 DREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 481 RALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAALNN 560
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLAR 559
|
....
gi 15596443 561 QRAA 564
Cdd:COG4618 560 PAAA 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-557 |
2.24e-122 |
|
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: 377.25 E-value: 2.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 14 QALAASRGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFD 93
Cdd:COG2274 149 RLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRID 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 94 GQLHGRIYA-------AAFERnlRAGGQEASQaLHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGA 166
Cdd:COG2274 229 LRLSSRFFRhllrlplSFFES--RSVGDLASR-FRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 167 LALMALAWFNERATRAplaKAGELSIKSGQLASN---NLRNAEVIEAMGMLGSMRGRWERLHQAFLDqqslASERAARIN 243
Cdd:COG2274 306 PLYVLLGLLFQPRLRR---LSREESEASAKRQSLlveTLRGIETIKALGAESRFRRRWENLLAKYLN----ARFKLRRLS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 244 ALSKYLRIALQSL----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSGLLD---EF 316
Cdd:COG2274 379 NLLSTLSGLLQQLatvaLLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDlppER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 317 PARERRMELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAE 396
Cdd:COG2274 459 EEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 397 IRQYERETLGPRIGYLPQDIELFAGTVAENIArFGEVQAD--KVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQR 474
Cdd:COG2274 539 LRQIDPASLRRQIGVVLQDVFLFSGTIRENIT-LGDPDATdeEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 475 QRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQV 554
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
...
gi 15596443 555 LAA 557
Cdd:COG2274 697 LAR 699
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
20-309 |
3.27e-114 |
|
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: 341.89 E-value: 3.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYAAAFERNL-RAGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALAWFNER 178
Cdd:cd18586 81 VFRAVLELPLeSRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 179 ATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLDQQSLASERAARINALSKYLRIALQSLVL 258
Cdd:cd18586 161 ATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLIL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 259 GLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
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 ... |
14-558 |
7.11e-95 |
|
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: 305.25 E-value: 7.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 14 QALAASRGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFD 93
Cdd:TIGR03375 140 STLKESWPLYRDVLIASLLINLLALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYFLDVAGKKAD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 94 GQLHGRIyaaaFERNLR--------AGGQEASQaLHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVg 165
Cdd:TIGR03375 220 LILSAKL----FERVLGlrmearpaSVGSFANQ-LREFESVRDFFTSATLTALIDLPFALLFLLVIAIIGGPLVWVPLV- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 166 ALALMALAWFnerATRAPLAKAGELSIKSGQLasnnlRNAEVIEAMGML---------GSMRGRWERLHqAFLDQqslAS 236
Cdd:TIGR03375 294 AIPLILLPGL---LLQRPLSRLAEESMRESAQ-----RNAVLVESLSGLetikalnaeGRFQRRWEQTV-AALAR---SG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 237 ERAARINALSKYLRIALQSL----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSGL 312
Cdd:TIGR03375 362 LKSRFLSNLATNFAQFIQQLvsvaIVVVGVYLISDGELTMGGLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQSLDEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 313 LD---EFPARERRMELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGS 389
Cdd:TIGR03375 442 MQlpvERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 390 VRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIArFGEVQADK--VVEAARLAGVHELVLRLPQGYDTVLGVGGA 467
Cdd:TIGR03375 522 VLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIA-LGAPYADDeeILRAAELAGVTEFVRRHPDGLDMQIGERGR 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 468 GLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHL 547
Cdd:TIGR03375 601 SLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVA 679
|
570
....*....|.
gi 15596443 548 YGERDQVLAAL 558
Cdd:TIGR03375 680 DGPKDQVLEAL 690
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-545 |
1.41e-86 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 280.13 E-value: 1.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 1 MARLGSSVTNEIKQALAASRGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEAL 80
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 81 RSFVLVRVSERFDGQLHGRIYA-------AAFERNlrAGGQEASQALHDLTTLRQFItGQALFAFFDAPWFPV-YLLVIF 152
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEhllrlplSFFDRR--RTGDLLSRLTNDVDAVEQFL-AHGLPQLVRSVVTLIgALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 153 LFDPWLGLLSLVGALALMALAWFNER----ATRAPLAKAGELSiksgQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAF 228
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRrlrkLFRRVQEALAELN----GRLQESLSGIRVVKAFGREERELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 229 LDQQSLASERAARINALSKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRR 308
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 309 LSGLLD---EFPARERRMELPEPRGHLLLESLDAAPPGSEaRTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPT 385
Cdd:COG1132 314 IFELLDeppEIPDPPGAVPLPPVRGEIEFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 386 LHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIaRFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLG 463
Cdd:COG1132 393 TSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI-RYGRPDAtdEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 464 VGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAG 543
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
..
gi 15596443 544 QL 545
Cdd:COG1132 551 RI 552
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
332-545 |
1.80e-67 |
|
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: 216.70 E-value: 1.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGY 411
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQDIELFAGTVAENIarfgevqadkvveaarLAGvhelvlrlpqgydtvlgvggaglsgGQRQRIALARALYGAPTLVV 491
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------LSG-------------------------GQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 492 LDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-556 |
5.53e-64 |
|
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: 222.70 E-value: 5.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 19 SRGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHG 98
Cdd:TIGR01846 137 YRKQFREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 99 RIYaaafeRNLRA------GGQEASQAL---HDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALAL 169
Cdd:TIGR01846 217 RLY-----RHLLGlplgyfESRRVGDTVarvRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 170 MALAWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWER-----LHQAFLDQQS--LASERAARI 242
Cdd:TIGR01846 292 ALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRqlaayVAASFRVTNLgnIAGQAIELI 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 243 NALSkylrialQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSGLLDE--FPARE 320
Cdd:TIGR01846 372 QKLT-------FAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSptEPRSA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 321 RRMELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY 400
Cdd:TIGR01846 445 GLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 401 ERETLGPRIGYLPQDIELFAGTVAENIArFGEVQAD--KVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIA 478
Cdd:TIGR01846 525 DPAWLRRQMGVVLQENVLFSRSIRDNIA-LCNPGAPfeHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIA 603
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 479 LARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREI-CRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
146-557 |
1.09e-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: 219.25 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 146 VYLLVIFLFDPWLGLLSLVG-ALALMALAWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERL 224
Cdd:COG4987 145 AAVAFLAFFSPALALVLALGlLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 225 HQAFLDQQslasERAARINALSKYLRIALQSL----VLGLGAWLAVEGRItPGMMIAGSILMGRALG-PIDQLIGVWKQW 299
Cdd:COG4987 225 EARLAAAQ----RRLARLSALAQALLQLAAGLavvaVLWLAAPLVAAGAL-SGPLLALLVLAALALFeALAPLPAAAQHL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 300 GAARDAYRRLSGLLDEFPA-RERRMELPEPRGHLL-LESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLAR 377
Cdd:COG4987 300 GRVRAAARRLNELLDAPPAvTEPAEPAPAPGGPSLeLEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 378 VVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAEN--IARfGEVQADKVVEAARLAGVHELVLRLP 455
Cdd:COG4987 380 LLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENlrLAR-PDATDEELWAALERVGLGDWLAALP 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 456 QGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCAD 535
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMD 537
|
410 420
....*....|....*....|..
gi 15596443 536 RLLALNAGQLHLYGERDQVLAA 557
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQ 559
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-557 |
5.47e-58 |
|
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: 203.84 E-value: 5.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 8 VTNEIKQALAASRGALRsVAAFSGVINLLMLVPSLYML--QVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVL 85
Cdd:COG4988 4 LDKRLKRLARGARRWLA-LAVLLGLLSGLLIIAQAWLLasLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 86 VRVSERFDGQLHGRIYAAAFERNLRAGGQEASQALHDLTT-----LRQFITG---QALFAFFdAPWfpVYLLVIFLFDPW 157
Cdd:COG4988 83 FRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTegveaLDGYFARylpQLFLAAL-VPL--LILVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 158 LGLLSLVGA----LALMALAWFNERATRAPLAKAGELSiksGQLAsnnlrnaEVIEAMGMLgsmrgrweRLHQAfldqqs 233
Cdd:COG4988 160 SGLILLVTAplipLFMILVGKGAAKASRRQWRALARLS---GHFL-------DRLRGLTTL--------KLFGR------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 234 lASERAARINALS--------KYLRIA-LQSLVLGLG-----AWLAVEGRITpgmMIAGSILMGRAL----------GPI 289
Cdd:COG4988 216 -AKAEAERIAEASedfrkrtmKVLRVAfLSSAVLEFFaslsiALVAVYIGFR---LLGGSLTLFAALfvlllapeffLPL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 290 DQLIGVWKQWGAARDAYRRLSGLLDEFPARERRMELPEPRG---HLLLESLDAAPPGsEARTLRGLTLAIPAGSVVGVIG 366
Cdd:COG4988 292 RDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAgppSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 367 PSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIaRFGEVQADK--VVEAARL 444
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL-RLGRPDASDeeLEAALEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 445 AGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLI 524
Cdd:COG4988 450 AGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|...
gi 15596443 525 THRAGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
342-545 |
1.52e-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: 181.63 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAG 421
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIArFGEVQAD--KVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:cd03245 93 TLRDNIT-LGAPLADdeRILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 500 DDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:cd03245 172 DMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
20-309 |
4.76e-50 |
|
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: 175.08 E-value: 4.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHgr 99
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 iyAAAFERNL--------RAGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMA 171
Cdd:cd18566 79 --NAAFEHLLslplsffeREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 172 LAWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLhqafLDQQSLASERAARINA----LSK 247
Cdd:cd18566 157 VAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERL----QANAAYAGFKVAKINAvaqtLGQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 248 YLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18566 233 LFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
147-544 |
6.67e-50 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 183.99 E-value: 6.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 147 YLLVIFLFDPWLGL----LSLVGALALMALAWFNERATRAPLAKAGelsiKSGQLASNNLRNAEVIEAMGMLGSMRGRWE 222
Cdd:TIGR03796 284 YALLMLLYDPVLTLigiaFAAINVLALQLVSRRRVDANRRLQQDAG----KLTGVAISGLQSIETLKASGLESDFFSRWA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 223 RLH-QAFLDQQSLASeRAARINALSKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGA 301
Cdd:TIGR03796 360 GYQaKLLNAQQELGV-LTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 302 ARDAYRRLS-------GLLDEFPARERRMELPEPR--GHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGK 372
Cdd:TIGR03796 439 LEGDLNRLDdvlrnpvDPLLEEPEGSAATSEPPRRlsGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 373 SSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIARFGEVQADK-VVEAARLAGVHELV 451
Cdd:TIGR03796 519 STIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDAdLVRACKDAAIHDVI 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 452 LRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLaaiQALKARGCTVLLITHRAGVL 531
Cdd:TIGR03796 599 TSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIID---DNLRRRGCTCIIVAHRLSTI 675
|
410
....*....|...
gi 15596443 532 GCADRLLALNAGQ 544
Cdd:TIGR03796 676 RDCDEIIVLERGK 688
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
349-556 |
4.60e-49 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 170.49 E-value: 4.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIa 428
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNI- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQA 506
Cdd:cd03253 96 RYGRPDAtdEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596443 507 LLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03253 176 IQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-544 |
4.14e-48 |
|
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: 165.63 E-value: 4.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 334 LESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLP 413
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QDIELFAGTVAENIarfgevqadkvveaarlagvhelvlrLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLD 493
Cdd:cd03228 83 QDPFLFSGTIRENI--------------------------LSGG---------------QRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 494 EPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQ 544
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
348-556 |
3.89e-47 |
|
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: 165.09 E-value: 3.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 348 TLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENI 427
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 aRFG--EVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQ 505
Cdd:cd03254 98 -RLGrpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 506 ALLAAIQALKaRGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03254 177 LIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
79-557 |
5.97e-46 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 170.65 E-value: 5.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 79 ALRSFVLVRVSERFDGQLHGRIYA-------AAFERNLraGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVI 151
Cdd:TIGR02204 76 AARFYLVTWLGERVVADIRRAVFAhlislspSFFDKNR--SGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMM 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 152 FLFDPWLGLLSLVGALALMALAWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLDQ 231
Cdd:TIGR02204 154 FITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 232 QSLASERAARINALSKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSG 311
Cdd:TIGR02204 234 ARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 312 LL---DEFPARERRMELPEP-RGHLLLESLDAAPPG-SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTL 386
Cdd:TIGR02204 314 LLqaePDIKAPAHPKTLPVPlRGEIEFEQVNFAYPArPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 387 HGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIaRFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLGV 464
Cdd:TIGR02204 394 SGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENI-RYGRPDAtdEEVEAAARAAHAHEFISALPEGYDTYLGE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 465 GGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKArGCTVLLITHRAGVLGCADRLLALNAGQ 544
Cdd:TIGR02204 473 RGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK-GRTTLIIAHRLATVLKADRIVVMDQGR 551
|
490
....*....|...
gi 15596443 545 LHLYGERDQVLAA 557
Cdd:TIGR02204 552 IVAQGTHAELIAK 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-557 |
3.12e-45 |
|
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: 160.09 E-value: 3.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAG 421
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIA--RFGEVQADkVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:cd03251 91 TVAENIAygRPGATREE-VEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 500 DDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:cd03251 170 DTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
146-557 |
1.13e-44 |
|
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: 167.20 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 146 VYLLVIFLFDPWLglLSLVGALALMALAWFNERATRAPLAKAGELSIKSGQL---ASNNLRNAEVIEAMGMLGSMRGRWE 222
Cdd:TIGR02203 143 IGLFIVLLYYSWQ--LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVttvAEETLQGYRVVKLFGGQAYETRRFD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 223 RLHQAFLDQQ-SLASERAARINALSKYLRIALqSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGA 301
Cdd:TIGR02203 221 AVSNRNRRLAmKMTSAGSISSPITQLIASLAL-AVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 302 ARDAYRRLSGLLDEFP-ARERRMELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVL 380
Cdd:TIGR02203 300 GLAAAESLFTLLDSPPeKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 381 GIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA--RFGEVQADKVVEAARLAGVHELVLRLPQGY 458
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAygRTEQADRAEIERALAAAYAQDFVDKLPLGL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 459 DTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKaRGCTVLLITHRAGVLGCADRLL 538
Cdd:TIGR02203 460 DTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEKADRIV 538
|
410
....*....|....*....
gi 15596443 539 ALNAGQLHLYGERDQVLAA 557
Cdd:TIGR02203 539 VMDDGRIVERGTHNELLAR 557
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
343-557 |
8.08e-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: 156.11 E-value: 8.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGT 422
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFGE-VQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDD 501
Cdd:cd03252 92 IRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 502 SGEQALLAAIQALKArGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
145-557 |
1.20e-43 |
|
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: 166.07 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 145 PVYLLVIFLFDPwlgllslvgalalmalawfneratraPLAKAGELSIKSGQ-LASNNLRNAEVIEAMGMLGSMRGRWER 223
Cdd:TIGR01193 306 PVYAVIIILFKR--------------------------TFNKLNHDAMQANAvLNSSIIEDLNGIETIKSLTSEAERYSK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 224 LHQAFLD--QQSLASERAARI-NALSKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWG 300
Cdd:TIGR01193 360 IDSEFGDylNKSFKYQKADQGqQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 301 AARDAYRRLSGLL---DEFPARERRMELPEPRGHLLLESLDAAPpGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLAR 377
Cdd:TIGR01193 440 AARVANNRLNEVYlvdSEFINKKKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 378 VVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENI---ARFGeVQADKVVEAARLAGVHELVLRL 454
Cdd:TIGR01193 519 LLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllgAKEN-VSQDEIWAACEIAEIKDDIENM 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 455 PQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARgcTVLLITHRAGVLGCA 534
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS 675
|
410 420
....*....|....*....|...
gi 15596443 535 DRLLALNAGQLHLYGERDQVLAA 557
Cdd:TIGR01193 676 DKIIVLDHGKIIEQGSHDELLDR 698
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-540 |
1.51e-43 |
|
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: 163.23 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRsVAAFSGVINLLMLVPSLYML-QVYDRVLSSANEVTLLMLTLMALGVFVFM-GALEALRSFVLVRVSERFDGQLH 97
Cdd:TIGR02857 2 RRALA-LLALLGVLGALLIIAQAWLLaRVVDGLISAGEPLAELLPALGALALVLLLrALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 98 GRIYAAAFERN-----LRAGGQEASQALHDLTTL----RQFITGQALFAFfdAPWfpVYLLVIFLFDpWLGLLSLVGALA 168
Cdd:TIGR02857 81 ERLLEAVAALGprwlqGRPSGELATLALEGVEALdgyfARYLPQLVLAVI--VPL--AILAAVFPQD-WISGLILLLTAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 169 L----MAL-AWFNERATRAPLAKAGELSiksGQLAsNNLRNAEVIEAMGMLGSMRGRWERLHQAFldqqslaSERAARIn 243
Cdd:TIGR02857 156 LipifMILiGWAAQAAARKQWAALSRLS---GHFL-DRLRGLPTLKLFGRAKAQAAAIRRSSEEY-------RERTMRV- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 244 alskyLRIA-LQSLVLGLGAWLAVEG-RITPGM-MIAGSILMGRAL----------GPIDQLIGVWKQWGAARDAYRRLS 310
Cdd:TIGR02857 224 -----LRIAfLSSAVLELFATLSVALvAVYIGFrLLAGDLDLATGLfvlllapefyLPLRQLGAQYHARADGVAAAEALF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 311 GLLD--EFPARERRMELPEPRGHLLLESLDAAPPGSEARtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHG 388
Cdd:TIGR02857 299 AVLDaaPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 389 SVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA-RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGA 467
Cdd:TIGR02857 378 SIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRlARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 468 GLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLAL 540
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
341-556 |
8.56e-40 |
|
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: 145.17 E-value: 8.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIE--L 418
Cdd:COG1122 11 PGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDdqL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIArFG---------EVQAdKVVEAARLAGVHEL----VLRLPQGydtvlgvggaglsggQRQRIALARALYG 485
Cdd:COG1122 89 FAPTVEEDVA-FGpenlglpreEIRE-RVEEALELVGLEHLadrpPHELSGG---------------QKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 486 APTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
149-527 |
2.09e-38 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 148.66 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 149 LVIFLFDPWLGLLSLVG-ALALMALAWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQA 227
Cdd:TIGR02868 146 AAIAVLSVPAALILAAGlLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 228 FLDqqslASERAARINALSKylriALQSLVLGLGAWLAV--------EGRITPgMMIAGSILMGRAL-GPIDQLIGVWKQ 298
Cdd:TIGR02868 226 LTR----AERRAAAATALGA----ALTLLAAGLAVLGALwaggpavaDGRLAP-VTLAVLVLLPLAAfEAFAALPAAAQQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 299 WGAARDAYRRLSGLLD-EFPARERRMELPEPRG----HLLLESLDAAPPGSeARTLRGLTLAIPAGSVVGVIGPSGSGKS 373
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDaAGPVAEGSAPAAGAVGlgkpTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 374 SLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAEN--IARfGEVQADKVVEAARLAGVHELV 451
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlrLAR-PDATDEELWAALERVGLADWL 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 452 LRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQAlKARGCTVLLITHR 527
Cdd:TIGR02868 455 RALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
349-556 |
2.89e-38 |
|
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: 141.14 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIa 428
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFG--EVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQA 506
Cdd:cd03249 98 RYGkpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596443 507 LLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03249 178 VQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
349-549 |
1.15e-36 |
|
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: 136.08 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15596443 509 AAIQAlKARGCTVLLITHR-AGVLGCaDRLLALNAGQLHLYG 549
Cdd:cd03244 180 KTIRE-AFKDCTVLTIAHRlDTIIDS-DRILVLDKGRVVEFD 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
146-572 |
1.42e-35 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 141.50 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 146 VYLLVIFLFDPWLGLLSLVgalALMALAWFNERATR---APLAKAGELSIKSGQLASNNLRNAEVIEAMGMlgsmrgrwE 222
Cdd:COG5265 169 VAGILLVKYDWWFALITLV---TVVLYIAFTVVVTEwrtKFRREMNEADSEANTRAVDSLLNYETVKYFGN--------E 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 223 RLHQAFLDQQSLASERAARINALSKYLRIALQSLVLGLG--------AWLAVEGRITPG--MMIaGSILMGRALgPIDQL 292
Cdd:COG5265 238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGltammlmaAQGVVAGTMTVGdfVLV-NAYLIQLYI-PLNFL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 293 IGVWKQWGAARDAYRRLSGLLDEFPA---RERRMELPEPRGHLLLE----SLDAAPPGseartLRGLTLAIPAGSVVGVI 365
Cdd:COG5265 316 GFVYREIRQALADMERMFDLLDQPPEvadAPDAPPLVVGGGEVRFEnvsfGYDPERPI-----LKGVSFEVPAGKTVAIV 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 366 GPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIArFGEVQA--DKVVEAAR 443
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIA-YGRPDAseEEVEAAAR 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 444 LAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLL 523
Cdd:COG5265 470 AAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLV 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 524 ITHRAGVLGCADRLLALNAGQLHLYGERDQVLAAlnNQRAAS--ASQQRAD 572
Cdd:COG5265 549 IAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ--GGLYAQmwARQQEEE 597
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
342-544 |
2.54e-35 |
|
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: 132.21 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIE--LF 419
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDdqFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AGTVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAP 487
Cdd:cd03225 90 GPTVEEEVA-FGlenlglpeEEIEERVEEALELVGLEGLRDRSPFtlsgG---------------QKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 488 TLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQ 544
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-545 |
4.40e-35 |
|
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: 131.82 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 339 AAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIEL 418
Cdd:cd03248 20 AYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIAR-FGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNS 497
Cdd:cd03248 100 FARSLQDNIAYgLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15596443 498 NLDDSGEQALLAAIQALKARGcTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERR-TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
349-563 |
4.49e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyeretLGPRIGYLPQDIEL---FAGTVAE 425
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVPQRAEVdwdFPITVRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIA-----------RFGEVQADKVVEAARLAGVHELVLR----LPQGydtvlgvggaglsggQRQRIALARALYGAPTLV 490
Cdd:COG1121 97 VVLmgrygrrglfrRPSRADREAVDEALERVGLEDLADRpigeLSGG---------------QQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH-RAGVLGCADRLLALNaGQLHLYGERDQVLAALNNQRA 563
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPENLSRA 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
349-555 |
6.08e-35 |
|
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: 132.47 E-value: 6.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIEL-FAGTVAENI 427
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 A--------RFGEVQAD---KVVEAARLAGVHELVLR----LPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:COG1120 97 AlgryphlgLFGRPSAEdreAVEEALERTGLEHLADRpvdeLSGG---------------ERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 493 DEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITH------RagvlgCADRLLALNAGQLHLYGERDQVL 555
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHdlnlaaR-----YADRLVLLKDGRIVAQGPPEEVL 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
252-556 |
1.09e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 139.47 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 252 ALQSLVLGLGAWLAVEGRITPGMMIagSILM-----GRALgpiDQLIGVWKQWGAARDAYRRLSGLLDEFPARERRMELP 326
Cdd:TIGR00958 397 LIQVLVLYYGGQLVLTGKVSSGNLV--SFLLyqeqlGEAV---RVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLA 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 327 EPRGHLLLESLD---AAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERE 403
Cdd:TIGR00958 472 PLNLEGLIEFQDvsfSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 404 TLGPRIGYLPQDIELFAGTVAENIArFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALAR 481
Cdd:TIGR00958 552 YLHRQVALVGQEPVLFSGSVRENIA-YGLTDTpdEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLaaiQALKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQ---ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
332-584 |
4.16e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.80 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP---TLHGSVRLDGAEIRQYERETLGPR 408
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 IGYLPQDIE--LFAGTVAENIARFGEVQA-------DKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIAL 479
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENLGlsraearARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 480 ARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260
....*....|....*....|....*..
gi 15596443 558 LNNQRAASASQQRADYRVAGYGAPQVV 584
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
251-556 |
7.72e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 135.92 E-value: 7.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 251 IALqSLVLGLGAWLAVEGRITPGM-------MIAgsiLMGralgPIDQLIGVWKQWGAARDAYRRLSGLLDEFPARER-R 322
Cdd:PRK11176 261 LAL-AFVLYAASFPSVMDTLTAGTitvvfssMIA---LMR----PLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEgK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 323 MELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYER 402
Cdd:PRK11176 333 RVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 403 ETLGPRIGYLPQDIELFAGTVAENI--ARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALA 480
Cdd:PRK11176 413 ASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIA 492
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 481 RALY-GAPTLvVLDEPNSNLDDSGEQALLAAIQAL-KARgcTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK11176 493 RALLrDSPIL-ILDEATSALDTESERAIQAALDELqKNR--TSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
349-549 |
2.13e-33 |
|
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: 126.88 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyeretLGPRIGYLPQDIEL---FAGTVAE 425
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQRRSIdrdFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIA-----------RFGEVQADKVVEAARLAGVHELVLR----LPQGydtvlgvggaglsggQRQRIALARALYGAPTLV 490
Cdd:cd03235 90 VVLmglyghkglfrRLSKADKAKVDEALERVGLSELADRqigeLSGG---------------QQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNaGQLHLYG 549
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLLN-RTVVASG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
349-558 |
2.66e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.10 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG-IWPTlHGSVRLDGAEIRQYERETLgPRIGYLPQDIELFAG-TVAEN 426
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRPT-SGEVRVLGEDVARDPAEVR-RRIGYVPQEPALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IARFGEV----------QADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEP 495
Cdd:COG1131 94 LRFFARLyglprkeareRIDELLELFGLTDAaDRKVGTLSGG---------------MKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 496 NSNLDDSGEQALLAAIQALKARGCTVLLITHragVLG----CADRLLALNAGQLHLYGERDQVLAAL 558
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTH---YLEeaerLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
20-309 |
3.27e-33 |
|
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: 128.78 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYA-------AAFERnlRAGGQEASQAlHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMAL 172
Cdd:cd18555 81 FFEhllklpySFFEN--RSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 173 AWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHqaflDQQSLASERAARINA----LSKY 248
Cdd:cd18555 158 LLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLF----KKQLKAFKKKERLSNilnsISSS 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 249 LRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
345-544 |
4.48e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.20 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQdielfagtva 424
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 eniarfgevqadkvveaarlagvhelvlrLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:cd00267 81 -----------------------------LSGG---------------QRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596443 505 QALLAAIQALKARGCTVLLITHRAGVLG-CADRLLALNAGQ 544
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
352-545 |
5.91e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 130.35 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPtLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIArFG 431
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVL-LG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 432 EVQAD--KVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLA 509
Cdd:PRK11174 447 NPDASdeQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190
....*....|....*....|....*....|....*.
gi 15596443 510 AIQALkARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK11174 527 ALNAA-SRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
349-545 |
3.02e-31 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 119.42 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyERETLGPRIGYLPQDIELFAG-TVAENi 427
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVREN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 arfgevqadkvveaarlagvhelvLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQAL 507
Cdd:cd03230 94 ------------------------LKLSGG---------------MKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596443 508 LAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQL 545
Cdd:cd03230 135 WELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
347-562 |
1.05e-30 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 120.35 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG-IWPTlHGSVRLDGAEIRQYERETLGpRIGYLPQDIELFAG-TVA 424
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPD-SGSILIDGEDVRKEPREARR-QIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIARFGEVQ----------ADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLD 493
Cdd:COG4555 93 ENIRYFAELYglfdeelkkrIEELIELLGLEEFlDRRVGELSTG---------------MKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGC-ADRLLALNAGQLHLYGERDQVLAALNNQR 562
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
349-537 |
1.31e-30 |
|
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: 118.74 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyERETLGPRIGYLPQDIELFAG-TVAENI 427
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 A--------RFGEVQADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:COG4133 97 RfwaalyglRADREAIDEALEAVGLAGLaDLPVRQLSAG---------------QKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596443 499 LDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRL 537
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
20-309 |
1.39e-30 |
|
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: 121.16 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IY------AAAFERNLRAGgqEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALA 173
Cdd:cd18782 81 IIdhllrlPLGFFDKRPVG--ELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 174 WFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLDQQSLASERAARINALSKYLRIAL 253
Cdd:cd18782 159 FLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 254 QSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18782 239 SLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
349-549 |
2.18e-30 |
|
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: 117.15 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFagtvaeNIA 428
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQALELL------GLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFgevqADKVVEaaRLAGvhelvlrlpqGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:cd03214 89 HL----ADRPFN--ELSG----------G---------------ERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596443 509 AAIQAL-KARGCTVLLITH---RAgvLGCADRLLALNAGQLHLYG 549
Cdd:cd03214 138 ELLRRLaRERGKTVVMVLHdlnLA--ARYADRVILLKDGRIVAQG 180
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
238-556 |
3.72e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.82 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 238 RAARINAL---SKYLRIALQSLV-LGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWK--QWGAArdAYRRLSG 311
Cdd:PRK10789 215 RVARIDARfdpTIYIAIGMANLLaIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNivERGSA--AYSRIRA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 312 LLDEFPARERRME-LPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSV 390
Cdd:PRK10789 293 MLAEAPVVKDGSEpVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 391 RLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA--RFGEVQADkVVEAARLAGVHELVLRLPQGYDTVLGVGGAG 468
Cdd:PRK10789 373 RFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIAlgRPDATQQE-IEHVARLASVHDDILRLPQGYDTEVGERGVM 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 469 LSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALkARGCTVLLITHRAGVLGCADRLLALNAGQLHLY 548
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
....*...
gi 15596443 549 GERDQVLA 556
Cdd:PRK10789 531 GNHDQLAQ 538
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
343-545 |
5.26e-30 |
|
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: 117.61 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLGPRIGYLPQDielf 419
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRRKEIQMVFQD---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AG-------TVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGyDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVL 492
Cdd:cd03257 91 PMsslnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAGVL-GCADRLLALNAGQL 545
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVaKIADRVAVMYAGKI 224
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
20-309 |
9.08e-30 |
|
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: 119.08 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVL-SSANE--------VTLlmltlmalgVFVFMGALEALRSFVLVRVSE 90
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVpNNAIEtlwvlaigVLI---------ALLFDFILKLLRAYFIDVAGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 91 RFDGQLHGRIyaaaFERNL--------RAGGQEASQaLHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLS 162
Cdd:cd18587 72 RADVILSSRL----FERVLglrlearpASVGSFANN-LREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 163 LVGALALMALAWFneraTRAPLAKAGELSIKSGQLasnnlRNA---------EVIEAMGMLGSMRGRWERLHQafldQQS 233
Cdd:cd18587 147 LVAIPLVLLYGLL----LQKPLRRLVEESMRESAQ-----KNAllveslsglETIKALGAEGRMQRRWEEAVA----ALA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 234 LASERAARINALSKYLRIALQSL----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18587 214 RSSLKSRLLSSSATNFAQFVQQLvtvaIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
12-557 |
6.69e-29 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.99 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 12 IKQALAASRGALRSVAAFSGVINLL-MLVPsLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSE 90
Cdd:TIGR03797 127 LRFALRGARRDLLAILAMGLLGTLLgMLVP-IATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLET 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 91 RFDGqlhgRIYAAAFER--NLRAG-------GQEASQALhDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLL 161
Cdd:TIGR03797 206 RMDA----SLQAAVWDRllRLPVSffrqystGDLASRAM-GISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 162 SLVGALALMA----LAWFNERATRAPLAKAGELSIKSGQLAS--NNLRNAEVIEAMgmlgsmRGRWERLhqaFLDQQSLA 235
Cdd:TIGR03797 281 AVALALVAIAvtlvLGLLQVRKERRLLELSGKISGLTVQLINgiSKLRVAGAENRA------FARWAKL---FSRQRKLE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 236 SeRAARINALSKYLRIALQSLVLGLGAWLAV----EGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSG 311
Cdd:TIGR03797 352 L-SAQRIENLLTVFNAVLPVLTSAALFAAAIsllgGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKP 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 312 LLDEFP-ARERRMELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSV 390
Cdd:TIGR03797 431 ILEALPeVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 391 RLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLS 470
Cdd:TIGR03797 511 FYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLS 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 471 GGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKArgcTVLLITHRAGVLGCADRLLALNAGQLHLYGE 550
Cdd:TIGR03797 591 GGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV---TRIVIAHRLSTIRNADRIYVLDAGRVVQQGT 667
|
....*..
gi 15596443 551 RDQVLAA 557
Cdd:TIGR03797 668 YDELMAR 674
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
349-545 |
8.07e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 8.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 -----RFGEVQADKVVEAARLAGVHELVL-----RLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:COG4619 96 fpfqlRERKFDRERALELLERLGLPPDILdkpveRLSGG---------------ERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15596443 499 LDDSGEQALLAAIQALKAR-GCTVLLITHRAGVLG-CADRLLALNAGQL 545
Cdd:COG4619 161 LDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
345-544 |
8.60e-29 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 112.67 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG-IWPTlHGSVRLDGAEIRQYERETLGPR--IGYLPQDIELFAG 421
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPD-SGSILIDGEDLTDLEDELPPLRrrIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArfgevqadkvveaarlagvhelvLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:cd03229 91 lTVLENIA-----------------------LGLSGG---------------QQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 501 DSGEQALLAAIQALKAR-GCTVLLITHR-AGVLGCADRLLALNAGQ 544
Cdd:cd03229 133 PITRREVRALLKSLQAQlGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
349-554 |
1.43e-28 |
|
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: 113.81 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLH-----GSVRLDGAEIR--QYERETLGPRIGYLPQDIELFAG 421
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIA--------RFGEVQADKVVEAARLAGVHELVLRLPQGYDtvlgvggagLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:cd03260 96 SIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKARgCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQV 554
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
332-556 |
1.93e-28 |
|
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: 113.30 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLGpr 408
Cdd:cd03224 1 LEVENLNAGYGKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPHERARAG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 IGYLPQDIELFAG-TVAENIaRFGEVQADKVVEAARLAGVHELVLRLPQ-----------GydtvlgvggaglsggQRQR 476
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENL-LLGAYARRRAKRKARLERVYELFPRLKErrkqlagtlsgG---------------EQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 477 IALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARfALEIADRAYVLERGRVVLEGTAAELL 220
|
.
gi 15596443 556 A 556
Cdd:cd03224 221 A 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
347-545 |
2.30e-28 |
|
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: 113.74 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIEL-------F 419
Cdd:COG1124 19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhprhtV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AGTVAE--NIARFGEVQAdKVVEAARLAGVHELVL-RLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:COG1124 99 DRILAEplRIHGLPDREE-RIAELLEQVGLPPSFLdRYPHqlsgG---------------QRQRVAIARALILEPELLLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAGVLGC-ADRLLALNAGQL 545
Cdd:COG1124 163 DEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-557 |
4.85e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.08 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY---ERETLGPRIGYLPQDIE 417
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 --LFAG-TVAENIARF--------GEVQADKVVEAARLAGVHELVL-RLP----QGydtvlgvggaglsggQRQRIALAR 481
Cdd:COG1123 353 ssLNPRmTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLAdRYPhelsGG---------------QRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-495 |
6.98e-28 |
|
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: 109.27 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAG-TVAENI 427
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 428 ARFGEVQA-DKVVEAARLAGVHELvLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:pfam00005 81 RLGLLLKGlSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
349-546 |
1.41e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEIRQYERETL----GPRIGYLPQDIELFAG-T 422
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPT-SGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLPElT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIA---RFGEVQA----DKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVV 491
Cdd:COG1136 103 ALENVAlplLLAGVSRkerrERARELLERVGLGDRLDHRPSqlsgG---------------QQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 492 LDEPNSNLD-DSGEQaLLAAIQAL-KARGCTVLLITHRAGVLGCADRLLALNAGQLH 546
Cdd:COG1136 168 ADEPTGNLDsKTGEE-VLELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
257-569 |
2.58e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 116.60 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 257 VLGLGAWLAVEGRITPGMMIA----GSILMGRalgpIDQLIGVWKQWGAARDAYRRLSGLLDEFPARERRMELPEP---R 329
Cdd:PRK13657 257 ILVLGAALVQKGQLRVGEVVAfvgfATLLIGR----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLgrvK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 330 GHLLLESLDAAPPGSeARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRI 409
Cdd:PRK13657 333 GAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 410 GYLPQDIELFAGTVAENIaRFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAP 487
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNI-RVGRPDAtdEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 488 TLVVLDEPNSNLDDSGEQALLAAIQALKaRGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQvLAALNNQRAASAS 567
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE-LVARGGRFAALLR 568
|
..
gi 15596443 568 QQ 569
Cdd:PRK13657 569 AQ 570
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
20-309 |
6.91e-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: 110.67 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYA-------AAFERnlRAGGQEASQaLHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMAL 172
Cdd:cd18588 81 LFRhllrlplSYFES--RQVGDTVAR-VRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 173 AWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLhqafLDQQSLASERAARINALSKYLRIA 252
Cdd:cd18588 158 SLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEEL----LARYVKASFKTANLSNLASQIVQL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 253 LQSL----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18588 234 IQKLttlaILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-556 |
7.07e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 109.06 E-value: 7.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLGprIGYLPQDIELFAG-TVA 424
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEIARLG--IGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENI----------------ARFGEV----QADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARAL 483
Cdd:cd03219 94 ENVmvaaqartgsglllarARREEReareRAEELLERVGLADLaDRPAGELSYG---------------QQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 484 YGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDvVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-549 |
7.50e-27 |
|
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: 107.40 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYErETLGPRIGYLPQDIELFAG 421
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIARfgevqadkvveaaRLAGvhelvlrlpqgydtvlgvggaglsgGQRQRIALARALYGAPTLVVLDEPNSNLDD 501
Cdd:cd03247 90 TLRNNLGR-------------RFSG-------------------------GERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15596443 502 SGEQALLAAI-QALKARgcTVLLITHRAGVLGCADRLLALNAGQLHLYG 549
Cdd:cd03247 132 ITERQLLSLIfEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
347-549 |
1.90e-26 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 107.11 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAEN 426
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IARFGEVQADKVVEAARlagVHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQA 506
Cdd:cd03369 102 LDPFDEYSDEEIYGALR---VSEGGLNLSQG---------------QRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596443 507 LLAAIQALKArGCTVLLITHRAGVLGCADRLLALNAGQLHLYG 549
Cdd:cd03369 164 IQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-544 |
2.13e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 106.78 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVrldgaeirqyereTLGPRIGYLPQDIELFA 420
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTVAENI---ARFGEVQADKVVEAARLagvhELVLR-LPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:cd03250 80 GTIRENIlfgKPFDEERYEKVIKACAL----EPDLEiLPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15596443 497 SNLDDSGEQALLA-AIQALKARGCTVLLITHRAGVLGCADRLLALNAGQ 544
Cdd:cd03250 156 SAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
349-545 |
3.34e-26 |
|
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: 106.81 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP----RIGYLPQDIELFAG-TV 423
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrrrHIGFVFQSFNLLPDlTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIA-------RFGEVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:cd03255 100 LENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSelsgG---------------QQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 493 DEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
345-549 |
4.48e-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: 106.06 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERetlgpRIGYLPQDIELFAG 421
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERR-----NIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPT 488
Cdd:cd03259 87 lTVAENIA-FGlklrgvpkAEIRARVRELLELVGLEGLLNRYPHelsgG---------------QQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 489 LVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITH-RAGVLGCADRLLALNAGQLHLYG 549
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
212-556 |
5.07e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.61 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 212 GMLGSMRGRWERLHQAFLDQQSlaseRAARINALSKYLRIALQSLVLGLGAWLA---VEGRITPGMMIAGSILMGRA--- 285
Cdd:PRK11160 217 GAEDRYRQQLEQTEQQWLAAQR----RQANLTGLSQALMILANGLTVVLMLWLAaggVGGNAQPGALIALFVFAALAafe 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 286 -LGPIDqliGVWKQWGAARDAYRRLSGLLD-----EFPARErrmELPEPRGHLLLESLDAAPPGSEARTLRGLTLAIPAG 359
Cdd:PRK11160 293 aLMPVA---GAFQHLGQVIASARRINEITEqkpevTFPTTS---TAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 360 SVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIaRFGEVQAD--K 437
Cdd:PRK11160 367 EKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNL-LLAAPNASdeA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 438 VVEAARLAGVHELvLRLPQGYDTVLGVGGAGLSGGQRQRIALARA-LYGAPtLVVLDEPNSNLDDSGEQALLAAIQALkA 516
Cdd:PRK11160 446 LIEVLQQVGLEKL-LEDDKGLNAWLGEGGRQLSGGEQRRLGIARAlLHDAP-LLLLDEPTEGLDAETERQILELLAEH-A 522
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15596443 517 RGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK11160 523 QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
347-546 |
7.12e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.42 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETlgpRIGYLPQDIE--LFAGTVA 424
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK---SIGYVMQDVDyqLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIaRFGEVQADKVVEAA----RLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:cd03226 91 EEL-LLGLKELDAGNEQAetvlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596443 501 DSGEQALLAAIQALKARGCTVLLITHRAGVLG-CADRLLALNAGQLH 546
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAkVCDRVLLLANGAIV 205
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
257-545 |
8.36e-26 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 111.90 E-value: 8.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 257 VLGLGAWLAVEGRITPGMMIA----GSILMGRalgpIDQLIGVWKQWGAARDAYRRLSGLLDEFPARERRM---ELPEPR 329
Cdd:TIGR01192 257 ILVIGTVLVIKGELSVGEVIAfigfANLLIGR----LDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPAdapELPNVK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 330 GHLLLESLDAAPPGSeARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRI 409
Cdd:TIGR01192 333 GAVEFRHITFEFANS-SQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 410 GYLPQDIELFAGTVAENIaRFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAP 487
Cdd:TIGR01192 412 ATVFQDAGLFNRSIRENI-RLGREGAtdEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNA 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 488 TLVVLDEPNSNLDDSGEQALLAAIQALKaRGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:TIGR01192 491 PILVLDEATSALDVETEARVKNAIDALR-KNRTTFIIAHRLSTVRNADLVLFLDQGRL 547
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
349-557 |
1.35e-25 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 105.45 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLGPRIGYLPQDIELFAG-TVA 424
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIA-------RFGEVQADKVV----EAARLAGVHELvlrLP----QGydtvlgvggaglsggQRQRIALARALYGAPTL 489
Cdd:COG1127 101 ENVAfplrehtDLSEAEIRELVleklELVGLPGAADK---MPselsGG---------------MRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELrDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
347-557 |
2.00e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 110.58 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAEN 426
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQA 506
Cdd:PRK10790 435 VTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 507 LLAAIQALKARgCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:PRK10790 515 IQQALAAVREH-TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
345-555 |
2.34e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 106.00 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG-IWPTlHGSVRLDGAEIRQYERETLGP---RIGYLPQDIE--L 418
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT-SGTVTIDGRDITAKKKKKLKDlrkKVGLVFQFPEhqL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIArFG---------EVQAdKVVEAARLAGVHELVL-----RLPQGydtvlgvggaglsggQRQRIALARALY 484
Cdd:TIGR04521 96 FEETVYKDIA-FGpknlglseeEAEE-RVKEALELVGLDEEYLerspfELSGG---------------QMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 485 GAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
349-556 |
7.73e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 103.35 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR---QYERETLGPRIGYLPQDIELFAG-TVA 424
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRRRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIA-------RFGE-VQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:cd03261 96 ENVAfplrehtRLSEeEIREIVLEKLEAVGLRGAEDLYPAelsgG---------------MKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-565 |
6.04e-24 |
|
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: 100.87 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrqyerETLGP---RIGYLPQDIELFAG-TVA 424
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPekrDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIArFG---------EVQAdKVVEAARLAGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03299 90 KNIA-YGlkkrkvdkkEIER-KVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 496 NSNLDDSGEQALLAAIQ-ALKARGCTVLLITH---RAGVLGcaDRLLALNAGQLHLYGERDQVLAALNNQRAAS 565
Cdd:cd03299 157 FSALDVRTKEKLREELKkIRKEFGVTVLHVTHdfeEAWALA--DKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
332-556 |
7.07e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 100.44 E-value: 7.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERETLGpr 408
Cdd:COG0410 4 LEVENLHAGYGGIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlppHRIARLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 IGYLPQDIELFAG-TVAENIARFGEVQADKVVEAARLAGVHEL--VL--RLPQ-------GydtvlgvggaglsggQRQR 476
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELfpRLkeRRRQragtlsgG---------------EQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 477 IALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARfALEIADRAYVLERGRIVLEGTAAELL 224
|
.
gi 15596443 556 A 556
Cdd:COG0410 225 A 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
341-551 |
9.28e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 99.74 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEIRQYERETLgP----RIGYLPQD 415
Cdd:COG2884 12 PGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEeRPT-SGQVLVNGQDLSRLKRREI-PylrrRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAG-TVAENIA------RFGEVQADKVVEAArLAGV------HELVLRLPQGydtvlgvggaglsggQRQRIALARA 482
Cdd:COG2884 88 FRLLPDrTVYENVAlplrvtGKSRKEIRRRVREV-LDLVglsdkaKALPHELSGG---------------EQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 483 LYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH-RAGVLGCADRLLALNAGQLHLYGER 551
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
345-549 |
3.05e-23 |
|
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: 98.12 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEREtlgpRIGYLPQDIELFAG-TV 423
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPEERGLYPKmKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIARFGEVQADKVVEAAR----------LAGVHELVLR-LPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRridewlerleLSEYANKRVEeLSKG---------------NQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYG 549
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
340-557 |
4.44e-23 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 98.04 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 340 APPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEIRQYERETLGP---RIGYLPQD 415
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT-SGSVLVDGTDLTLLSGKELRKarrRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAG-TVAENIARFGEVqaDKVVEAARLAGVHELvLRL------PQGYDTVLgvggaglSGGQRQRIALARALYGAPT 488
Cdd:cd03258 91 FNLLSSrTVFENVALPLEI--AGVPKAEIEERVLEL-LELvgledkADAYPAQL-------SGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 489 LVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVL-GCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
353-564 |
7.41e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 7.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 353 TLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERetlgPrIGYLPQDIELFAG-TVAENIA 428
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppAER----P-VSMLFQENNLFPHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 -------RFGEVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNS 497
Cdd:COG3840 94 lglrpglKLTAEQRAQVEQALERVGLAGLLDRLPGqlsgG---------------QRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 498 NLDDSGEQALLAAIQAL-KARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLAALNNQRAA 564
Cdd:COG3840 159 ALDPALRQEMLDLVDELcRERGLTVLMVTHDpEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
349-557 |
7.51e-23 |
|
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: 103.87 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:TIGR00957 1382 PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15596443 509 AAIQAlKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAA 557
Cdd:TIGR00957 1462 STIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
349-564 |
9.72e-23 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 99.76 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGprIGYLPQDIELFAG-TVAENI 427
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG--IAYVYQNYMLFPHkTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ArFG--------EVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:NF040840 94 A-FGlklrkvpkEEIERKVKEIMELLGISHLLHRKPR-----------TLSGGEQQRVALARALIIEPKLLLLDEPLSAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 500 DDSGEQALLAAIQALKAR-GCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLAALNNQRAA 564
Cdd:NF040840 162 DVQTRDELIREMKRWHREfGFTAIHVTHNfEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVA 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
349-545 |
1.28e-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: 99.40 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERetlgpRIGYLPQDIELFAG-TVA 424
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEKR-----NVGMVFQDYALFPHlTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIArFG--------EVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:COG3842 96 ENVA-FGlrmrgvpkAEIRARVAELLELVGLEGLADRYPHqlsgG---------------QQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 493 DEPNSNLDDS--GE-QALLAAIQalKARGCTVLLITH-RAGVLGCADRLLALNAGQL 545
Cdd:COG3842 160 DEPLSALDAKlrEEmREELRRLQ--RELGITFIYVTHdQEEALALADRIAVMNDGRI 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
341-526 |
1.31e-22 |
|
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: 96.16 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI-RQYERET--LGPRIGYLPQDIE 417
Cdd:TIGR02673 12 PGGVAA--LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnRLRGRQLplLRRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 LF-AGTVAENIARFGEVQADK-------VVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTL 489
Cdd:TIGR02673 90 LLpDRTVYENVALPLEVRGKKereiqrrVGAALRQVGLEHKADAFPE-----------QLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATH 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
349-526 |
1.36e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.47 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyeretLGPRIGYLPQDIELFA-GTVAENI 427
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDRGVVFQEPALLPwLTVLDNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ArFG--------EVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEP 495
Cdd:COG1116 102 A-LGlelrgvpkAERRERARELLELVGLAGFEDAYPHqlsgG---------------MRQRVAIARALANDPEVLLMDEP 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596443 496 NSNLDdsgE------QALLAAIqaLKARGCTVLLITH 526
Cdd:COG1116 166 FGALD---AltrerlQDELLRL--WQETGKTVLFVTH 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
349-542 |
3.26e-22 |
|
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: 95.23 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyeretLGPRIGYLPQDIELFA-GTVAENI 427
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRGYVFQQDALLPwLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ArFG-EVQ-------ADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03293 95 A-LGlELQgvpkaeaRERAEELLELVGLSGFENAYPHqlsgG---------------MRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15596443 496 NSNLDD---SGEQALLAAIqaLKARGCTVLLITH---RAGVLgcADRLLALNA 542
Cdd:cd03293 159 FSALDAltrEQLQEELLDI--WRETGKTVLLVTHdidEAVFL--ADRVVVLSA 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
349-555 |
4.04e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.95 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIEL-FAGTVAENI 427
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 A------RFGEVQADKVVEAA-RLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARAL-------YGAPTL 489
Cdd:COG4559 97 AlgraphGSSAAQDRQIVREAlALVGLAHLAGRSYQtlsgG---------------EQQRVQLARVLaqlwepvDGGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH----RAGVlgcADRLLALNAGQLHLYGERDQVL 555
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlnlAAQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
336-549 |
1.29e-21 |
|
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: 92.61 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 336 SLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG--IWPTLHGSVRLDGaeiRQYERETLGPRIGYLP 413
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLING---RPLDKRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QDIELFAG-TVAENIaRFgevqadkvveAARLAGvhelvlrLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:cd03213 89 QDDILHPTlTVRETL-MF----------AAKLRG-------LSGG---------------ERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITH--RAGVLGCADRLLALNAGQLHLYG 549
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
332-541 |
1.39e-21 |
|
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: 91.83 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEARtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPtlHGSVRLDGAEirqyeretlGPRIGY 411
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP--WGSGRIGMPE---------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQDIELFAGTVAEniarfgevqadkvveaarlagvhelVLRLPqgYDTVLGVGgaglsggQRQRIALARALYGAPTLVV 491
Cdd:cd03223 69 LPQRPYLPLGTLRE-------------------------QLIYP--WDDVLSGG-------EQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596443 492 LDEPNSNLDDSGEQALLaaiQALKARGCTVLLITHRAGVLGCADRLLALN 541
Cdd:cd03223 115 LDEATSALDEESEDRLY---QLLKELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-545 |
1.46e-21 |
|
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: 91.72 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG-IWPTlHGSVRLDGAEIrqyerETLGPRigylpqdielfagtvaeni 427
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlYKPD-SGEILVDGKEV-----SFASPR------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 arfgevqadkvveAARLAGVhELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQAL 507
Cdd:cd03216 71 -------------DARRAGI-AMVYQLSVG---------------ERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596443 508 LAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:cd03216 122 FKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
20-309 |
1.98e-21 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 94.92 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYAAAFERNLRAGGQEAS----QALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALAWF 175
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTgdllMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 176 NERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLdQQSLASER-AARINALSKYLRIALQ 254
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQL-NASLRRGRlDALVDALLATLRLAAP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 255 SLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18779 240 LVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
343-556 |
2.20e-21 |
|
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: 93.52 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVV--LgIWPTlHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFA 420
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrL-IEPT-SGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENIARFGEVQadKVVEAARLAGVHELvLRL----PQGYdtvLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03295 89 HmTVEENIALVPKLL--KWPKEKIRERADEL-LALvgldPAEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 496 NSNLDDSGEQALLAAIQALKAR-GCTVLLITH---RAGVLGcaDRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQElGKTIVFVTHdidEAFRLA--DRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-568 |
2.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.03 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDI--EL 418
Cdd:PRK13647 15 KDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIArFGEVQA--------DKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLV 490
Cdd:PRK13647 93 FSSTVWDDVA-FGPVNMgldkdeveRRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGER----DQVLAALNNQRAAS 565
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKslltDEDIVEQAGLRLPL 240
|
...
gi 15596443 566 ASQ 568
Cdd:PRK13647 241 VAQ 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
341-556 |
2.73e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPgsearTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFA 420
Cdd:PLN03232 1249 PP-----VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 501 DSGEQALLAAIQAlKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PLN03232 1404 VRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-556 |
5.31e-21 |
|
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: 92.79 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLGprIGYLPQDIELFAG-TVA 424
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARLG--IARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENI-----ARFGEV--------------------QADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIA 478
Cdd:COG0411 98 ENVlvaahARLGRGllaallrlprarreereareRAEELLERVGLADRaDEPAGNLSYG---------------QQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 479 LARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDlVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
349-540 |
5.97e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyeretlGPRIGYLPQDIEL---FAGTVAE 425
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIA--RFGEVQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSG 503
Cdd:NF040873 77 LVAmgRWARRGLWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596443 504 EQALLAAIQALKARGCTVLLITHRAGVLGCADRLLAL 540
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
349-556 |
8.43e-21 |
|
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: 91.45 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERETLGprIGYLPQDIELFAG-TVA 424
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRARLG--IGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIARFGEVQadKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:cd03218 94 ENILAVLEIR--GLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15596443 505 QALLAAIQALKARGCTVLLITHRA-GVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:cd03218 170 QDIQKIIKILKDRGIGVLITDHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
349-545 |
8.90e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.06 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEIRQY----ERetlgpRIGYLPQDIELFAG-T 422
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLeTPD-SGRIVLNGRDLFTNlpprER-----RVGFVFQHYALFPHmT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIArFGeVQADKVVEAARLAGVHELvLRLPQ--------------GydtvlgvggaglsggQRQRIALARALYGAPT 488
Cdd:COG1118 92 VAENIA-FG-LRVRPPSKAEIRARVEEL-LELVQlegladrypsqlsgG---------------QRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 489 LVVLDEPNSNLDDSGEQAL---LAAIqaLKARGCTVLLITH-RAGVLGCADRLLALNAGQL 545
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELrrwLRRL--HDELGGTTVFVTHdQEEALELADRVVVMNQGRI 212
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
20-309 |
9.85e-21 |
|
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: 92.62 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYAAAFERNLRAggqEASQALHDLTT-------LRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMAL 172
Cdd:cd18568 81 FYKHLLSLPLSF---FASRKVGDIITrfqenqkIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 173 AwfnerATRAPLAKAGELSIKSGQLASNN-----LRNAEVIEAMGMLGSMRGRWERLHQAFLDQQSLASERAARINALSK 247
Cdd:cd18568 158 T-----LLSSPKLKRNSREIFQANAEQQSflveaLTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 248 YLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18568 233 LINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
307-544 |
1.19e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 307 RRLSGL------LDEFPARERRMELPEPrGHLLLESLDAAPPGSEARtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVL 380
Cdd:COG4178 333 DRLAGFeealeaADALPEAASRIETSED-GALALEDLTLRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 381 GIWPTLHGSVRLDGAEirqyeretlgpRIGYLPQDIELFAGTVAENIARFGEVQA---DKVVEAARLAGVHELVLRLPQG 457
Cdd:COG4178 411 GLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALLYPATAEAfsdAELREALEAVGLGHLAERLDEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 458 YD--TVLGVGgaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQAlKARGCTVLLITHRAGVLGCAD 535
Cdd:COG4178 480 ADwdQVLSLG-------EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHD 551
|
....*....
gi 15596443 536 RLLALNAGQ 544
Cdd:COG4178 552 RVLELTGDG 560
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-549 |
1.47e-20 |
|
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: 90.50 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGpRIGYLPQDIELFA 420
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENIARFGEVQADKVVEAarLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:cd03266 92 RlTARENLEYFAGLYGLKGDEL--TARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 500 DDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYG 549
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
349-555 |
1.94e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIEL-FAGTVAENI 427
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 A------RFGEVQADKVVEAA-RLAGVHELVLRL-PQ---GydtvlgvggaglsggQRQRIALARAL------YGAPTLV 490
Cdd:PRK13548 98 AmgraphGLSRAEDDALVAAAlAQVDLAHLAGRDyPQlsgG---------------EQQRVQLARVLaqlwepDGPPRWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRagvLGCA----DRLLALNAGQLHLYGERDQVL 555
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHD---LNLAaryaDRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-545 |
2.01e-20 |
|
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: 90.01 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 348 TLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDG---AEIRQYEREtlgprIGYLPQDIELFAG-TV 423
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPPKDRD-----IAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIA------RFGEVQAD-KVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:cd03301 90 YDNIAfglklrKVPKDEIDeRVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 497 SNLDDSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQL 545
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-562 |
2.45e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEREtlgpRIGYLPQDIELFAG-TVAENI 427
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIGYLPEERGLYPKmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ARFGE----------VQADKVVEAARLAG-----VHELVLRlpqgydtvlgvggaglsggQRQRIALARALYGAPTLVVL 492
Cdd:COG4152 93 VYLARlkglskaeakRRADEWLERLGLGDrankkVEELSKG-------------------NQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLAALNNQR 562
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNT 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-549 |
3.02e-20 |
|
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: 89.28 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP----RIGYLPQDIELFAG-TVAENIArFGev 433
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYALFPHlNVRENLA-FG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 434 qADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQA 513
Cdd:cd03297 100 -LKRKRNREDRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596443 514 LKAR-GCTVLLITHRAG-VLGCADRLLALNAGQLHLYG 549
Cdd:cd03297 177 IKKNlNIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
346-554 |
3.77e-20 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 89.71 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 346 ARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY---EREtlgprIGYLPQDIELFAG- 421
Cdd:cd03296 15 FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqERN-----VGFVFQHYALFRHm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIArFG-EVQ--ADKVVEAARLAGVHELvLRLPQgYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:cd03296 90 TVFDNVA-FGlRVKprSERPPEAEIRAKVHEL-LKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 499 LDDSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQLHLYGERDQV 554
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDElHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-557 |
4.43e-20 |
|
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: 91.27 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP---TLHGSVRLDGAEIRQYERETL----GPRIGYLPQ 414
Cdd:COG0444 14 RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELrkirGREIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 415 DielfAGT-----------VAENIARFGEVQA----DKVVEAARLAGVHELVLRLPQ-------Gydtvlgvggaglsgg 472
Cdd:COG0444 94 D----PMTslnpvmtvgdqIAEPLRIHGGLSKaearERAIELLERVGLPDPERRLDRyphelsgG--------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 473 QRQRIALARALYGAPTLVVLDEPNSNLDDSgEQA----LLAAIQalKARGCTVLLITHRAGVL-GCADRLLALNAGQLHL 547
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVT-IQAqilnLLKDLQ--RELGLAILFITHDLGVVaEIADRVAVMYAGRIVE 231
|
250
....*....|
gi 15596443 548 YGERDQVLAA 557
Cdd:COG0444 232 EGPVEELFEN 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-526 |
4.92e-20 |
|
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: 89.00 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERET---LGPRIGYLPQDIE 417
Cdd:cd03292 11 PNGTAA--LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 LFAG-TVAENIARFGEVQ-------ADKVVEAARLAGV----HELVLRLPQGydtvlgvggaglsggQRQRIALARALYG 485
Cdd:cd03292 89 LLPDrNVYENVAFALEVTgvppreiRKRVPAALELVGLshkhRALPAELSGG---------------EQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596443 486 APTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
349-549 |
7.83e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 88.33 E-value: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRqYERETLGPRIGYLPQDIELFAG-TVAENI 427
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDElTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ARFGEVQADKVVEAARLAGVHELVLRLPQGYDTvlgvGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQAL 507
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVELLLRVLGLTDKANK----RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596443 508 LAAIQALKaRGCTVLLITH---RAGVLgcADRLLALNAGQLHLYG 549
Cdd:cd03263 173 WDLILEVR-KGRSIILTTHsmdEAEAL--CDRIAIMSDGKLRCIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-527 |
8.30e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyeretLGPR------IGYLPQD 415
Cdd:COG1129 15 GGVKA--LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF-----RSPRdaqaagIAIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAG-TVAENI------ARFGEVQADKVVEAAR--LAGV------HELVLRLPQGydtvlgvggaglsggQRQRIALA 480
Cdd:COG1129 88 LNLVPNlSVAENIflgrepRRGGLIDWRAMRRRARelLARLgldidpDTPVGDLSVA---------------QQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596443 481 RALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHR 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
349-545 |
8.89e-20 |
|
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: 87.97 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERE--TLGPRIGYLPQDIELFAG-TVAE 425
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIArFGEVQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQ 505
Cdd:cd03262 96 NIT-LAPIKVKGMSKAEAEERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596443 506 ALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:cd03262 173 EVLDVMKDLAEEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
332-554 |
9.00e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 88.35 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLGpr 408
Cdd:TIGR03410 1 LEVSNLNVYYGQSHI--LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklPPHERARAG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 IGYLPQDIELFAG-TVAENIARFGEVQADKvvEAARLAGVHEL--VLRlpqgydTVLGVGGAGLSGGQRQRIALARALYG 485
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENLLTGLAALPRR--SRKIPDEIYELfpVLK------EMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 486 APTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQV 554
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
345-545 |
9.94e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.90 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrqyerETLGPR---IGYLPQDIELF-A 420
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKdrnIAMVFQSYALYpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPT 488
Cdd:COG3839 90 MTVYENIA-FPlklrkvpkAEIDRRVREAAELLGLEDLLDRKPKqlsgG---------------QRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 489 LVVLDEPNSNLDdsgeqALL-----AAIQAL-KARGCTVLLITHR---AgvLGCADRLLALNAGQL 545
Cdd:COG3839 154 VFLLDEPLSNLD-----AKLrvemrAEIKRLhRRLGTTTIYVTHDqveA--MTLADRIAVMNDGRI 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-571 |
1.20e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 90.93 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 354 LAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP----RIGYLPQDIELFAG-TVAENIa 428
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRIGYVFQEARLFPHlSVRGNL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHEL----------VLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:COG4148 99 LYGRKRAPRAERRISFDEVVELlgighlldrrPATLSGG---------------ERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 499 LDDSGEQALLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLAALNNQRAASASQQRA 571
Cdd:COG4148 164 LDLARKAEILPYLERLRDElDIPILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGS 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
349-562 |
1.32e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.23 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDG-------AEIRQYERETlgpriGYLPQDIELFAG 421
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkVDERLIRQEA-----GMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVA-ENIArFGEVQ---ADKVvEAARLAgvHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNS 497
Cdd:PRK09493 92 LTAlENVM-FGPLRvrgASKE-EAEKQA--RELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 498 NLDDSGEQALLAAIQALKARGCTVLLITHRAGVL-GCADRLLALNAGQLHLYGERDQVLAALNNQR 562
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIKNPPSQR 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
349-554 |
1.70e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 88.19 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETL---GPRIGYLPQDIELFAG-TVA 424
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRIGMIFQQFNLVPRlSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 EN--IARFGEV-----------QADKVVEAARLAGV------HELVLRLPQGydtvlgvggaglsggQRQRIALARALYG 485
Cdd:COG3638 99 TNvlAGRLGRTstwrsllglfpPEDRERALEALERVgladkaYQRADQLSGG---------------QQQRVAIARALVQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 486 APTLVVLDEPNSNLD-DSGEQ--ALLAAIQalKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQV 554
Cdd:COG3638 164 EPKLILADEPVASLDpKTARQvmDLLRRIA--REDGITVVVNLHQVDlARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-556 |
2.51e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.53 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGA--------EIRQyeretlgpRIGYLP 413
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRR--------QVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 Q--DIELFAGTVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARAL 483
Cdd:PRK13635 88 QnpDNQFVGATVQDDVA-FGlenigvprEEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 484 YGAPTLVVLDEPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
347-549 |
2.88e-19 |
|
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: 86.48 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGsVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYeRETLGPRIGYLPQDIELFAG-TVAE 425
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQEFGVYPNfTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 ---NIARFGEV-------QADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDE 494
Cdd:cd03264 92 fldYIAWLKGIpskevkaRVDEVLELVNLGDRaKKKIGSLSGG---------------MRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 495 PNSNLDDSGEQALLAAIQALkARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYG 549
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
20-294 |
3.52e-19 |
|
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: 88.34 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYA-------AAFERNlRAGgqEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMAL 172
Cdd:cd18783 81 TFDrllslpiDFFERT-PAG--VLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 173 AWFNERATRAPLAKAGELSIKSGQLASNNLRNAEVIEAMGMLGSMRGRWERLhqafLDQQSLASERAARINALSKYLRIA 252
Cdd:cd18783 158 ILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDER----VARAIRARFAVGRLSNWPQTLTGP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15596443 253 LQSL----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIG 294
Cdd:cd18783 234 LEKLmtvgVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAG 279
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
343-543 |
4.92e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 86.23 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPR----IGYLPQDIEL 418
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENI---ARFGEVQADKVVEAARLAGVHELvlrLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03290 91 LNATVEENItfgSPFNKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596443 496 NSNLDDSGEQALLAA--IQALKARGCTVLLITHRAGVLGCADRLLALNAG 543
Cdd:cd03290 168 FSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
349-555 |
5.89e-19 |
|
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: 86.68 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG-IWPTLHGSVRLDGaeiRQYERET---LGPRIGY----LPQDIElfA 420
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFG---ERRGGEDvweLRKRIGLvspaLQLRFP--R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTVAENI---ARFG---------EVQADKVVEAARLAGVHEL----VLRLPQGydtvlgvggaglsggQRQRIALARALY 484
Cdd:COG1119 94 DETVLDVvlsGFFDsiglyreptDEQRERARELLELLGLAHLadrpFGTLSQG---------------EQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 485 GAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
349-526 |
1.55e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.06 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEI--------RQYERetlgpRIGYLPQDIELF 419
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLeRPT-SGSVLVDGVDLtalserelRAARR-----KIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AG-TVAENIARFGEVQadKVVEAARLAGVHELvLRL----------PQ----GydtvlgvggaglsggQRQRIALARALY 484
Cdd:COG1135 95 SSrTVAENVALPLEIA--GVPKAEIRKRVAEL-LELvglsdkadayPSqlsgG---------------QKQRVGIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596443 485 GAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITH 526
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH 199
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
347-546 |
1.56e-18 |
|
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: 84.71 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR---QYERETLGPR-IGYLPQDIELFAG- 421
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSklsSNERAKLRNKkLGFIYQFHHLLPDf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIARFGEVQADKVVEAARLAgvHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDD 501
Cdd:TIGR02211 99 TALENVAMPLLIGKKSVKEAKERA--YEMLEKV--GLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 502 SGEQALLAAIQAL-KARGCTVLLITHRAGVLGCADRLLALNAGQLH 546
Cdd:TIGR02211 175 NNAKIIFDLMLELnRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
354-545 |
1.67e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.53 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 354 LAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YEREtlgprIGYLPQDIELFAG-TVAENIA- 428
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlapYQRP-----VSMLFQENNLFAHlTVRQNIGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 ------RFGEVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:TIGR01277 94 glhpglKLNAEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596443 503 GEQALLAAIQAL-KARGCTVLLITHR-AGVLGCADRLLALNAGQL 545
Cdd:TIGR01277 163 LREEMLALVKQLcSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
349-556 |
1.78e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.80 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLdDSGEQALL 508
Cdd:PLN03130 1335 PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV-DVRTDALI 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15596443 509 AAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PLN03130 1414 QKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
347-545 |
4.35e-18 |
|
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: 83.04 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrQYERETLGpRIGYLPQDIELFAG-TVAE 425
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALR-RIGALIEAPGFYPNlTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 N------IARFGEVQADKVVEAARLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:cd03268 92 NlrllarLLGIRKKRIDEVLDVVGLKDSaKKKVKGFSLG---------------MKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15596443 499 LDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSeIQKVADRIGIINKGKL 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
349-570 |
4.49e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyeretlGPRIGYLPQDIELFAG-TVAENI 427
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 AR-FGEVQ-------------ADKVVEAARLAGVHELVLRLpQGYD------TVLGVGGAGLSGGQRQ----------RI 477
Cdd:COG0488 83 LDgDAELRaleaeleeleaklAEPDEDLERLAELQEEFEAL-GGWEaearaeEILSGLGFPEEDLDRPvselsggwrrRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 478 ALARALYGAPTLVVLDEPNSNLDdsgeqalLAAI----QALKARGCTVLLITH-RAGVLGCADRLLALNAGQLHLYG--- 549
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLD-------LESIewleEFLKNYPGTVLVVSHdRYFLDRVATRILELDRGKLTLYPgny 234
|
250 260
....*....|....*....|....*.
gi 15596443 550 -----ERDQVLAAlnnQRAASASQQR 570
Cdd:COG0488 235 sayleQRAERLEQ---EAAAYAKQQK 257
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
349-545 |
6.44e-18 |
|
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: 83.06 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERetlgpRIGYLPQDIELFAG-TVA 424
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKR-----PVNTVFQNYALFPHlTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIArFG--------EVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:cd03300 91 ENIA-FGlrlkklpkAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 497 SNLDDSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQL 545
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKI 209
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
354-541 |
6.56e-18 |
|
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: 82.98 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 354 LAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEREtlgprIGYLPQDIEL-------FAGTVAEN 426
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-----IGYVPQRHEFawdfpisVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IA-------RFGEVQADKVVEAARLAGVHELVLRlPQGydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:TIGR03771 76 RTghigwlrRPCVADFAAVRDALRRVGLTELADR-PVG----------ELSGGQRQRVLVARALATRPSVLLLDEPFTGL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596443 500 DDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALN 541
Cdd:TIGR03771 145 DMPTQELLTELFIELAGAGTAILMTTHDlAQAMATCDRVVLLN 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
344-545 |
6.72e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 6.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIE-LFAGT 422
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFG--------EVQADKVVEAARLAGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:PRK13642 98 TVEDDVAFGmenqgiprEEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596443 495 PNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
356-558 |
8.26e-18 |
|
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: 83.42 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 356 IPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIARFGEVQA 435
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 436 DKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQ-AL 514
Cdd:cd03288 124 DRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMtAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 515 KARgcTVLLITHRAGVLGCADRLLALNAGQL-------HLYGERDQVLAAL 558
Cdd:cd03288 204 ADR--TVVTIAHRVSTILDADLVLVLSRGILvecdtpeNLLAQEDGVFASL 252
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-559 |
2.10e-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: 84.01 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP----RIGYLPQDIELFAG-TVAEN 426
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IaRFGEVQADKVVEAARLAGVHELVlrlpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQA 506
Cdd:TIGR02142 96 L-RYGMKRARPSERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 507 LLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLAALN 559
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
349-526 |
2.41e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.99 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP---TLHGSVRLDGAEIrqyereTLGP----RIGYLPQDIELFAG 421
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRL------TALPaeqrRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArFG----------EVQADKVVEAARLAGVHElvlRLPQ----GydtvlgvggaglsggQRQRIALARALYGA 486
Cdd:COG4136 91 lSVGENLA-FAlpptigraqrRARVEQALEEAGLAGFAD---RDPAtlsgG---------------QRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596443 487 PTLVVLDEPNSNLDdsgeQALLAAI-----QALKARGCTVLLITH 526
Cdd:COG4136 152 PRALLLDEPFSKLD----AALRAQFrefvfEQIRQRGIPALLVTH 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
344-592 |
3.84e-17 |
|
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: 85.77 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAeirqyeretlgprIGYLPQDIELFAGTV 423
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIArFG----EVQADKVVEAARLAGVHELvlrLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:TIGR00957 716 RENIL-FGkalnEKYYQQVLEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 500 DDSGEQALLAAIQALKA--RGCTVLLITHRAGVLGCADRLLALNAGQLHLYG------ERDQVLAALNNQRAASASQQRA 571
Cdd:TIGR00957 792 DAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGsyqellQRDGAFAEFLRTYAPDEQQGHL 871
|
250 260
....*....|....*....|..
gi 15596443 572 -DYRVAGYGAPQVVAAPRQGGV 592
Cdd:TIGR00957 872 eDSWTALVSGEGKEAKLIENGM 893
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
347-557 |
3.92e-17 |
|
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: 84.74 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTlHGSVRLDGAEIRQYERETLGPrigyLPQDIEL-----FAG 421
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRP----LRRRMQVvfqdpFGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -----TVAENIARFGEVQADKVVEAARLAGVHELV----------LRLPQ----GydtvlgvggaglsggQRQRIALARA 482
Cdd:COG4172 375 lsprmTVGQIIAEGLRVHGPGLSAAERRARVAEALeevgldpaarHRYPHefsgG---------------QRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 483 LYGAPTLVVLDEPNSNLDDSgEQA----LLAAIQalKARGCTVLLITH-----RAgvlgCADRLLALNAGQLHLYGERDQ 553
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVS-VQAqildLLRDLQ--REHGLAYLFISHdlavvRA----LAHRVMVMKDGKVVEQGPTEQ 512
|
....
gi 15596443 554 VLAA 557
Cdd:COG4172 513 VFDA 516
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
342-555 |
3.99e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.58 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQ--DIELF 419
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQnpDNQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AGTVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVV 491
Cdd:PRK13632 98 GATVEDDIA-FGlenkkvppKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 492 LDEPNSNLDDSGEQALLAAIQALKARGC-TVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
349-562 |
4.46e-17 |
|
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: 81.83 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyeretlgpRIGYLPQDIELFAGTVAENIA 428
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 rFG----EVQADKVVEAARLagvHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:cd03291 120 -FGvsydEYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 505 QAL----LAAIQALKARgctvLLITHRAGVLGCADRLLALNAGQLHLYGerdqVLAALNNQR 562
Cdd:cd03291 196 KEIfescVCKLMANKTR----ILVTSKMEHLKKADKILILHEGSSYFYG----TFSELQSLR 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-543 |
6.55e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 318 ARERRMELPEPRGHLLLESLDAAPPGSEART----------------LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG 381
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAKASIPGSMSTVaidlagvsksygdkavVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 382 IWPTLHGSVRLDGAEIRQYERETLGpRIGYLPQ----DIELfagTVAENIARFG--------EVQA--DKVVEAARL-AG 446
Cdd:PRK13536 90 MTSPDAGKITVLGVPVPARARLARA-RIGVVPQfdnlDLEF---TVRENLLVFGryfgmstrEIEAviPSLLEFARLeSK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 447 VHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:PRK13536 166 ADARVSDLSGG---------------MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
250 260
....*....|....*....|
gi 15596443 527 ---RAGVLgcADRLLALNAG 543
Cdd:PRK13536 231 fmeEAERL--CDRLCVLEAG 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
349-554 |
6.84e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSL-------------ARVvlgiwptlHGSVRLDGAEI--RQYERETLGPRIGYLP 413
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLlrclnrmndlipgARV--------EGEILLDGEDIydPDVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QDIELFAGTVAENIArFG--------EVQADKVVEAA-RLAGV--------HELVLRLPQGydtvlgvggaglsggQRQR 476
Cdd:COG1117 99 QKPNPFPKSIYDNVA-YGlrlhgiksKSELDEIVEESlRKAALwdevkdrlKKSALGLSGG---------------QQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 477 IALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARgCTVLLITH------RagvlgCADRLLALNAGQLHLYGE 550
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHnmqqaaR-----VSDYTAFFYLGELVEFGP 236
|
....
gi 15596443 551 RDQV 554
Cdd:COG1117 237 TEQI 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
349-554 |
7.73e-17 |
|
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: 80.30 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP---RIGYLPQDIELFAG-TVA 424
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQIGMIFQQFNLIERlSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENI--ARFGEV-----------QADKVVEAARLAGVhelvlrlpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVV 491
Cdd:cd03256 97 ENVlsGRLGRRstwrslfglfpKEEKQRALAALERV---------GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 492 LDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGV-LGCADRLLALNAGQLHLYGERDQV 554
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
352-526 |
1.06e-16 |
|
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: 79.07 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrqyerETLGPR---IGYLPQDIELFAG-TVAENI 427
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-----TAAPPAdrpVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 A-------RFGEVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:cd03298 92 GlglspglKLTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180
....*....|....*....|....*..
gi 15596443 501 DSGEQALLAAIQALKA-RGCTVLLITH 526
Cdd:cd03298 161 PALRAEMLDLVLDLHAeTKMTVLMVTH 187
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
352-557 |
1.12e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYL------PQDIelfagTVAE 425
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLaqnattPGDI-----TVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIA-----------RFGEVQADKVVEAARLAGVHELVLrlpQGYDTVlgvggaglSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:PRK10253 101 LVArgryphqplftRWRKEDEEAVTKAMQATGITHLAD---QSVDTL--------SGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 495 PNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGvLGC--ADRLLALNAGQLHLYGERDQVLAA 557
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLN-QACryASHLIALREGKIVAQGAPKEIVTA 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
313-548 |
1.38e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 313 LDEFPARERRMEL----PEPRGHLLLEsLDAAPPGSEARTL-RGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLH 387
Cdd:COG0488 291 REEPPRRDKTVEIrfppPERLGKKVLE-LEGLSKSYGDKTLlDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 388 GSVRLdGaeirqyerETLgpRIGYLPQDIELFAG--TVAENIARFGEvqADKVVEAARLAG--------VHELVLRLPQG 457
Cdd:COG0488 370 GTVKL-G--------ETV--KIGYFDQHQEELDPdkTVLDELRDGAP--GGTEQEVRGYLGrflfsgddAFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 458 ydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLD-DSGEqALLAAIQALKarGcTVLLITH-RAGVLGCAD 535
Cdd:COG0488 437 ---------------EKARLALAKLLLSPPNVLLLDEPTNHLDiETLE-ALEEALDDFP--G-TVLLVSHdRYFLDRVAT 497
|
250
....*....|...
gi 15596443 536 RLLALNAGQLHLY 548
Cdd:COG0488 498 RILEFEDGGVREY 510
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
349-526 |
1.40e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrqyERETLGPRIGYL-PQDIELFAGTVAENI 427
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ---ARF---GEVQADKVVEAARLAGvhelVLRLPQGYdtvlgvggagLSGGQRQRIALARAL-YGAPtLVVLDEPNSNLD 500
Cdd:PRK13539 95 efwAAFlggEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLvSNRP-IWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 15596443 501 DSGEQALLAAIQALKARGCTVLLITH 526
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
334-557 |
2.53e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 334 LESLDAAPPGseaRTL-RGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYL 412
Cdd:PRK10575 14 LRNVSFRVPG---RTLlHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 413 PQDIELFAG-TVAENIA-----------RFGEVQADKVVEAARLAGV----HELVLRLPQGydtvlgvggaglsggQRQR 476
Cdd:PRK10575 91 PQQLPAAEGmTVRELVAigrypwhgalgRFGAADREKVEEAISLVGLkplaHRLVDSLSGG---------------ERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 477 IALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVLG--CaDRLLALNAGQLHLYGERDQ 553
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAAryC-DYLVALRGGEMIAQGTPAE 234
|
....
gi 15596443 554 VLAA 557
Cdd:PRK10575 235 LMRG 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
341-564 |
2.54e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRqYE-------RETLGprIGYLP 413
Cdd:PRK13639 12 PDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDkksllevRKTVG--IVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QDIELFAGTVAENIArFG---------EVQaDKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALY 484
Cdd:PRK13639 87 PDDQLFAPTVEEDVA-FGplnlglskeEVE-KRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 485 GAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGC-ADRLLALNAGQLHLYGERDQVLAALNNQRA 563
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETIRK 233
|
.
gi 15596443 564 A 564
Cdd:PRK13639 234 A 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
347-555 |
2.61e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAG-TVAE 425
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIA-----------RFGEVQADKVVEAARLAGVHELVLRLpqgydtvlgvgGAGLSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:PRK11231 96 LVAygrspwlslwgRLSAEDNARVNQAMEQTRINHLADRR-----------LTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 495 PNSNLDDSGEQALLAAIQALKARGCTVLLITH---RAgvlgC--ADRLLALNAGQLHLYGERDQVL 555
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQA----SryCDHLVVLANGHVMAQGTPEEVM 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
349-549 |
2.91e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.04 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyeretlgpRIGYLPQDIELFAGTVAENIA 428
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 rFG----EVQADKVVEAARLagvHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:TIGR01271 509 -FGlsydEYRYTSVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15596443 505 QAL----LAAIQALKARgctvLLITHRAGVLGCADRLLALNAGQLHLYG 549
Cdd:TIGR01271 585 KEIfescLCKLMSNKTR----ILVTSKLEHLKKADKILLLHEGVCYFYG 629
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
347-541 |
4.04e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyeretlGPRIGYLPQDIELFAgTVAEN 426
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQKLYLDT-TLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IARF-----GEVQAD-----KVVEAARLagvHELVLRLPQGYDTvlgvggaglsggqrQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK09544 86 VNRFlrlrpGTKKEDilpalKRVQAGHL---IDAPMQKLSGGET--------------QRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596443 497 SNLDDSGEQALLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALN 541
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHlVMAKTDEVLCLN 195
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-545 |
5.20e-16 |
|
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: 77.41 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEREtLGPRIGYLPQDIELFAG-TVAE 425
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDElTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIARFGEVQ-------ADKVVEAARLAGVHELVLRLPQGYDTVLgvggaglsggqRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:cd03265 93 NLYIHARLYgvpgaerRERIDELLDFVGLLEAADRLVKTYSGGM-----------RRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 499 LDDSGEQALLAAIQALKAR-GCTVLLITH---RAGVLgcADRLLALNAGQL 545
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEfGMTILLTTHymeEAEQL--CDRVAIIDHGRI 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
349-545 |
6.14e-16 |
|
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: 77.92 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVR--------LDGAEIRQYERE----------TLGPRig 410
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAFRRDvqlvfqdspsAVNPR-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 411 ylpQDIELFAGTVAENIARFGEvqadkvveAARLAGVHELvLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLV 490
Cdd:TIGR02769 105 ---MTVRQIIGEPLRHLTSLDE--------SEQKARIAEL-LDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHR-AGVLGCADRLLALNAGQL 545
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDlRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
342-554 |
7.58e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.17 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGS--EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI--RQYERETLGPRIGYLPQ--D 415
Cdd:PRK13637 14 EGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAGTVAENIArFG---------EVQaDKVVEAARLAGVHelvlrlpqgYDTVLGVGGAGLSGGQRQRIALARALYGA 486
Cdd:PRK13637 94 YQLFEETIEKDIA-FGpinlglseeEIE-NRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 487 PTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRA-GVLGCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMeDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
349-563 |
1.00e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 76.96 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERE--TLGPRIGYLPQDIELFAG-TVAE 425
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGMVFQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NI-----------------------ARFG-EVQADKVveAARLAGvhelvlrlpqGydtvlgvggaglsggQRQRIALAR 481
Cdd:COG1126 97 NVtlapikvkkmskaeaeeramellERVGlADKADAY--PAQLSG----------G---------------QQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 482 ALYGAPTLVVLDEPNSNLDD--SGEqaLLAAIQALKARGCTVLLITHRAG----VlgcADRLLALNAGQLHLYGERDQVL 555
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPelVGE--VLDVMRDLAKEGMTMVVVTHEMGfareV---ADRVVFMDGGRIVEEGPPEEFF 224
|
....*...
gi 15596443 556 AALNNQRA 563
Cdd:COG1126 225 ENPQHERT 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
352-554 |
1.04e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YEREtlgprIGYLPQDIELFAG-TVAENI 427
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppYQRP-----INMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ArFGEVQ--------ADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:PRK11607 113 A-FGLKQdklpkaeiASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 500 DDS-GEQALLAAIQALKARGCTVLLITH-RAGVLGCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK11607 181 DKKlRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-559 |
1.17e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYER-ETLGPRIGYLPQDIEL- 418
Cdd:PRK13644 12 PDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAG-TVAENIArFGE-------VQADKVVEAArLA--GVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPT 488
Cdd:PRK13644 90 FVGrTVEEDLA-FGPenlclppIEIRKRVDRA-LAeiGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 489 LVVLDEPNSNLD-DSGEqALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAALN 559
Cdd:PRK13644 157 CLIFDEVTSMLDpDSGI-AVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
349-546 |
1.68e-15 |
|
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: 75.93 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETL----GPRIGYLPQDIELFAG-TV 423
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLPTlTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIA----RFGEVQADKVVEAArLA--GVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVLD 493
Cdd:COG4181 108 LENVMlpleLAGRRDARARARAL-LErvGLGHRLDHYPAqlsgG---------------EQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 494 EPNSNLD-DSGEQ--ALLAAIQAlkARGCTVLLITHRAGVLGCADRLLALNAGQLH 546
Cdd:COG4181 172 EPTGNLDaATGEQiiDLLFELNR--ERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
388-541 |
1.97e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 388 GSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIaRFGEVQA--DKVVEAARLAGVHELVLRLPQGYDTVLGVG 465
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFGKEDAtrEDVKRACKFAAIDEFIESLPNKYDTNVGPY 1355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 466 GAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARG-CTVLLITHRAGVLGCADRLLALN 541
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
332-527 |
2.09e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYeretlGPR--- 408
Cdd:PRK10762 5 LQLKGIDKAFPGVKA--LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN-----GPKssq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 ---IGYLPQDIELFAG-TVAENI-------ARFGEV-------QADKVVeaARLA---GVHELVLRLPQGydtvlgvgga 467
Cdd:PRK10762 78 eagIGIIHQELNLIPQlTIAENIflgrefvNRFGRIdwkkmyaEADKLL--ARLNlrfSSDKLVGELSIG---------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 468 glsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:PRK10762 146 -----EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHR 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
364-564 |
2.47e-15 |
|
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: 77.15 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 364 VIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGprIGYLPQDIELFAG-TVAENIArFGeVQADKVVEAA 442
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFPHmTVEENVA-FG-LKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 443 RLAGVHElVLRLPQgYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTV 521
Cdd:TIGR01187 77 IKPRVLE-ALRLVQ-LEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15596443 522 LLITH-RAGVLGCADRLLALNAGQLHLYGERDQVLAALNNQRAA 564
Cdd:TIGR01187 155 VFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVA 198
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
349-549 |
2.61e-15 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 75.80 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP---RIGYLPQDIELFAG-TVA 424
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRIGMIFQHYNLIERlTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENI---------------ARFGEVQADKVVEAARLAGVHELVLrlpQGYDTVlgvggaglSGGQRQRIALARALYGAPTL 489
Cdd:TIGR02315 98 ENVlhgrlgykptwrsllGRFSEEDKERALSALERVGLADKAY---QRADQL--------SGGQQQRVAIARALAQQPDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 490 VVLDEPNSNLD-DSGEQALLAAIQALKARGCTVLLITHRAGV-LGCADRLLALNAGQLHLYG 549
Cdd:TIGR02315 167 ILADEPIASLDpKTSKQVMDYLKRINKEDGITVIINLHQVDLaKKYADRIVGLKAGEIVFDG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
349-570 |
2.81e-15 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 76.43 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTlHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:cd03289 99 PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 509 AAIQALKArGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAALNNQRAASASQQR 570
Cdd:cd03289 179 KTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-526 |
2.97e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.08 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 351 GLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI--------RQYERE----------TLGPR--IG 410
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgrelRPLRRRmqmvfqdpyaSLNPRmtVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 411 ylpqDIelfagtVAE-----NIARFGEVQaDKVVEAARLAGVH-ELVLRLPQ----GydtvlgvggaglsggQRQRIALA 480
Cdd:COG4608 116 ----DI------IAEplrihGLASKAERR-ERVAELLELVGLRpEHADRYPHefsgG---------------QRQRIGIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 481 RALYGAPTLVVLDEPNSNLDDSgeqallaaIQA--------LKAR-GCTVLLITH 526
Cdd:COG4608 170 RALALNPKLIVCDEPVSALDVS--------IQAqvlnlledLQDElGLTYLFISH 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
346-545 |
3.03e-15 |
|
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: 74.01 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 346 ARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY-ERETLGPRIGYLPQD---IELFAG 421
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRsPRDAIRAGIAYVPEDrkrEGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArfgevqadkvveaarlagvheLVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:cd03215 93 lSVAENIA---------------------LSSLLSGG---------------NQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 501 DSGEQALLAAIQALKARGCTVLLI-THRAGVLGCADRLLALNAGQL 545
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKAVLLIsSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
345-554 |
4.69e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYER----ETLGPRIGYLPQ--DIEL 418
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIA----RFG--EVQADKVV-EAARLAGVHE-LVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLV 490
Cdd:PRK13649 99 FEETVLKDVAfgpqNFGvsQEEAEALArEKLALVGISEsLFEKNP-----------FELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRA-GVLGCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
349-562 |
5.07e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI--------RQYERETLGPRIGYLPQDIELFA 420
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENIARfGEVQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:PRK11264 99 HrTVLENIIE-GPVIVKGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 500 DDSGEQALLAAIQALKARGCTVLLITHRAGVL-GCADRLLALNAGQLHLYGERDQVLAALNNQR 562
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
335-545 |
5.17e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 74.61 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 335 ESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG---IWPTLHGSVRLDGAEIrqyERETLGPRIGY 411
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR---KPDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQDIELFAG-TVAENIA---------RFGEVQADKVVEAARLAGVHELVLRlpqgydtvlGVGGAGLSGGQRQRIALAR 481
Cdd:cd03234 86 VRQDDILLPGlTVRETLTytailrlprKSSDAIRKKRVEDVLLRDLALTRIG---------GNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH--RAGVLGCADRLLALNAGQL 545
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
349-543 |
5.56e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.67 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPT-LVVLDEPNSNLDdsgeQAL 507
Cdd:PTZ00243 1406 PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANID----PAL 1481
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596443 508 LAAIQA--LKA-RGCTVLLITHRAGVLGCADRLLALNAG 543
Cdd:PTZ00243 1482 DRQIQAtvMSAfSAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
95-545 |
6.65e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 95 QLHGRIYAAAFERNLR---------AGGQEASQALHDLTTLRQFitGQALFAFFDAPwFPVYLLVIFLFDPwLGLLSLVG 165
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRlthearknfASGKVTNMITTDANALQQI--AEQLHGLWSAP-FRIIVSMVLLYQQ-LGVASLFG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 166 ALALMALAWFN----ERATRapLAKAGeLSIKSGQLASNNlrnaEVIEAMGMLGSMRgrWERLHQAFLD---QQSLASER 238
Cdd:PLN03232 447 SLILFLLIPLQtlivRKMRK--LTKEG-LQWTDKRVGIIN----EILASMDTVKCYA--WEKSFESRIQgirNEELSWFR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 239 AARInaLSKYLRIALQSL-----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRLSGLL 313
Cdd:PLN03232 518 KAQL--LSAFNSFILNSIpvvvtLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 314 defpARERRMELPEP------------RGHLLLESLDAAPpgsearTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG 381
Cdd:PLN03232 596 ----LSEERILAQNPplqpgapaisikNGYFSWDSKTSKP------TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 382 IWPTLH-GSVRLDGAeirqyeretlgprIGYLPQDIELFAGTVAENI---ARFGEVQADKVVEAARLAgvHELVLrLPqG 457
Cdd:PLN03232 666 ELSHAEtSSVVIRGS-------------VAYVPQVSWIFNATVRENIlfgSDFESERYWRAIDVTALQ--HDLDL-LP-G 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 458 YD-TVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADR 536
Cdd:PLN03232 729 RDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR 808
|
....*....
gi 15596443 537 LLALNAGQL 545
Cdd:PLN03232 809 IILVSEGMI 817
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
332-556 |
8.34e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSeaRTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR---QYERETLGpr 408
Cdd:PRK10895 4 LTAKNLAKAYKGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 IGYLPQDIELFAG-TVAENIARFGEVQADKVVEAAR------LAGVHELVLRLPQGydtvlgvggAGLSGGQRQRIALAR 481
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIRDDLSAEQREdranelMEEFHIEHLRDSMG---------QSLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRA-GVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-572 |
1.18e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTlHGSVRLDGAEIRQYERETLGPRIGYLPQDIE-LFAGTVAENIARF 430
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 431 gevQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALA-------RALYGAPTLVVLDEPNSNLDDSG 503
Cdd:PRK03695 94 ---QPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 504 EQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLAALNNQRAASASQQRAD 572
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
344-545 |
1.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.38 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQ--DIELFAG 421
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQnpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:PRK13650 98 TVEDDVA-FGlenkgiphEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
330-527 |
2.26e-14 |
|
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: 76.87 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 330 GHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTlHGSVRLDGAEIRQYERETLGPRI 409
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 410 GYLPQDIELFAGTVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTL 489
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQALKArGCTVLLITHR 527
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFS-NCTVILSEHR 1411
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
349-545 |
2.92e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.45 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEIRQYERETLGP---RIGYLPQDIELFAG-TV 423
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPT-SGRVLVDGQDLTALSEKELRKarrQIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIA--------RFGEVQAdKVVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVV 491
Cdd:PRK11153 100 FDNVAlplelagtPKAEIKA-RVTELLELVGLSDKADRYPAqlsgG---------------QKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 492 LDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAGVL-GCADRLLALNAGQL 545
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
347-527 |
3.35e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP--TLHGSVRLDGAEIRQYE-RETLGPRIGYLPQDIELFAG-T 422
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNiRDTERAGIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENI------ARFGEVQADKVV-EAARL-------AGVHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPT 488
Cdd:PRK13549 99 VLENIflgneiTPGGIMDYDAMYlRAQKLlaqlkldINPATPVGNLGLG---------------QQQLVEIAKALNKQAR 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596443 489 LVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHK 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
349-544 |
3.36e-14 |
|
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: 72.08 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGA------------EIRQYERETLG---------P 407
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqasprEILALRRRTIGyvsqflrviP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 408 RIGYLpqDIelfagtVAENIARFGEVQADKVVEAARLagvheLV-LRLPQ------------GydtvlgvggaglsggQR 474
Cdd:COG4778 107 RVSAL--DV------VAEPLLERGVDREEARARAREL-----LArLNLPErlwdlppatfsgG---------------EQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 475 QRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVL-GCADRLLALNAGQ 544
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVReAVADRVVDVTPFS 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
350-540 |
3.77e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 350 RGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR----QYERETLgpRIGYLPQ-DIELfagTVA 424
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYHQDLL--YLGHQPGiKTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIaRF-----GEVQADKVVEAAR---LAGVHELVLR-LPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEP 495
Cdd:PRK13538 93 ENL-RFyqrlhGPGDDEALWEALAqvgLAGFEDVPVRqLSAG---------------QQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 496 NSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLAL 540
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQdLPVASDKVRKLRL 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-526 |
4.05e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.30 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 351 GLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGpRIGYLPQDIELFAG-TVAENIAR 429
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ-RVGVVPQFDNLDPDfTVRENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 430 FGEVQADKVVEA-ARLAGVHELVlRLPQGYDtvlgVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:PRK13537 104 FGRYFGLSAAAArALVPPLLEFA-KLENKAD----AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170
....*....|....*...
gi 15596443 509 AAIQALKARGCTVLLITH 526
Cdd:PRK13537 179 ERLRSLLARGKTILLTTH 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-561 |
4.10e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.77 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGA------EIRQYERETLGPRIGYLPQDIELFAG- 421
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIARfgEVQADKVVEAARLAGVHELVLRLPQGYDTV---LGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:PRK14246 106 SIYDNIAY--PLKSHGIKEKREIKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 499 LDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQLHLYGERDQVLAALNNQ 561
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
353-526 |
4.14e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 353 TLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEirqYERETLGPR-IGYLPQDIELFAG-TVAENIA-- 428
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRpVSMLFQENNLFSHlTVAQNIGlg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 -----RFGEVQADKVVEAARLAGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSG 503
Cdd:PRK10771 96 lnpglKLNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180
....*....|....*....|....
gi 15596443 504 EQALLAAI-QALKARGCTVLLITH 526
Cdd:PRK10771 165 RQEMLTLVsQVCQERQLTLLMVSH 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
347-527 |
4.39e-14 |
|
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: 74.86 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP--TLHGSVRLDGAEIR-QYERETLGPRIGYLPQDIELFAG-T 422
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKaSNIRDTERAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFGEV--QADKVVEAARLAGVHELV--LRLPQGYDTvlgVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:TIGR02633 95 VAENIFLGNEItlPGGRMAYNAMYLRAKNLLreLQLDADNVT---RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180
....*....|....*....|....*....
gi 15596443 499 LDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
344-554 |
4.43e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQ--DIELFAG 421
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TVAENIArFG--------EVQADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:PRK13652 95 TVEQDIA-FGpinlgldeETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
349-531 |
6.53e-14 |
|
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: 70.63 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIwPT---LHGSVRLDGAEIRQ---YERETLGprIGYLPQDIELFAGT 422
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKyevTEGEILFKGEDITDlppEERARLG--IFLAFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARF-------GEvqadkvveaarlagvhelvlrlpqgydtvlgvggaglsggqRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03217 93 KNADFLRYvnegfsgGE-----------------------------------------KKRNEILQLLLLEPDLAILDEP 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 15596443 496 NSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVL 531
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLL 167
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
349-550 |
6.81e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVrldgaeirQYEREtlgprIGYLPQDIELFAGTVAENIA 428
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERS-----IAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDS-GE--- 504
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGErvv 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596443 505 -QALLAAIqalkaRGCTVLLITHRAGVLGCADRLLALNAGQLHLYGE 550
Cdd:PTZ00243 823 eECFLGAL-----AGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
345-556 |
8.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.97 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI----RQYERETLGPRIGYLPQDIE--L 418
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQFPEhqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIA----RFGEVQAD---KVVEAARLAGVHELVL-RLPqgYDtvlgvggagLSGGQRQRIALARALYGAPTLV 490
Cdd:PRK13634 99 FEETVEKDICfgpmNFGVSEEDakqKAREMIELVGLPEELLaRSP--FE---------LSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRA-GVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMeDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
349-526 |
9.93e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEREtlgpRIGYLPQDIEL-FAGTVAENI 427
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA----QRKAFRRDIQMvFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ARF--GEVQAD------KVVEAARLAGVHELvLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:PRK10419 104 PRKtvREIIREplrhllSLDKAERLARASEM-LRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180
....*....|....*....|....*...
gi 15596443 500 DDSGEQALLAAIQALKARGCTV-LLITH 526
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTAcLFITH 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-545 |
1.82e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.98 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIW---PTLHGSVRLDGAEIRQYERETLGPRIGYLPQ--DI 416
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQnpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 417 ELFAGTVAENIArFGeVQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK13640 96 QFVGATVGDDVA-FG-LENRAVPRPEMIKIVRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596443 497 SNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
347-558 |
1.84e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGS--VRL-----DGAEIRQYERETLGPRIGYLPQDIELF 419
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVgdewvDMTKPGPDGRGRAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 A-GTVAENIARfgEVQADKVVEAARLAGVHELVLrlpQGYD-----TVLGVGGAGLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:TIGR03269 378 PhRTVLDNLTE--AIGLELPDELARMKAVITLKM---VGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 494 EPNSNLDDSGEQALLAAIqaLKAR---GCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVLAAL 558
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSI--LKAReemEQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
343-549 |
2.31e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.55 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIE-LFAG 421
Cdd:PRK13648 19 SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArFG----EVQADKVVEaaRLAGVHELVLRLPQGYDTvlgvgGAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK13648 99 sIVKYDVA-FGlenhAVPYDEMHR--RVSEALKQVDMLERADYE-----PNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 497 SNLDDSGEQALLAAIQALKA-RGCTVLLITHRAGVLGCADRLLALNAGQLHLYG 549
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-536 |
2.34e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI-WPTlHGSVRLDGAEIRQYeretlGPR------IGYLPQDIELFAG 421
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLyQPD-SGEILIDGKPVRIR-----SPRdaialgIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIA-----------RFGEVQAdKVVEAARLAGV----HELVLRLPQGydtvlgvggaglsggQRQRIALARALYG 485
Cdd:COG3845 95 lTVAENIVlgleptkggrlDRKAARA-RIRELSERYGLdvdpDAKVEDLSVG---------------EQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596443 486 APTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADR 536
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLReVMAIADR 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
345-528 |
2.81e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.92 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyERETLGPRIGYLP-QDIELFAGTV 423
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGhLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENI---ARFGEVQADKVVEAARLAGV----HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPN 496
Cdd:TIGR01189 91 LENLhfwAAIHGGAQRTIEDALAAVGLtgfeDLPAAQLSAG---------------QQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 15596443 497 SNLDDSGEQALLAAIQALKARGCTVLLITHRA 528
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
341-545 |
3.09e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEA-RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVvLGIW--PTlHGSVRLDGAEIRQYERETLG----PRIGYLP 413
Cdd:PRK10535 15 PSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNI-LGCLdkPT-SGTYRVAGQDVATLDADALAqlrrEHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QDIELFAG-TVAENIarfgEVQA--DKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLV 490
Cdd:PRK10535 93 QRYHLLSHlTAAQNV----EVPAvyAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-526 |
3.27e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 331 HLLLESLDAAPPGSEART--LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrqyerETLGPR 408
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 409 IGYLPQDIELFAG-TVAENIArFGeVQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAP 487
Cdd:COG4525 78 RGVVFQKDALLPWlNVLDNVA-FG-LRLRGVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15596443 488 TLVVLDEPNSNLDDSGE---QALLaaIQALKARGCTVLLITH 526
Cdd:COG4525 154 RFLLMDEPFGALDALTReqmQELL--LDVWQRTGKGVFLITH 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
344-543 |
3.75e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTL-HGSVRLDGaeirqyeretlgpRIGYLPQDIELFAGT 422
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRG-------------TVAYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFGEVQADKVVEAARLAGV-HELVLrLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDD 501
Cdd:PLN03130 695 VRDNILFGSPFDPERYERAIDVTALqHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596443 502 S-GEQALLAAIQAlKARGCTVLLITHRAGVLGCADRLLALNAG 543
Cdd:PLN03130 774 HvGRQVFDKCIKD-ELRGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
349-554 |
3.80e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI-RQYERETlgpRIGYLPQDIELFAG-TVAEN 426
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsRLHARDR---KVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 IArFG------------EVQADKVVEAARLAGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:PRK10851 95 IA-FGltvlprrerpnaAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 495 PNSNLDDSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEElKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
364-545 |
4.07e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 364 VIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERETLGP-------------RIGYLPQ--DIELFAGTVAE 425
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknNHELITNPyskkiknfkelrrRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIArFGEVQ-ADKVVEAARLAGVHELVLRLPQGYdtvLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:PRK13631 137 DIM-FGPVAlGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGE 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15596443 505 QALLAAIQALKARGCTVLLITHRA-GVLGCADRLLALNAGQL 545
Cdd:PRK13631 213 HEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-526 |
4.26e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVV-----LGIWPTLHGSVRLDGAEIRQYERETLGPRIGY---LPQDI 416
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIELRRRVQMvfqIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 417 ELFagTVAENIArFGeVQADKVVEAAR-LAGVHELVLRLPQGYDTV---LGVGGAGLSGGQRQRIALARALYGAPTLVVL 492
Cdd:PRK14247 95 PNL--SIFENVA-LG-LKLNRLVKSKKeLQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|....
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKaRGCTVLLITH 526
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELK-KDMTIVLVTH 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
349-556 |
4.39e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.29 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ---YERETLGprIGYLPQDIELFAG-TVA 424
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRARLG--IGYLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIARFGEVQadKVVEAARLAGVHELV-------LRLPQGYdtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNS 497
Cdd:COG1137 97 DNILAVLELR--KLSKKEREERLEELLeefgithLRKSKAY---------SLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 498 NLD-----DSgeQALlaaIQALKARGCTVlLIT-HRagV---LGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:COG1137 166 GVDpiavaDI--QKI---IRHLKERGIGV-LITdHN--VretLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-529 |
5.26e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLgprIGYLPQDIEL---FAGTVAE 425
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVdwsFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NI--ARFGEV-------QADKVVEAARLAGVHELVLRLPQgydtvlgvgGAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK15056 100 VVmmGRYGHMgwlrrakKRDRQIVTAALARVDMVEFRHRQ---------IGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|...
gi 15596443 497 SNLDDSGEQALLAAIQALKARGCTVLLITHRAG 529
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
347-546 |
9.57e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI-RQYERET--LGPRIGYLPQDIELF---- 419
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVpfLRRQIGMIFQDHHLLmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 -----------AGTVAENIARFGEVQADKVveaARLAGVHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPT 488
Cdd:PRK10908 96 vydnvaipliiAGASGDDIRRRVSAALDKV---GLLDKAKNFPIQLSGG---------------EQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 489 LVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCAD-RLLALNAGQLH 546
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
20-309 |
9.86e-13 |
|
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: 69.01 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQL--- 96
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLilg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 97 -HGRIYA--AAFERNLRAGgqEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALA 173
Cdd:cd18570 81 yFKHLLKlpLSFFETRKTG--EIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 174 W----FNERATRaplakagELSIKSGQLASN---NLRNAEVIEAmgmLGSMRGRWERLHQAFLDQQSLaSERAARINALS 246
Cdd:cd18570 159 LlfnkPFKKKNR-------EVMESNAELNSYlieSLKGIETIKS---LNAEEQFLKKIEKKFSKLLKK-SFKLGKLSNLQ 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 247 KYLRIALQSL----VLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18570 228 SSIKGLISLIgsllILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
349-526 |
1.16e-12 |
|
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: 67.13 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyERETLGPRIGYLP-QDIELFAGTVAENI 427
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGhAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ARFGEVQADKVVEAA----RLAGV-HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:cd03231 95 RFWHADHSDEQVEEAlarvGLNGFeDRPVAQLSAG---------------QQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....
gi 15596443 503 GEQALLAAIQALKARGCTVLLITH 526
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTH 183
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
345-557 |
1.31e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIEL-FAGTV 423
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENI-----------ARFGEVQADKVVEAARLAGVHELVLRlpqGYDTVlgvggaglSGGQRQRIALARALYGAPTLVVL 492
Cdd:PRK09536 95 RQVVemgrtphrsrfDTWTETDRAAVERAMERTGVAQFADR---PVTSL--------SGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLG--CaDRLLALNAGQLHLYGERDQVLAA 557
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAAryC-DELVLLADGRVRAAGPPADVLTA 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
345-545 |
1.45e-12 |
|
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: 67.74 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeIRQYERetlgpRIGYLPQdIELFAGT-- 422
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKR-----RKKFLRR-IGVVFGQkt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 -------VAENIARFGEV-QADKVVEAARLAGVHELvLRLPQgydtVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:cd03267 105 qlwwdlpVIDSFYLLAAIyDLPPARFKKRLDELSEL-LDLEE----LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15596443 495 PNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKdIEALARRVLVIDKGRL 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
349-544 |
1.53e-12 |
|
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: 65.16 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEirqyeretlgpRIGYLPQdielfagtvaenia 428
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 rfgevqadkvveaarLAGvhelvlrlpqGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALl 508
Cdd:cd03221 71 ---------------LSG----------G---------------EKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL- 109
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596443 509 aaIQALKARGCTVLLITH-RAGVLGCADRLLALNAGQ 544
Cdd:cd03221 110 --EEALKEYPGTVILVSHdRYFLDQVATKIIELEDGK 144
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
352-545 |
1.56e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRqyERETLGPRIGYLPQDIELFAG-TVAENIA-- 428
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSLGENVGyg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 -----RFGEVQADKVVEAAR---LAGVHE-LVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:PRK11432 103 lkmlgVPKEERKQRVKEALElvdLAGFEDrYVDQISGG---------------QQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15596443 500 DDSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQL 545
Cdd:PRK11432 168 DANLRRSMREKIRELQQQfNITSLYVTHdQSEAFAVSDTVIVMNKGKI 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
347-566 |
1.62e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYER-ETLGPRIGYLPQDIELFAG-TVA 424
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSRmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIArFGEVQADKVVEAARLAGVHELVLRLPQGYdtvlGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:PRK11614 99 ENLA-MGGFFAERDQFQERIKWVYELFPRLHERR----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 505 QALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLygeRDQVLAALNNQRAASA 566
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANqALKLADRGYVLENGHVVL---EDTGDALLANEAVRSA 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
350-548 |
1.80e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 350 RGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDgaEIRQYERETLGPRIGYLPQDIELFAG-TVAENIA 428
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQSYALYPHlSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 rFG-------EVQADKVVE-AARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:PRK11000 98 -FGlklagakKEEINQRVNqVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 501 DSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQ-------LHLY 548
Cdd:PRK11000 166 AALRVQMRIEISRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRvaqvgkpLELY 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
344-555 |
2.05e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTlHGSVRLDGAEIRQYERETLGPRIGYLPQDIE-LFAGT 422
Cdd:COG4138 7 AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFgevQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALY-------GAPTLVVLDEP 495
Cdd:COG4138 86 VFQYLALH---QPAGASSEAVEQLLAQLAEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 496 NSNLDDSGEQALLAAIQALKARGCTVLLITH---RAgvLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHdlnHT--LRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
338-554 |
4.30e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 338 DAAPPGSEARTLR---GLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYE----RET------ 404
Cdd:PRK15079 23 GKQWFWQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewRAVrsdiqm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 405 --------LGPRIgylpqdielfagTVAENIAR-----FGEVQADKVVEAarlagVHELVLR---LPQgydtVLGVGGAG 468
Cdd:PRK15079 103 ifqdplasLNPRM------------TIGEIIAEplrtyHPKLSRQEVKDR-----VKAMMLKvglLPN----LINRYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 469 LSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSgEQA----LLAAIQalKARGCTVLLITHRAGVLG-CADRLLALNAG 543
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVS-IQAqvvnLLQQLQ--REMGLSLIFIAHDLAVVKhISDRVLVMYLG 238
|
250
....*....|.
gi 15596443 544 QLHLYGERDQV 554
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
352-554 |
4.66e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERET-LGP---RIGYLPQDIELFAG-TVAEN 426
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPekrRIGYVFQDARLFPHyKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 ----IARFGEVQADKVVEaarLAGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:PRK11144 97 lrygMAKSMVAQFDKIVA---LLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 503 GEQALLAAIQALKARGCT-VLLITHRAG-VLGCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK11144 163 RKRELLPYLERLAREINIpILYVSHSLDeILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
349-540 |
4.94e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKVVEAARLAGVHElvLRLPqgyDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:PRK10247 103 FPWQIRNQQPDPAIFLDDLER--FALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190
....*....|....*....|....*....|...
gi 15596443 509 AAIQAL-KARGCTVLLITHRAGVLGCADRLLAL 540
Cdd:PRK10247 178 EIIHRYvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
349-543 |
5.27e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.95 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQyeretLGPRIGYLPQDIELFAG-TVAENI 427
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-----PGPDRMVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ArfgeVQADKVVEAARLAGVHELVlrlPQGYDTVLGVGGAGLSGGQ-----RQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:TIGR01184 76 A----LAVDRVLPDLSKSERRAIV---EEHIALVGLTEAADKRPGQlsggmKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596443 503 GEQALLAAI-QALKARGCTVLLITHRAG-VLGCADRLLALNAG 543
Cdd:TIGR01184 149 TRGNLQEELmQIWEEHRVTVLMVTHDVDeALLLSDRVVMLTNG 191
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
26-309 |
5.31e-12 |
|
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: 66.81 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 26 VAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGRIYAAA- 104
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 105 ------FERNlrAGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVgALALMALA--WFN 176
Cdd:cd07346 84 rlslsfFDRN--RTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALL-LLPLYVLIlrYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 177 ERATRAplakAGELSIKSGQLASN---NLRNAEVIEAMGMLGSMRGRWERLHQAFLDQQSLASERAARINALSKYLRIAL 253
Cdd:cd07346 161 RRIRKA----SREVRESLAELSAFlqeSLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 254 QSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd07346 237 TALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
345-562 |
8.53e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR-------------QYERETLGPRIGY 411
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQDIELFAG-TVAENIAR-----FGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGgaglsggQRQRIALARALYG 485
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMEapiqvLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGG-------QQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 486 APTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVL-GCADRLLALNAGQLHLYGERDQVLAALNNQR 562
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
349-526 |
9.65e-12 |
|
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: 65.74 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETL----GPRIGYLPQDIELFAG-TV 423
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIArFG-EVQ-------ADKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03294 120 LENVA-FGlEVQgvpraerEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190
....*....|....*....|....*....|....
gi 15596443 496 NSNLDD---SGEQALLAAIQALKARgcTVLLITH 526
Cdd:cd03294 188 FSALDPlirREMQDELLRLQAELQK--TIVFITH 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-564 |
1.01e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 337 LDAAPPGSEA----------RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHG-----SVRLDGAEIRQYe 401
Cdd:PRK14271 15 VDAAAPAMAAvnltlgfagkTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 402 RETLG--PRIGYLPQDIELFAGTVAENIarFGEVQADKVVEAARLAGVHELVLRLPQGYDTV---LGVGGAGLSGGQRQR 476
Cdd:PRK14271 94 RDVLEfrRRVGMLFQRPNPFPMSIMDNV--LAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 477 IALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARgCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNlAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
....*....
gi 15596443 556 AALNNQRAA 564
Cdd:PRK14271 251 SSPKHAETA 259
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
332-526 |
1.06e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR--QYERETLGPRI 409
Cdd:PRK11248 2 LQISHLYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 410 GYLPQDielfagTVAENIArFGeVQADKVVEAARLAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTL 489
Cdd:PRK11248 80 GLLPWR------NVQDNVA-FG-LQLAGVEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596443 490 VVLDEPNSNLDD-SGEQALLAAIQALKARGCTVLLITH 526
Cdd:PRK11248 150 LLLDEPFGALDAfTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
20-293 |
1.37e-11 |
|
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: 65.56 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 20 RGALRSVAAFSGVINLLMLVPSLYMLQVYDRVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGR 99
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 100 IYA-------AAFERnlRAGGQEASQaLHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMAL 172
Cdd:cd18567 81 LFRhllrlplSYFEK--RHLGDIVSR-FGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 173 AWfnerATRAPLAKAGELSI-KSGQLASN---NLRNAEVIEAMGMLGSMRGRWERLHQAFLDqqslASERAARINALSKY 248
Cdd:cd18567 158 RL----ALYPPLRRATEEQIvASAKEQSHfleTIRGIQTIKLFGREAEREARWLNLLVDAIN----ADIRLQRLQILFSA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15596443 249 LRIALQSL----VLGLGAWLAVEGRITPGMMIA----GSILMGRALGPIDQLI 293
Cdd:cd18567 230 ANGLLFGLenilVIYLGALLVLDGEFTVGMLFAflayKDQFSSRASSLIDKLF 282
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
343-549 |
1.43e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGA---------EIRQyeretlgpRIGYLP 413
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsdeenlwDIRN--------KAGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 Q--DIELFAGTVAENIArFGE----VQAD----KVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARAL 483
Cdd:PRK13633 92 QnpDNQIVATIVEEDVA-FGPenlgIPPEeireRVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 484 YGAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVLGCADRLLALNAGQLHLYG 549
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
287-546 |
1.44e-11 |
|
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: 67.13 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 287 GPIDQLIGVWKQWGAARDAYRRLSGLldefparerRMELPEPRGHLLLESLDAAPPGSEARTLRGLT------------- 353
Cdd:COG4615 277 GPLSQLVGALPTLSRANVALRKIEEL---------ELALAAAEPAAADAAAPPAPADFQTLELRGVTyrypgedgdegft 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 354 -----LAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERET-------------LGPRIgyLPQD 415
Cdd:COG4615 348 lgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrqlfsavfsdfhLFDRL--LGLD 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAGTVAENIARFGevQADKV-VEAARLagvheLVLRLPQGydtvlgvggaglsggQRQRIALARALY-GAPtLVVLD 493
Cdd:COG4615 426 GEADPARARELLERLE--LDHKVsVEDGRF-----STTDLSQG---------------QRKRLALLVALLeDRP-ILVFD 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 494 EpnsnlddsgeqalLAAIQ--------------ALKARGCTVLLITHRAGVLGCADRLLALNAGQLH 546
Cdd:COG4615 483 E-------------WAADQdpefrrvfytellpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
349-526 |
1.55e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSL-------------ARVVLGIwpTLHGS----VRLDGAEIRQyeretlgpRIGY 411
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrlndlipgFRVEGKV--TFHGKnlyaPDVDPVEVRR--------RIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQDIELFAGTVAENIArFG------EVQADKVVEAArlagvhelvLRLPQGYDTV---LGVGGAGLSGGQRQRIALARA 482
Cdd:PRK14243 96 VFQKPNPFPKSIYDNIA-YGaringyKGDMDELVERS---------LRQAALWDEVkdkLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15596443 483 LYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARgCTVLLITH 526
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTH 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-526 |
1.98e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEarTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDgaeirqyeretLGPRIGYLPQDIELFA 420
Cdd:TIGR03719 15 PPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-----------PGIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENI-----------ARFGEVQA---------DKVV-EAARL------AGVHEL---------VLRLPQGYDTVlg 463
Cdd:TIGR03719 82 TkTVRENVeegvaeikdalDRFNEISAkyaepdadfDKLAaEQAELqeiidaADAWDLdsqleiamdALRCPPWDADV-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 464 vggAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDdsGEQ-ALLAaiQALKARGCTVLLITH 526
Cdd:TIGR03719 160 ---TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD--AESvAWLE--RHLQEYPGTVVAVTH 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
347-579 |
2.11e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVV-----LGIWPTLHGSVRLDGAEIRQYERETLGPR--IGYLPQDIELF 419
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTVDLRkeIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AGTVAENiarfgevqadkVVEAARLAGVH---------ELVLRLPQGYDTV---LGVGGAGLSGGQRQRIALARALYGAP 487
Cdd:PRK14239 99 PMSIYEN-----------VVYGLRLKGIKdkqvldeavEKSLKGASIWDEVkdrLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 488 TLVVLDEPNSNLDDSGEQALLAAIQALKARgCTVLLITH---RAGVLgcADRLLALNAGQLHLYGERDQVLaaLNNQRaa 564
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRsmqQASRI--SDRTGFFLDGDLIEYNDTKQMF--MNPKH-- 240
|
250
....*....|....*
gi 15596443 565 sasQQRADYRVAGYG 579
Cdd:PRK14239 241 ---KETEDYISGKFG 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
341-556 |
3.26e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrQYERE---TLGPRIGYLPQ--D 415
Cdd:PRK13636 16 SDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESVGMVFQdpD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELFAGTVAENIArFGEVQAdKVVEAArlagVHELVLRLPQ--GYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:PRK13636 93 NQLFSASVYQDVS-FGAVNL-KLPEDE----VRKRVDNALKrtGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 494 EPNSNLDDSGEQALLAAI-QALKARGCTVLLITHRAGV--LGCaDRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIvpLYC-DNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
349-431 |
3.44e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSL------ARVVlgiwptLHGSVRLDGAEIRQ-YERETLGPRIGYLPQDI----- 416
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLlsliagARKI------QQGRVEVLGGDMADaRHRRAVCPRIAYMPQGLgknly 90
|
90
....*....|....*.
gi 15596443 417 -ELfagTVAENIARFG 431
Cdd:NF033858 91 pTL---SVFENLDFFG 103
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-526 |
4.81e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVvLGIWPTLHGSVRLDG-AEI---RQYERET----LGPRIGYLPQDIEL 418
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGrVEFfnqNIYERRVnlnrLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIArFG--------EVQADKVVEAARLAG---------VHELVLRLPQGydtvlgvggaglsggQRQRIALAR 481
Cdd:PRK14258 100 FPMSVYDNVA-YGvkivgwrpKLEIDDIVESALKDAdlwdeikhkIHKSALDLSGG---------------QQQRLCIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARG-CTVLLITH 526
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSH 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-545 |
6.03e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.91 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY----ERETLGPRIGYLPQDIELFAG-TV 423
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIAR---FGEVQADKVVEAAR--LAGVhelvlrlpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:PRK11629 105 LENVAMpllIGKKKPAEINSRALemLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15596443 499 LDDSGEQALLAAIQALKAR-GCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
349-540 |
6.32e-11 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 63.02 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVL--GIWPTLHGS-------VRLDGAE----------------------- 396
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypALARRLHLKkeqpgnhDRIEGLEhidkvividqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 397 -------IRQ----------YERETLgpRIGYLPQDI-ELFAGTVAE------NIARFgevqadkvveAARLAGVHELVL 452
Cdd:cd03271 91 ytgvfdeIRElfcevckgkrYNRETL--EVRYKGKSIaDVLDMTVEEaleffeNIPKI----------ARKLQTLCDVGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 453 rlpqGYDTvLGVGGAGLSGGQRQRIALARALYGA---PTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG 529
Cdd:cd03271 159 ----GYIK-LGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
250
....*....|.
gi 15596443 530 VLGCADRLLAL 540
Cdd:cd03271 234 VIKCADWIIDL 244
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
345-531 |
7.52e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrQYERETlgprigylpqdielfagTVA 424
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-QFGREA-----------------SLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 ENIARFGEVqaDKVVEAARLAGVHE--LVLRLPQGYDTvlgvggaglsgGQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:COG2401 104 DAIGRKGDF--KDAVELLNAVGLSDavLWLRRFKELST-----------GQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|
gi 15596443 503 GEQALLAAIQ-ALKARGCTVLLITHRAGVL 531
Cdd:COG2401 171 TAKRVARNLQkLARRAGITLVVATHHYDVI 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-545 |
7.59e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 346 ARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRqyereTLGPR------IGYLPQD--IE 417
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-----IRSPRdairagIAYVPEDrkGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 -LFAG-TVAENI--------ARFGEVQADKVVEAA---------RLAGVHELVLRLP---QgydtvlgvggaglsggqrQ 475
Cdd:COG1129 340 gLVLDlSIRENItlasldrlSRGGLLDRRRERALAeeyikrlriKTPSPEQPVGNLSggnQ------------------Q 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596443 476 RIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPeLLGLSDRILVMREGRI 472
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
346-526 |
8.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 346 ARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI----RQYERETLGPRIGYLPQ--DIELF 419
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AGTVAENIA----RFG--EVQADKVV-EAARLAGV-HELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVV 491
Cdd:PRK13643 99 EETVLKDVAfgpqNFGipKEKAEKIAaEKLEMVGLaDEFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190
....*....|....*....|....*....|....*
gi 15596443 492 LDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
349-544 |
8.84e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 63.71 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEretlgPR---IGYLPQDIELFAG-TVA 424
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-----PAdrdIAMVFQNYALYPHmSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 EN------IARFGEVQADK-VVEAARLAGVHELVLRLPQ----GydtvlgvggaglsggQRQRIALARALYGAPTLVVLD 493
Cdd:PRK11650 95 ENmayglkIRGMPKAEIEErVAEAARILELEPLLDRKPRelsgG---------------QRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKAR-GCTVLLITH---RAGVLgcADRLLALNAGQ 544
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHdqvEAMTL--ADRVVVMNGGV 212
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
128-295 |
9.70e-11 |
|
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: 62.88 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 128 QFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALA-LMALAWFNERATRAPLAkageLSIKSGQLAS---NNLR 203
Cdd:cd18569 113 NLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLnLLVLRLVSRKRVDLNRR----LLQDSGKLTGttmSGLQ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 204 NAEVIEAMGMLGSMRGRWERLHQAFLDQQSlaseRAARINALSKYLRIALQSL----VLGLGAWLAVEGRITPGMMIAGS 279
Cdd:cd18569 189 MIETLKASGAESDFFSRWAGYQAKVLNAQQ----ELGRTNQLLGALPTLLSALtnaaILGLGGLLVMDGALTIGMLVAFQ 264
|
170
....*....|....*.
gi 15596443 280 ILMGRALGPIDQLIGV 295
Cdd:cd18569 265 SLMASFLAPVNSLVGL 280
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
345-545 |
1.40e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.33 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIW-----PTLHGSVRLDGAEIRQYERETLGPRIGYLPQ--DIE 417
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 LFAGTVAENIArFGEVQ--ADKVVEAARLAGVHELVlRLPQGYdtvLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:PRK13645 103 LFQETIEKDIA-FGPVNlgENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596443 496 NSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDqVLRIADEVIVMHEGKV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
340-545 |
1.68e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 340 APPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQY---ERETLGprIGYLPQD- 415
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsprERRRLG--VAYIPEDr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 ------IELfagTVAENIA---------------RFGEVQ--ADKVVEAA--RLAGVHELVLRLPQGydtvlgvggagls 470
Cdd:COG3845 343 lgrglvPDM---SVAENLIlgryrrppfsrggflDRKAIRafAEELIEEFdvRTPGPDTPARSLSGG------------- 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 471 ggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLIThr-agVLGCADRLLALNAGQL 545
Cdd:COG3845 407 --NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISedldeILALSDRIAVMYEGRI 480
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
350-557 |
2.13e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 61.78 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 350 RGLTLAIpagsvvgvIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAE------------IR---QYERETLGPR--IGYL 412
Cdd:COG4167 38 AGQTLAI--------IGENGSGKSTLAKMLAGIIEPTSGEILINGHKleygdykyrckhIRmifQDPNTSLNPRlnIGQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 413 pQDIELFAGTVAENIARfgevqADKVVEAARLAGV---HELVlrlpqgYDTVLGVGgaglsggQRQRIALARALYGAPTL 489
Cdd:COG4167 110 -LEEPLRLNTDLTAEER-----EERIFATLRLVGLlpeHANF------YPHMLSSG-------QKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596443 490 VVLDEPNSNLDDS-GEQA--LLAAIQalKARGCTVLLITHRAGVLG-CADRLLALNAGQLHLYGERDQVLAA 557
Cdd:COG4167 171 IIADEALAALDMSvRSQIinLMLELQ--EKLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
349-566 |
2.58e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.87 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyeretlgpRIGYLpqdIELFAG-----TV 423
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSAL---LELGAGfhpelTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIaRFG---------EVQA--DKVVEaarLAGVHElVLRLP-----QGydtvlgvggaglsggQRQRIALARALYGAP 487
Cdd:COG1134 106 RENI-YLNgrllglsrkEIDEkfDEIVE---FAELGD-FIDQPvktysSG---------------MRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 488 TLVVLDEpnsnlddsgeqAL-----------LAAIQALKARGCTVLLITHRAGVLG--CaDRLLALNAGQLHLYGERDQV 554
Cdd:COG1134 166 DILLVDE-----------VLavgdaafqkkcLARIRELRESGRTVIFVSHSMGAVRrlC-DRAIWLEKGRLVMDGDPEEV 233
|
250
....*....|..
gi 15596443 555 LAALNNQRAASA 566
Cdd:COG1134 234 IAAYEALLAGRE 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
345-547 |
3.06e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETlgpRIGYlpQDIELFA-GTV 423
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDT---RLMF--QDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIArFG-----EVQADKVVEAARLAG-VHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNS 497
Cdd:PRK11247 99 IDNVG-LGlkgqwRDAALQALAAVGLADrANEWPAALSGG---------------QKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596443 498 NLDDSGEQALLAAIQAL-KARGCTVLLITHR-AGVLGCADRLLALNAGQLHL 547
Cdd:PRK11247 163 ALDALTRIEMQDLIESLwQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKIGL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-526 |
3.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLAR-----VVLGIWPTLHGSVRLDGAEIRQYERETLGPR--IGYLPQDIELFAG 421
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIEVRreVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArFGeVQADKVVEAAR-LAGVHELVLRLPQGYDTV---LGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK14267 100 lTIYDNVA-IG-VKLNGLVKSKKeLDERVEWALKKAALWDEVkdrLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190
....*....|....*....|....*....|
gi 15596443 497 SNLDDSGEQALLAAIQALKaRGCTVLLITH 526
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELK-KEYTIVLVTH 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-568 |
3.32e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPR--IGYLPQDIE--LFA 420
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRqqVATVFQDPEqqIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTVAENIA----RFGEVQAD---KVVEAARLAGV----HELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTL 489
Cdd:PRK13638 93 TDIDSDIAfslrNLGVPEAEitrRVDEALTLVDAqhfrHQPIQCLSHG---------------QKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVL-GCADRLLALNAGQLHLYGERDQVLAALNNQRAASASQ 568
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQ 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
345-544 |
4.18e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEI---RQYERETLgprIGYLPQDIelFAG 421
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEYKRAKY---IGRVFQDP--MMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 T-----VAENIA-------RFGEVQAdkvVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTL 489
Cdd:COG1101 93 TapsmtIEENLAlayrrgkRRGLRRG---LTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHR---AGVLGcaDRLLALNAGQ 544
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNmeqALDYG--NRLIMMHEGR 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
352-527 |
4.28e-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: 62.46 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEirqyeretlgpRIGYLPQDIELFAGTVAENIARFG 431
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFYVPQRPYMTLGTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 432 EVQ-------ADKVVEAArLAGVH-ELVLRLPQGYDTVlGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSG 503
Cdd:TIGR00954 540 SSEdmkrrglSDKDLEQI-LDNVQlTHILEREGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|....
gi 15596443 504 EQALLaaiQALKARGCTVLLITHR 527
Cdd:TIGR00954 618 EGYMY---RLCREFGITLFSVSHR 638
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
345-526 |
4.77e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.35 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTL--HGSVRLDGAEIRQ---YERETLGPRIGY-LPQDI-- 416
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLElepDERARAGLFLAFqYPEEIpg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 417 ---ELFAGTVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQRQRIALARALygAPTLVVLD 493
Cdd:TIGR01978 92 vsnLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRNEILQMALL--EPKLAILD 169
|
170 180 190
....*....|....*....|....*....|...
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:TIGR01978 170 EIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-510 |
6.73e-10 |
|
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: 59.73 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGS-----VVGVIGPSGSGKSSLARVvlgiwptLHGSVRLDGAEIrqyerETLGPRIGYLPQDIEL-FA 420
Cdd:cd03237 8 KTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKM-------LAGVLKPDEGDI-----EIELDTVSYKPQYIKAdYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTV----AENIARFGEvQADKVVEAARlagvhelvlrlPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:cd03237 76 GTVrdllSSITKDFYT-HPYFKTEIAK-----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170
....*....|....
gi 15596443 497 SNLDDsgEQALLAA 510
Cdd:cd03237 144 AYLDV--EQRLMAS 155
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
349-526 |
6.86e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.70 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIwPTLH---GSVRLDGAEIRQ---YERETLGprIGYLPQDIELFAG- 421
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEvtsGSILLDGEDILElspDERARAG--IFLAFQYPVEIPGv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 TV------AENIARFGEVQA----DKVVEAARLagvhelvLRLPQGYdtvlgvggaglsgGQR-----------QRIALA 480
Cdd:COG0396 93 SVsnflrtALNARRGEELSAreflKLLKEKMKE-------LGLDEDF-------------LDRyvnegfsggekKRNEIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 481 RALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
347-530 |
7.02e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETlgprIGYLPQDIELfagtVAEN 426
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEA----QKLLRQKIQI----VFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 427 iaRFGEVQADKVVE---------------AARLAGVHELV----LRlPQGYDtvlgVGGAGLSGGQRQRIALARALYGAP 487
Cdd:PRK11308 101 --PYGSLNPRKKVGqileepllintslsaAERREKALAMMakvgLR-PEHYD----RYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596443 488 TLVVLDEPNSNLDDSgEQA----LLAAIQalKARGCTVLLITHRAGV 530
Cdd:PRK11308 174 DVVVADEPVSALDVS-VQAqvlnLMMDLQ--QELGLSYVFISHDLSV 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
349-544 |
7.38e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDG-------AEIRQyeretlgprIGYLPQDIELFAG 421
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpAENRH---------VNTVFQSYALFPH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 -TVAENIArFG---------EVQAdKVVEAARLAGVHELVLRLPQgydtvlgvggaGLSGGQRQRIALARALYGAPTLVV 491
Cdd:PRK09452 101 mTVFENVA-FGlrmqktpaaEITP-RVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 492 LDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITH-RAGVLGCADRLLALNAGQ 544
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDGR 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
350-541 |
7.75e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 350 RGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRL-DGAEIRQYERETLGPRIGYLPQDIELFAGTVAENIA 428
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 ----------------------------------------------------------RFGEVQADKVVEAARLAGVHEL 450
Cdd:PTZ00265 482 yslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrkNYQTIKDSEVVDVSKKVLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 451 VLRLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTV-LLITHRAG 529
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLS 641
|
250
....*....|..
gi 15596443 530 VLGCADRLLALN 541
Cdd:PTZ00265 642 TIRYANTIFVLS 653
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
69-292 |
1.37e-09 |
|
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: 59.42 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 69 GVFVFMGALEA----LRSFVLVRVSERFDGQLHGRIYA------AAFERNLRaGGQEASQALHDLTTLRQFItGQALFAF 138
Cdd:cd18543 43 LLLLALGVAEAvlsfLRRYLAGRLSLGVEHDLRTDLFAhlqrldGAFHDRWQ-SGQLLSRATSDLSLVQRFL-AFGPFLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 139 FDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALAWFNER----ATRAPLAKAGELSiksgQLASNNLRNAEVIEAMGML 214
Cdd:cd18543 121 GNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRryfpASRRAQDQAGDLA----TVVEESVTGIRVVKAFGRE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 215 GSMRGRWERLHQAFLDQQSLASERAARINALSKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQL 292
Cdd:cd18543 197 RRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRML 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
349-526 |
1.71e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTlHGSVRLDGAEIRQYERETLGP---RIGYLPQDIELFAG---T 422
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLPvrhRIQVVFQDPNSSLNprlN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFGEV---------QADKVVEAARLAGVH-ELVLRLPQGYDtvlgvggaglsGGQRQRIALARALYGAPTLVVL 492
Cdd:PRK15134 381 VLQIIEEGLRVhqptlsaaqREQQVIAVMEEVGLDpETRHRYPAEFS-----------GGQRQRIAIARALILKPSLIIL 449
|
170 180 190
....*....|....*....|....*....|....*
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITH 526
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISH 484
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
342-527 |
2.24e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR-QYERETLGPRIGYLPQDIELFA 420
Cdd:PRK11288 15 PGVKA--LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENI------ARFGEVQADKVVEAARLAgVHELVLRL----PQGYDTVlgvggaglsgGQRQRIALARALYGAPTL 489
Cdd:PRK11288 93 EmTVAENLylgqlpHKGGIVNRRLLNYEAREQ-LEHLGVDIdpdtPLKYLSI----------GQRQMVEIAKALARNARV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596443 490 VVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
345-545 |
3.58e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERE----TLGPRIGYLPQ--DIEL 418
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirPVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIArFG----EVQADKVVEAArlagvHELVLRLpqGYD-TVLGVGGAGLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:PRK13646 99 FEDTVEREII-FGpknfKMNLDEVKNYA-----HRLLMDL--GFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAGVLGC-ADRLLALNAGQL 545
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARyADEVIVMKEGSI 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-557 |
4.12e-09 |
|
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: 59.31 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP----TLHGSVRLDGAEIRQYERETL----GPRIGYLP 413
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERELrrirGNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QdiE-------LFagTVAENIA-------RFGEVQA-DKVVEAARLAGVHELVLRLPQ-------Gydtvlgvggaglsg 471
Cdd:COG4172 99 Q--EpmtslnpLH--TIGKQIAevlrlhrGLSGAAArARALELLERVGIPDPERRLDAyphqlsgG-------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 472 gQRQRIALARALYGAPTLVVLDEPNSNLDDSgEQA----LLAAIQalKARGCTVLLITHRAGVLG-CADRLLALNAGQLH 546
Cdd:COG4172 161 -QRQRVMIAMALANEPDLLIADEPTTALDVT-VQAqildLLKDLQ--RELGMALLLITHDLGVVRrFADRVAVMRQGEIV 236
|
250
....*....|.
gi 15596443 547 LYGERDQVLAA 557
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-545 |
5.21e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGS--EARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDG----AEIRQYERETLGPRIGYLPQ- 414
Cdd:PRK13641 14 PGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 415 -DIELFAGTVAENIaRFGEVQADKVVEAARLAGVHELV-LRLPqgyDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVL 492
Cdd:PRK13641 94 pEAQLFENTVLKDV-EFGPKNFGFSEDEAKEKALKWLKkVGLS---EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRA-GVLGCADRLLALNAGQL 545
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
349-526 |
5.82e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLdgaeirqyereTLGPRIGYLPQDIELFAG-TVAENI 427
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-----------APGIKVGYLPQEPQLDPEkTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 -----------ARFGEVQA---------DKVV-EAARL------AGVHEL---------VLRLPQGyD---TVLGVGgag 468
Cdd:PRK11819 92 eegvaevkaalDRFNEIYAayaepdadfDALAaEQGELqeiidaADAWDLdsqleiamdALRCPPW-DakvTKLSGG--- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 469 lsggQRQRIALARALYGAPTLVVLDEPNSNLDdsGEQ-ALLAaiQALKARGCTVLLITH 526
Cdd:PRK11819 168 ----ERRRVALCRLLLEKPDMLLLDEPTNHLD--AESvAWLE--QFLHDYPGTVVAVTH 218
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
69-309 |
7.51e-09 |
|
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: 57.11 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 69 GVFVFMGALEALRSFVLVRVSERFDGQLHGRIYA-------AAFERNLraGGQEASQALHDLTTLRQFITGQALFAFFDA 141
Cdd:cd18546 47 AVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAhlqrlslDFHERET--SGRIMTRMTSDIDALSELLQTGLVQLVVSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 142 PWFPVYLLVIFLFDPWLGLLSLVgALALMALA--WFNERATRAPLAKAGELSIKSGQLaSNNLRNAEVIEAMGMLGSMRG 219
Cdd:cd18546 125 LTLVGIAVVLLVLDPRLALVALA-ALPPLALAtrWFRRRSSRAYRRARERIAAVNADL-QETLAGIRVVQAFRRERRNAE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 220 RWERLHQAFLDqqslASERAARINAL----SKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGV 295
Cdd:cd18546 203 RFAELSDDYRD----ARLRAQRLVAIyfpgVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQV 278
|
250
....*....|....
gi 15596443 296 WKQWGAARDAYRRL 309
Cdd:cd18546 279 FDSYQQARAALEKI 292
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-549 |
7.83e-09 |
|
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: 55.71 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG--IWPTLHGSVRLDGAEIRqyerETLGPRIGYLPQ-DIEL 418
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD----KNFQRSTGYVEQqDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAGTVAENIaRFgevqadkvveAARLAGVhelvlrlpqgydtvlgvggaglSGGQRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:cd03232 92 PNLTVREAL-RF----------SALLRGL----------------------SVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596443 499 LDDSGEQALLAAIQALKARGCTVLLITHR--AGVLGCADRLLAL-NAGQLHLYG 549
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAILCTIHQpsASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
118-309 |
9.89e-09 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 57.07 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 118 QALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMA--LAWFNERAtraplakagELSIKSG 195
Cdd:cd18571 103 QRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILwiLLFLKKRK---------KLDYKRF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 196 QLASNNLRNaeVIEamgMLGSM------------RGRWERLhqafldQQSLAseraaRINalSKYLRIA-LQS------- 255
Cdd:cd18571 174 DLSSENQSK--LIE---LINGMqeiklnnserqkRWEWERI------QAKLF-----KIN--IKSLKLDqYQQigalfin 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 256 -----LVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18571 236 qlkniLITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
345-556 |
1.23e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EART-LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGiwpTLHGSvRLDG---AEIRQYERETLgPRIGYLPQDIELFA 420
Cdd:PLN03211 79 QERTiLNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGN-NFTGtilANNRKPTKQIL-KRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENIARFGEVQADKVVEAARLAGVHELV---LRLPQGYDTVLGVG-GAGLSGGQRQRIALARALYGAPTLVVLDEP 495
Cdd:PLN03211 154 HlTVRETLVFCSLLRLPKSLTKQEKILVAESViseLGLTKCENTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 496 NSNLDDSGEQALLAAIQALKARGCTVLLITHRAG--VLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSsrVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
344-545 |
1.50e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLAR--------------VVLGIWPTLHGSVRLDGA-------------- 395
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalllpdtgtieWIFKDEKNKKKTKEKEKVleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 396 ----EIRQyeretlgpRIGYLPQDIE--LFAGTVAENIArFGEVQ--ADKVvEAARLAGVHELVLRLPQGYdtvLGVGGA 467
Cdd:PRK13651 98 kkikEIRR--------RVGVVFQFAEyqLFEQTIEKDII-FGPVSmgVSKE-EAKKRAAKYIELVGLDESY---LQRSPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 468 GLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRA-GVLGCADRLLALNAGQL 545
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKI 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-526 |
1.50e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP--TLHGSVRLDGAE-----IRQYERetLGprIGYLPQ 414
Cdd:NF040905 12 PGVKA--LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVcrfkdIRDSEA--LG--IVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 415 DIELFAG-TVAENI------ARFGEVQADKV-VEAARL---AGVHE----LVLRLPQGydtvlgvggaglsggQRQRIAL 479
Cdd:NF040905 86 ELALIPYlSIAENIflgnerAKRGVIDWNETnRRARELlakVGLDEspdtLVTDIGVG---------------KQQLVEI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596443 480 ARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
344-565 |
2.04e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIG---------YLPQ 414
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 415 DIELFAGTVAENIArfgevqaDKVVEAARLAGVHELVlrlpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDE 494
Cdd:PRK10938 94 GEDDTGRTTAEIIQ-------DEVKDPARCEQLAQQF-----GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 495 PNSNLDDSGEQALLAAIQALKARGCTVLLITHR----------AGVLgcADRllalnagQLHLYGERDQVLA-ALNNQRA 563
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITLVLVLNRfdeipdfvqfAGVL--ADC-------TLAETGEREEILQqALVAQLA 232
|
..
gi 15596443 564 AS 565
Cdd:PRK10938 233 HS 234
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
342-544 |
2.08e-08 |
|
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: 54.25 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLgiwpTLHGSVRLDGAEIRQYERETLgpRIGYLPQDIELFAG 421
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFSRNKLI--FIDQLQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 422 tvaeniarfgevqadkvveaarlagvhelVLRLPQGYDTVlgvggaglSGGQRQRIALARALYGAP--TLVVLDEPNSNL 499
Cdd:cd03238 78 -----------------------------YLTLGQKLSTL--------SGGELQRVKLASELFSEPpgTLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596443 500 DDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQ 544
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
344-555 |
2.21e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.47 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSL----ARVVlgiwPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELF 419
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLlsmiSRLL----PPDSGEVLVDGLDVATTPSRELAKRLAILRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 420 AG-TVAENIA--RF----GEVQAD---KVVEAARLAGVHELVLR----LPQGydtvlgvggaglsggQRQRIALARAL-- 483
Cdd:COG4604 88 SRlTVRELVAfgRFpyskGRLTAEdreIIDEAIAYLDLEDLADRyldeLSGG---------------QRQRAFIAMVLaq 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 484 ---YgaptlVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVLGC-ADRLLALNAGQLHLYGERDQVL 555
Cdd:COG4604 153 dtdY-----VLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEII 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
347-562 |
2.65e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIW---PTLHGSVRLDGAEIRQYERETLGPR-----IGYLPQDIEL 418
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARDIRksranTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 419 FAG-TVAENI---------------ARFGEVQADKVVEAARLAGV----HELVLRLPQGydtvlgvggaglsggQRQRIA 478
Cdd:PRK09984 98 VNRlSVLENVligalgstpfwrtcfSWFTREQKQRALQALTRVGMvhfaHQRVSTLSGG---------------QQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 479 LARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQvla 556
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQ--- 239
|
....*.
gi 15596443 557 aLNNQR 562
Cdd:PRK09984 240 -FDNER 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
353-555 |
2.88e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 353 TLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYE----RETLGPRIGYLPQDIELFAG-TVAENI 427
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 ArFG--------EVQADKVVEAARLAGVHELVlrlpQGYDTVLGVGgaglsggQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:PRK10070 128 A-FGmelaginaEERREKALDALRQVGLENYA----HSYPDELSGG-------MRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 500 DD---SGEQALLAAIQALKARgcTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVL 555
Cdd:PRK10070 196 DPlirTEMQDELVKLQAKHQR--TIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
349-545 |
2.97e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGP----RIGYLPQDIELFAGTVA 424
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 425 -ENIAR----FGEVQADKVVEAARL---AGVHELVLRLPqgydtvlgvggAGLSGGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK10584 106 lENVELpallRGESSRQSRNGAKALleqLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596443 497 SNLD-DSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAGQL 545
Cdd:PRK10584 175 GNLDrQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
352-530 |
2.99e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVV-LGIWP---TLH-------GSVRLDGAEIRQYEREtlgprIGYLPQDIELFA 420
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPrsgTLNiagnhfdFSKTPSDKAIRELRRN-----VGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENI--------------ARfgeVQADKVVEAARLAG-VHELVLRLPQGydtvlgvggaglsggQRQRIALARALY 484
Cdd:PRK11124 96 HlTVQQNLieapcrvlglskdqAL---ARAEKLLERLRLKPyADRFPLHLSGG---------------QQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 485 GAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGV 530
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEV 203
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
349-526 |
3.90e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.81 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVV--LGIwPTlHGSVRLDGAEI---------------RQYERetLGPRIGY 411
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCInlLET-PD-SGEIRVGGEEIrlkpdrdgelvpadrRQLQR--IRTRLGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQDIELFAG-TVAENIAR-----FGEVQADKVVEAARL---AGVHELVLRLPQ----GydtvlgvggaglsggQRQRIA 478
Cdd:COG4598 100 VFQSFNLWSHmTVLENVIEapvhvLGRPKAEAIERAEALlakVGLADKRDAYPAhlsgG---------------QQQRAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15596443 479 LARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
352-554 |
4.97e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPT---LHGSVRLDGAEI-----RQYER--------------ETLGP-- 407
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpeKELNKlraeqismifqdpmTSLNPym 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 408 RIGylPQDIELF--------AGTVAENIARFGEVqadKVVEAARLAGV--HELvlrlpqgydtvlgvggaglSGGQRQRI 477
Cdd:PRK09473 115 RVG--EQLMEVLmlhkgmskAEAFEESVRMLDAV---KMPEARKRMKMypHEF-------------------SGGMRQRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 478 ALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAGVL-GCADRLLALNAGQLHLYGERDQV 554
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVaGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
27-283 |
7.33e-08 |
|
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: 54.19 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 27 AAFSGVINLLMLVPSLYMLQVYDrVLSSANEVTLLMLTLMALGVFVFMGALEALRSFVLVRVSERFDGQLHGRIYAAAFE 106
Cdd:pfam00664 8 AILSGAISPAFPLVLGRILDVLL-PDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 107 RNL-----RAGGQEASQALHDLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMAL-AWFNERAT 180
Cdd:pfam00664 87 QPMsffdtNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVsAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 181 RAPLAKAGELSiKSGQLASNNLRNAEVIEAMGMLGSMRgrwERLHQAfLDQQSLASERAARINALS----KYLRIALQSL 256
Cdd:pfam00664 167 KLSRKEQKAVA-KASSVAEESLSGIRTVKAFGREEYEL---EKYDKA-LEEALKAGIKKAVANGLSfgitQFIGYLSYAL 241
|
250 260
....*....|....*....|....*..
gi 15596443 257 VLGLGAWLAVEGRITPGMMIAGSILMG 283
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
303-545 |
7.57e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 303 RDAYRRLSGLLDEFPARERRMEL-PEPRGHLLLES--LDAAPPGSEARTLRG----------------LTLAIPAGSVVG 363
Cdd:PRK15439 214 RDGTIALSGKTADLSTDDIIQAItPAAREKSLSASqkLWLELPGNRRQQAAGapvltvedltgegfrnISLEVRAGEILG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 364 VIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYE-RETLGPRIGYLPQDIE---LFA-GTVAENIARFGEVQ---- 434
Cdd:PRK15439 294 LAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDRQssgLYLdAPLAWNVCALTHNRrgfw 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 435 ADKVVEAARLAGVHE-LVLRLPQGYDTVlgvggAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQA 513
Cdd:PRK15439 374 IKPARENAVLERYRRaLNIKFNHAEQAA-----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS 448
|
250 260 270
....*....|....*....|....*....|...
gi 15596443 514 LKARGCTVLLITHR-AGVLGCADRLLALNAGQL 545
Cdd:PRK15439 449 IAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
352-554 |
1.18e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELF------AGTVAE 425
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFdqllgpEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIARFGEVQADKVVEAARLAGVHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGE- 504
Cdd:PRK10522 422 PALVEKWLERLKMAHKLELEDGRISNLKLSKG---------------QKKRLALLLALAEERDILLLDEWAADQDPHFRr 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 505 ---QALLAaiqALKARGCTVLLITHRAGVLGCADRLLALNAGQL-HLYG-ERDQV 554
Cdd:PRK10522 487 efyQVLLP---LLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLsELTGeERDAA 538
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
336-545 |
1.65e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 336 SLDAAPPgsearTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPT----LHGSVRLDG-----AEIRQYERETL- 405
Cdd:PRK10418 11 ALQAAQP-----LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvapCALRGRKIATIm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 406 -GPRIGYLPqdIELFAGTVAENIARFGEVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAglsggQRQRIALArALY 484
Cdd:PRK10418 86 qNPRSAFNP--LHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGML-----QRMMIALA-LLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 485 GAPTLVVlDEPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAGVLG-CADRLLALNAGQL 545
Cdd:PRK10418 158 EAPFIIA-DEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVArLADDVAVMSHGRI 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
347-543 |
1.94e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeiRQYERET------LGprIGYLPQDI---- 416
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKLDhklaaqLG--IGIIYQELsvid 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 417 ELfagTVAEN--IARF--GEVQADKVVEAARLAGVHELVLrLPQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVL 492
Cdd:PRK09700 94 EL---TVLENlyIGRHltKKVCGVNIIDWREMRVRAAMML-LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAG 543
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
342-527 |
2.05e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 342 PGSEArtLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR-QYERETLGPRIGYLPQDIELFA 420
Cdd:PRK10982 9 PGVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 G-TVAENI--ARFGE----VQADKVVEAARlAGVHELvlrlpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLD 493
Cdd:PRK10982 87 QrSVMDNMwlGRYPTkgmfVDQDKMYRDTK-AIFDEL------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190
....*....|....*....|....*....|....
gi 15596443 494 EPNSNLDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHK 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
349-535 |
2.68e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQ----YERET--LGPRIGYLPqDIELFAGT 422
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctYQKQLcfVGHRSGINP-YLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFGEVQADKVVEAARLagvhELVLRLPQGydtvlgvggaGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:PRK13540 96 LYDIHFSPGAVGITELCRLFSL----EHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180 190
....*....|....*....|....*....|...
gi 15596443 503 GEQALLAAIQALKARGCTVLLITHRAGVLGCAD 535
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
344-570 |
2.76e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeiRQYERET------LGprIGYLPQDIE 417
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG---NPCARLTpakahqLG--IYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 LFAG-TVAENIArFG----EVQADKVVEAARLAGVHeLVLRLPQGYDTVlgvggaglsgGQRQRIALARALYGAPTLVVL 492
Cdd:PRK15439 97 LFPNlSVKENIL-FGlpkrQASMQKMKQLLAALGCQ-LDLDSSAGSLEV----------ADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 493 DEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGE-----RDQVLAALN-NQRAAS 565
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTIALSGKtadlsTDDIIQAITpAAREKS 244
|
....*
gi 15596443 566 ASQQR 570
Cdd:PRK15439 245 LSASQ 249
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
349-538 |
5.12e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARvvlgiwptlhgsvrldgaeirqyeretlgprigylpqDIELFAGTVAENIA 428
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILD-------------------------------------AIGLALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADkVVEAARLAGVHELVLRLPQGydtvlgvggaglsggQRQRIALARAL----YGAPTLVVLDEPNSNLDDSGE 504
Cdd:cd03227 54 RRSGVKAG-CIVAAVSAELIFTRLQLSGG---------------EKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....
gi 15596443 505 QALLAAIQALKARGCTVLLITHRAGVLGCADRLL 538
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
351-543 |
8.81e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 351 GLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGpRIGYLP--QDIELFAG-TVAENI 427
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-RMGVVRtfQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 -------------------ARFGEVQADKVVEAA---RLAGVHELVLR----LPQGydtvlgvggaglsggQRQRIALAR 481
Cdd:PRK11300 102 lvaqhqqlktglfsgllktPAFRRAESEALDRAAtwlERVGLLEHANRqagnLAYG---------------QQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALNAG 543
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKlVMGISDRIYVVNQG 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
349-526 |
9.09e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPT---LHGSVRLDGAEIrqyERETLGPRIGYLPQDiELFAG--TV 423
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQD-DLFIPtlTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 424 AENIARFGEVQADKVVEAA-RLAGVHELV--LRLPQGYDTVLGVGGAGLSGG--QRQRIALARALYGAPTLVVLDEPNSN 498
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKeKRERVDEVLqaLGLRKCANTRIGVPGRVKGLSggERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180
....*....|....*....|....*...
gi 15596443 499 LDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
359-545 |
1.38e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVVLGIWPTLH-GSVRLDGAEIR-QYERETLGPRIGYLPQD------IELFAgtVAENIA-- 428
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgiVPILG--VGKNITls 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 ---RFGEVQadKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQrQRIALARALYGAPTLVVLDEPNSNLDDSGEQ 505
Cdd:TIGR02633 364 vlkSFCFKM--RIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQ-QKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596443 506 ALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQL 545
Cdd:TIGR02633 441 EIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
349-526 |
1.64e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARV--VLGIwP---TLH-------GSVRLDGAEIRQYEREtlgprIGYLPQDI 416
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVlnLLET-PdsgQLNiaghqfdFSQKPSEKAIRLLRQK-----VGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 417 ELFAG-TVAENI--------------ARFgevQADKVVEAARLAG-VHELVLRLPQGydtvlgvggaglsggQRQRIALA 480
Cdd:COG4161 92 NLWPHlTVMENLieapckvlglskeqARE---KAMKLLARLRLTDkADRFPLHLSGG---------------QQQRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596443 481 RALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
352-549 |
1.73e-06 |
|
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: 51.55 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIrQYERETLGPRIGYLPQDIELFAG-TVAENIARF 430
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 431 GEVQAdKVVEAARL--------AGVHELvlRLPQGYDtvlgvggagLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:TIGR01257 1028 AQLKG-RSWEEAQLemeamledTGLHHK--RNEEAQD---------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596443 503 GEQALLAAIqaLKAR-GCTVLLITH---RAGVLGcaDRLLALNAGQLHLYG 549
Cdd:TIGR01257 1096 SRRSIWDLL--LKYRsGRTIIMSTHhmdEADLLG--DRIAIISQGRLYCSG 1142
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
359-557 |
1.78e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVVLGIWPTLH-GSVRLDGAEIR-QYERETLGPRIGYLPQD-----IELFAGtVAENIA--- 428
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgIVPVMG-VGKNITlaa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 --RFgeVQADKVVEAARLAGVHELVLRLPQGYDTVLGVGGAGLSGGQrQRIALARALYGAPTLVVLDEPNSNLDDSGEQA 506
Cdd:PRK13549 367 ldRF--TGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQ-QKAVLAKCLLLNPKILILDEPTRGIDVGAKYE 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 507 LLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQL-------HLYGErdQVLAA 557
Cdd:PRK13549 444 IYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLkgdlinhNLTQE--QVMEA 500
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
349-394 |
1.90e-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: 49.07 E-value: 1.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDG 394
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
352-535 |
1.94e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.76 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETL---GPRIGYLPQDIELFAG-TVAENI 427
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDmNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 428 A-------RFGEVQADKVV----EAARLAGVHELVLRLPQGydtvlgvggaglsgGQRQRIALARALYGAPTLVVLDEPN 496
Cdd:PRK11831 106 AyplrehtQLPAPLLHSTVmmklEAVGLRGAAKLMPSELSG--------------GMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596443 497 SNLDDSGEQALLAAIQAL-KARGCTVLLITHRA-GVLGCAD 535
Cdd:PRK11831 172 VGQDPITMGVLVKLISELnSALGVTCVVVSHDVpEVLSIAD 212
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
343-537 |
2.10e-06 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLArvvlgiWPTLHgsvrldgAEIRQYERETLGP----RIGYLPQD--- 415
Cdd:cd03270 5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLA------FDTIY-------AEGQRRYVESLSAyarqFLGQMDKPdvd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 -IELFA------------------GTVAEnIARFGEVQADKVVEAARLagvhELVLRLPQGYDTvLGVGGAGLSGGQRQR 476
Cdd:cd03270 72 sIEGLSpaiaidqkttsrnprstvGTVTE-IYDYLRLLFARVGIRERL----GFLVDVGLGYLT-LSRSAPTLSGGEAQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 477 IALARALYGAPT--LVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRL 537
Cdd:cd03270 146 IRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-557 |
2.27e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETL--------------GPRIGYLPQ 414
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIelseqsaaqmrhvrGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 415 DI-----ELFagTVAENIARF-----GEVQADKVVEAARLAgvhELVlRLPQGyDTVLGVGGAGLSGGQRQRIALARALY 484
Cdd:PRK10261 112 EPmtslnPVF--TVGEQIAESirlhqGASREEAMVEAKRML---DQV-RIPEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 485 GAPTLVVLDEPNSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAGVLG-CADRLLALNAGQLHLYGERDQVLAA 557
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAeIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
359-532 |
2.36e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVVLG-IWPTLHGSVRLDGAEIRQYEREtlgprigylpqdielfagtvaeniarfgevqadk 437
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLD---------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 438 vveaarlagvhelvlrlpQGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAI------ 511
Cdd:smart00382 48 ------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlll 109
|
170 180
....*....|....*....|.
gi 15596443 512 QALKARGCTVLLITHRAGVLG 532
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG 130
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
352-528 |
2.85e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 352 LTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLP---QDIelfagTVAENIA 428
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPglkADL-----STLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 RFGEVQADKvveAARLAGVHELVLRLPQGYDTVLGVGGAGlsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALL 508
Cdd:PRK13543 105 FLCGLHGRR---AKQMPGSALAIVGLAGYEDTLVRQLSAG----QKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVN 177
|
170 180
....*....|....*....|
gi 15596443 509 AAIQALKARGCTVLLITHRA 528
Cdd:PRK13543 178 RMISAHLRGGGAALVTTHGA 197
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
348-557 |
3.64e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 348 TLR-GLTLAIpagsvvgvIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAE---------------IRQYERETLGPR--I 409
Cdd:PRK15112 35 TLReGQTLAI--------IGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysyrsqrirmIFQDPSTSLNPRqrI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 410 GYLpQDIELFAGTVAENIARfgevqADKVVEAARLAGVhelvlrLPQG---YDTVLGVGgaglsggQRQRIALARALYGA 486
Cdd:PRK15112 107 SQI-LDFPLRLNTDLEPEQR-----EKQIIETLRQVGL------LPDHasyYPHMLAPG-------QKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596443 487 PTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAGVLG-CADRLLALNAGQLHLYGERDQVLAA 557
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
305-526 |
4.10e-06 |
|
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: 49.55 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 305 AYRRLSGllDEFPARERRMEL---PEPR-GHLLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVL 380
Cdd:TIGR03719 292 RYEELLS--QEFQKRNETAEIyipPGPRlGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 381 GIWPTLHGSVRLDgaeirqyerETLgpRIGYLPQDIELFAG--TVAENIA------RFG--EVQADKVVEAARLAGV--H 448
Cdd:TIGR03719 370 GQEQPDSGTIEIG---------ETV--KLAYVDQSRDALDPnkTVWEEISggldiiKLGkrEIPSRAYVGRFNFKGSdqQ 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 449 ELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKarGCTVlLITH 526
Cdd:TIGR03719 439 KKVGQLSGG---------------ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAV-VISH 498
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
332-526 |
4.33e-06 |
|
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: 50.01 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 332 LLLESLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYEREtLGPRIGY 411
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-VHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 412 LPQ-DI--ELFAGTvaENIARFGEVQADKVVEAARLA--GVHELVLRLpqgYDTVLGVGGAGLsggQRQRIALARALYGA 486
Cdd:TIGR01257 2017 CPQfDAidDLLTGR--EHLYLYARLRGVPAEEIEKVAnwSIQSLGLSL---YADRLAGTYSGG---NKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15596443 487 PTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITH 526
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
349-527 |
6.08e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG--IWPTLHGSVRLDGAEIRQyerETLGPRIGYLPQ-DIELFAGTVAE 425
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGFPKKQ---ETFARISGYCEQnDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NI--ARF----GEVQ-------ADKVVEAARLAGVHELVLRLP--QGYDTvlgvggaglsgGQRQRIALARALYGAPTLV 490
Cdd:PLN03140 973 SLiySAFlrlpKEVSkeekmmfVDEVMELVELDNLKDAIVGLPgvTGLST-----------EQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR 527
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
312-543 |
6.08e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 312 LLDEFPARERRMELPEPRGHLLLE----SLDAAPPGSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSL-----ARVVLGI 382
Cdd:TIGR00956 738 LTDESDDVNDEKDMEKESGEDIFHwrnlTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGV 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 383 wptLHGSVRLDGAEIRQyerETLGPRIGYLPQ-DIELFAGTVAENIaRFGEV--QADKVVEAARLAGVHEL--VLRLPQG 457
Cdd:TIGR00956 818 ---ITGGDRLVNGRPLD---SSFQRSIGYVQQqDLHLPTSTVRESL-RFSAYlrQPKSVSKSEKMEYVEEVikLLEMESY 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 458 YDTVLGVGGAGLSGGQRQRIALARALYGAPTLVV-LDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR--AGVLGCA 534
Cdd:TIGR00956 891 ADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsAILFEEF 970
|
....*....
gi 15596443 535 DRLLALNAG 543
Cdd:TIGR00956 971 DRLLLLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
321-545 |
6.92e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 321 RRME-----LPEPRGHLLLESLDAAPPGseartLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGA 395
Cdd:PRK10762 240 RKLEdqyprLDKAPGEVRLKVDNLSGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 396 EIR-QYERETLGPRIGYLPQDIE---LFAG-TVAEN---------------IARFGEVQAdkVVEAARLAGVH----ELV 451
Cdd:PRK10762 315 EVVtRSPQDGLANGIVYISEDRKrdgLVLGmSVKENmsltalryfsraggsLKHADEQQA--VSDFIRLFNIKtpsmEQA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 452 LRLPQGydtvlgvggaglsgGQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGV 530
Cdd:PRK10762 393 IGLLSG--------------GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEV 458
|
250
....*....|....*
gi 15596443 531 LGCADRLLALNAGQL 545
Cdd:PRK10762 459 LGMSDRILVMHEGRI 473
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
474-555 |
9.68e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 474 RQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAGV---LgcADRLLALNAGQLHLYG 549
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVarlL--AHRLLVMKQGRVVESG 234
|
....*.
gi 15596443 550 ERDQVL 555
Cdd:PRK11701 235 LTDQVL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
343-544 |
1.32e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 343 GSEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPT-----LHGSVRLDGAEIRQYERETL----GPRIGYLP 413
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHASEQTLrgvrGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 QDielfaGTVAENIARFGEVQADKVV--------EAAR---LAGVHELVLRLPQGYdtvLGVGGAGLSGGQRQRIALARA 482
Cdd:PRK15134 99 QE-----PMVSLNPLHTLEKQLYEVLslhrgmrrEAARgeiLNCLDRVGIRQAAKR---LTDYPHQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 483 LYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKAR-GCTVLLITHRAG-VLGCADRLLALNAGQ 544
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSiVRKLADRVAVMQNGR 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
344-549 |
1.79e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.10 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPT---LHGSVRLDGAEI----RQYERETLgprigYLPQDI 416
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYkefaEKYPGEII-----YVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 417 ELFAG-TVAENIaRFgevqadkvveAARLAGvHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEP 495
Cdd:cd03233 93 VHFPTlTVRETL-DF----------ALRCKG-NEFVRGISGG---------------ERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 496 NSNLDDSGEQALLAAIQAL-KARGCTVLLITHRAG--VLGCADRLLALNAGQLHLYG 549
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMaDVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
338-571 |
2.95e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 338 DAAPPGSEART---LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGaeirqyERETLGPRIGYLPQ 414
Cdd:PRK13546 26 DALIPKHKNKTffaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 415 -----DIE---LFAGTVAENIARFgevqADKVVEAARLAG-VHELVLRLPQGydtvlgvggaglsggQRQRIALARALYG 485
Cdd:PRK13546 100 ltgieNIEfkmLCMGFKRKEIKAM----TPKIIEFSELGEfIYQPVKKYSSG---------------MRAKLGFSINITV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 486 APTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAG-VLGCADRLLALNAGQLHLYGERDQVL----AALNN 560
Cdd:PRK13546 161 NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGqVRQFCTKIAWIEGGKLKDYGELDDVLpkyeAFLND 240
|
250
....*....|.
gi 15596443 561 QRAASASQQRA 571
Cdd:PRK13546 241 FKKKSKAEQKE 251
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
475-540 |
3.66e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 475 QRIALARALYGA---PTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLAL 540
Cdd:PRK00635 816 QRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-526 |
3.73e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 356 IPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDgaeirqyeretlgPRIGYLPQDIEL-FAGTVAENIARFGEVQ 434
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPdYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 435 ADKVVEaarlagvHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDdsGEQALLAA--IQ 512
Cdd:PRK13409 429 GSSYYK-------SEIIKPL--QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVAkaIR 497
|
170
....*....|....*
gi 15596443 513 AL-KARGCTVLLITH 526
Cdd:PRK13409 498 RIaEEREATALVVDH 512
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
122-292 |
3.75e-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: 45.97 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 122 DLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGA-LALMALAWFNERATRAplakAGELSIKSGQLASn 200
Cdd:cd18564 120 DVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVApLLLLAARRFSRRIKEA----SREQRRREGALAS- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 201 nlRNAEVIEAMGMLGSMrGRWERLHQAFLDQ--QSL-ASERAARINALskYLR-----IAL-QSLVLGLGAWLAVEGRIT 271
Cdd:cd18564 195 --VAQESLSAIRVVQAF-GREEHEERRFAREnrKSLrAGLRAARLQAL--LSPvvdvlVAVgTALVLWFGAWLVLAGRLT 269
|
170 180
....*....|....*....|.
gi 15596443 272 PGMMIAGSILMGRALGPIDQL 292
Cdd:cd18564 270 PGDLLVFLAYLKNLYKPVRDL 290
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
475-540 |
3.80e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 3.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 475 QRIALARALYG---APTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLAL 540
Cdd:TIGR00630 836 QRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-545 |
4.44e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIwptLH---GSVRLDGAEIRQyERETLGPRIG-----------YLP- 413
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI---LVptsGEVRVLGYVPFK-RRKEFARRIGvvfgqrsqlwwDLPa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 414 -------QDI-ELFAGTVAENIARFGEvqadkvveaarLAGVHEL----VLRLPQGydtvlgvggaglsggQRQRIALAR 481
Cdd:COG4586 114 idsfrllKAIyRIPDAEYKKRLDELVE-----------LLDLGELldtpVRQLSLG---------------QRMRCELAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 482 ALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKA-RGCTVLLITHRAG-VLGCADRLLALNAGQL 545
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
69-309 |
5.42e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 45.50 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 69 GVFVFMGALEALRSFVLVRVSERFDGQLHGRIYA-------AAFERNLRagGQEASQALHDLTTLRQFITgQALFAFFDA 141
Cdd:cd18551 44 ALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRrllrlpvSFFDRRRS--GDLVSRVTNDTTLLRELIT-SGLPQLVTG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 142 PwfpVYLL--VIFLF--DPWLGLLSLVG-ALALMALAWFNERATRAPLAKAGELSIKSGQLaSNNLRNAEVIEAMG---- 212
Cdd:cd18551 121 V---LTVVgaVVLMFllDWVLTLVTLAVvPLAFLIILPLGRRIRKASKRAQDALGELSAAL-ERALSAIRTVKASNaeer 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 213 MLGSMRGRWERLHQAFLdqqslaseRAARINAL-SKYLRIALQS---LVLGLGAWLAVEGRITPGMMIAGSILMGRALGP 288
Cdd:cd18551 197 ETKRGGEAAERLYRAGL--------KAAKIEALiGPLMGLAVQLallVVLGVGGARVASGALTVGTLVAFLLYLFQLITP 268
|
250 260
....*....|....*....|.
gi 15596443 289 IDQLIGVWKQWGAARDAYRRL 309
Cdd:cd18551 269 LSQLSSFFTQLQKALGALERI 289
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
347-556 |
8.33e-05 |
|
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: 45.56 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI--WPTLHGSVRLDGAEIRQYERETLGPRIG---------YLPQD 415
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSKVGepcpvcggtLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 416 IELF--AGTVAENIAR------------FGEVQA-DKVVEAARLAGV--HELVLRLPQGYDTV-----LGVGGAGLSGGQ 473
Cdd:TIGR03269 94 VDFWnlSDKLRRRIRKriaimlqrtfalYGDDTVlDNVLEALEEIGYegKEAVGRAVDLIEMVqlshrITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 474 RQRIALARALYGAPTLVVLDEPNSNLDDsgEQALL---AAIQALKARGCTVLLITHRAGVLG-CADRLLALNAGQLHLYG 549
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDP--QTAKLvhnALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENGEIKEEG 251
|
....*..
gi 15596443 550 ERDQVLA 556
Cdd:TIGR03269 252 TPDEVVA 258
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
349-403 |
1.37e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLG--IWPTLHGSVRLDGAEIRQYERE 403
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE 79
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
354-531 |
1.92e-04 |
|
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: 43.51 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 354 LAIPA-GSVVGVIGPSGSGKSSLARVVLGI-------------WPTLHGSVRldGAEIRQYERETLGPRIGYL--PQDIE 417
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfddppdWDEILDEFR--GSELQNYFTKLLEGDVKVIvkPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 L----FAGTVAENIARFGEV-QADKVVEAARLAGVHEL-VLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVV 491
Cdd:cd03236 98 LipkaVKGKVGELLKKKDERgKLDELVDQLELRHVLDRnIDQLSGG---------------ELQRVAIAAALARDADFYF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15596443 492 LDEPNSNLDDsgEQALLAA--IQALKARGCTVLLITHRAGVL 531
Cdd:cd03236 163 FDEPSSYLDI--KQRLNAArlIRELAEDDNYVLVVEHDLAVL 202
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
346-376 |
2.17e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.17e-04
10 20 30
....*....|....*....|....*....|....
gi 15596443 346 ART--LRGLTLAIPAGSVVgVI-GPSGSGKSSLA 376
Cdd:COG0178 11 AREhnLKNIDVDIPRNKLV-VItGLSGSGKSSLA 43
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
345-526 |
2.49e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 345 EARTLRGLTLAIPAGSVVGVIGPSGSG--KSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLPQDIELFAGT 422
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 vaENIARFGEVqADKVVEAARlAGVHELVLRLpqGYDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDDS 502
Cdd:NF000106 105 --ENLYMIGR*-LDLSRKDAR-ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
170 180
....*....|....*....|....
gi 15596443 503 GEQALLAAIQALKARGCTVLLITH 526
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
356-526 |
2.62e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 42.37 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 356 IPAGSVVGVIGPSGSGKSSLA-----RVVLGI------WPTLHGSVRLDGAEIRqyeRETLGPRI----GYLPQDIELFA 420
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLAldlaaAVATGKpwlggpRVPEQGKVLYVSAEGP---ADELRRRLraagADLDLPARLLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 421 GTVAENIARFGEVQADKVVEAARlagvhelvlrlpqgydtvlgvggaglsggqRQRIALARALYGaPTLVVLDE-----P 495
Cdd:pfam13481 107 LSLVESLPLFFLDRGGPLLDADV------------------------------DALEAALEEVED-PDLVVIDPlaralG 155
|
170 180 190
....*....|....*....|....*....|..
gi 15596443 496 NSNLDDSGEQALLAAIQALKAR-GCTVLLITH 526
Cdd:pfam13481 156 GDENSNSDVGRLVKALDRLARRtGATVLLVHH 187
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
359-433 |
5.10e-04 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 41.23 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVV------LGIWPTLhgsvrLDGAEIRQyereTLGPRIGYLPQDIElfagtvaENIARFGE 432
Cdd:COG0529 16 GFVVWFTGLSGSGKSTLANALerrlfeRGRHVYL-----LDGDNVRH----GLNKDLGFSKEDRD-------ENIRRIGE 79
|
.
gi 15596443 433 V 433
Cdd:COG0529 80 V 80
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
349-556 |
5.75e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPRIGYLpQDIE---LFAGTVAE 425
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-ENIElkgLMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIARFgevqADKVVEAARLAG-VHELVLRLPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGE 504
Cdd:PRK13545 119 KIKEI----IPEIIEFADIGKfIYQPVKTYSSG---------------MKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15596443 505 QALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQLHLYGERDQVLA 556
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSlSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-526 |
7.62e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVvlgiwptLHGSVRLDGAEIRqyerETLgpRIGYLPQDIE-LFAGTVAENIarfGEVQADK 437
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKI-------LAGVLKPDEGEVD----EDL--KISYKPQYISpDYDGTVEEFL---RSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 438 V------VEAARLAGVHELVLR----LPQGydtvlgvggaglsggQRQRIALARALYGAPTLVVLDEPNSNLDdsGEQAL 507
Cdd:COG1245 430 FgssyykTEIIKPLGLEKLLDKnvkdLSGG---------------ELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRL 492
|
170 180
....*....|....*....|..
gi 15596443 508 LAA--IQAL-KARGCTVLLITH 526
Cdd:COG1245 493 AVAkaIRRFaENRGKTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-381 |
9.09e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 9.09e-04
10 20 30
....*....|....*....|....*....|.
gi 15596443 351 GLTLAIPAGSVVGVIGPSGSGKSSLARVVLG 381
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-545 |
1.08e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 341 PPGSEARTLRGL---------TLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIR-QYERETLGPRIG 410
Cdd:PRK11288 252 PLGEVRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 411 YLPQDIE---LFAG-TVAENIA--------RFGEV--------QADKVVEAARL--AGVHELVLRLPQGydtvlgvggag 468
Cdd:PRK11288 332 LCPEDRKaegIIPVhSVADNINisarrhhlRAGCLinnrweaeNADRFIRSLNIktPSREQLIMNLSGG----------- 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596443 469 lsggQRQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHR-AGVLGCADRLLALNAGQL 545
Cdd:PRK11288 401 ----NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
344-526 |
1.44e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 344 SEARTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERetlgPRIGYLPQDIEL-FAGT 422
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK----PYCTYIGHNLGLkLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 423 VAENIARFGEV-QADKVVEAArlagVHELVLrlpqgyDTVLGVGGAGLSGGQRQRIALARALYGAPTLVVLDEPNSNLDD 501
Cdd:PRK13541 87 VFENLKFWSEIyNSAETLYAA----IHYFKL------HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180
....*....|....*....|....*.
gi 15596443 502 SgEQALLAAIQALKAR-GCTVLLITH 526
Cdd:PRK13541 157 E-NRDLLNNLIVMKANsGGIVLLSSH 181
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
122-292 |
1.45e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 40.88 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 122 DLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALAWFNERATRAPLAKA----GELSiksgQL 197
Cdd:cd18542 105 DVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIreqeGELN----TV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 198 ASNNLRNAEVIEAMGMLGSMRGRWERLHQAFLDqqslASERAARInaLSKYLRI------ALQSLVLGLGAWLAVEGRIT 271
Cdd:cd18542 181 LQENLTGVRVVKAFAREDYEIEKFDKENEEYRD----LNIKLAKL--LAKYWPLmdflsgLQIVLVLWVGGYLVINGEIT 254
|
170 180
....*....|....*....|.
gi 15596443 272 PGMMIAGSILMGRALGPIDQL 292
Cdd:cd18542 255 LGELVAFISYLWMLIWPVRQL 275
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
343-415 |
2.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 343 GSEARTL-RGLTLAIPAGSVVGVIGPSGSGKSSLARvvlgiwpTLHGSVRLDGAEIRQYEREtlgpRIGYLPQD 415
Cdd:PRK15064 328 GFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLR-------TLVGELEPDSGTVKWSENA----NIGYYAQD 390
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
122-309 |
2.08e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 40.24 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 122 DLTTLRQFITGQALFAFFDAPWFPVYLLVIFLFDPWLGLLSLVGALALMALAWFNERATRAPLAKAGELSIKSGQLASNN 201
Cdd:cd18557 102 DTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEES 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 202 LRNAEVIEAMGMLGSMRGRWERLhqafLDQQSLASERAARINALSKYLRIALQSL----VLGLGAWLAVEGRITPGMMIA 277
Cdd:cd18557 182 LSNIRTVRSFSAEEKEIRRYSEA----LDRSYRLARKKALANALFQGITSLLIYLslllVLWYGGYLVLSGQLTVGELTS 257
|
170 180 190
....*....|....*....|....*....|....*
gi 15596443 278 ---GSILMGRALGpidQLIGVWKQWGAARDAYRRL 309
Cdd:cd18557 258 filYTIMVASSVG---GLSSLLADIMKALGASERV 289
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
349-531 |
2.12e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGI--WPTLHGSVRLDGAEIRQYERETLGPRIGYL----PQDI-----E 417
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMafqyPVEIpgvsnQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 LFAGTVAENIARFGEVQ-------ADKVVEAARLagvhelvLRLPQGYDTVLGVGGAGLSGGQRQRIALARALygAPTLV 490
Cdd:PRK09580 97 FFLQTALNAVRSYRGQEpldrfdfQDLMEEKIAL-------LKMPEDLLTRSVNVGFSGGEKKRNDILQMAVL--EPELC 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596443 491 VLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVL 531
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRIL 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
323-527 |
2.12e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 323 MELPEPRGHLLLESLDAAPPGSEART----------LRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP-------T 385
Cdd:PRK10938 240 VQLPEPDEPSARHALPANEPRIVLNNgvvsyndrpiLHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndlT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 386 LHGSVRLDGAEIRQYERetlgpRIGYLPQDIEL--FAGTVAEN--IARF----GEVQAdkVVEAARLAGVHELVLrlpQG 457
Cdd:PRK10938 320 LFGRRRGSGETIWDIKK-----HIGYVSSSLHLdyRVSTSVRNviLSGFfdsiGIYQA--VSDRQQKLAQQWLDI---LG 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 458 YDTVLGVGGAGLSGGQRQRIAL-ARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLL------------I 524
Cdd:PRK10938 390 IDKRTADAPFHSLSWGQQRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfvshhaedapacI 469
|
...
gi 15596443 525 THR 527
Cdd:PRK10938 470 THR 472
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
473-543 |
2.50e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596443 473 QRQRIALARALyGAP---TLVVLDEPNSNLDDSGEQALLAAIQALKARGCTVLLITHRAGVLGCADRLLALNAG 543
Cdd:PRK00635 481 EQERTALAKHL-GAEligITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
474-500 |
3.03e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 3.03e-03
10 20
....*....|....*....|....*..
gi 15596443 474 RQRIALARALYGAPTLVVLDEPNSNLD 500
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
475-535 |
3.05e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 3.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 475 QRIALARALYGA---PTLVVLDEPNSNL--DDsgEQALLAAIQALKARGCTVLLITHRAGVLGCAD 535
Cdd:COG0178 833 QRVKLASELSKRstgKTLYILDEPTTGLhfHD--IRKLLEVLHRLVDKGNTVVVIEHNLDVIKTAD 896
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
349-375 |
3.57e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 3.57e-03
10 20
....*....|....*....|....*..
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSL 375
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
347-514 |
3.91e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 39.42 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 347 RTLRGLTLAIPAGSVVGVIGPSGSGKSSLARVVLGIWP--------TLHGSVRLDGAEIRQYERETLGPRIGYLPQDIE- 417
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 418 LFAGTVAE--NIARFGEVQADKVVeAARLAGVHELVLRLPqGYDTVLGVGGAGLSGGQRQRIALARAL---------YGA 486
Cdd:PRK13547 95 AFAFSAREivLLGRYPHARRAGAL-THRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180
....*....|....*....|....*...
gi 15596443 487 PTLVVLDEPNSNLDDSGEQALLAAIQAL 514
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
354-545 |
3.95e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 354 LAIPAGSVVGVIGPSGSGKSSLARVvlgiwptLHGSVRLDGAEIrQYERETLGPRigyLPQD----IElfaGTV----AE 425
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKI-------LNGEVLLDDGRI-IYEQDLIVAR---LQQDpprnVE---GTVydfvAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 426 NIARFGEV--------------QADKVV-EAARLAGV--HELVLRLPQGYDTVLGVGGAGLSGG--------QRqRIALA 480
Cdd:PRK11147 90 GIEEQAEYlkryhdishlvetdPSEKNLnELAKLQEQldHHNLWQLENRINEVLAQLGLDPDAAlsslsggwLR-KAALG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 481 RALYGAPTLVVLDEPNSNLDdsgeqalLAAI----QALKARGCTVLLITH-RAGVLGCADRLLALNAGQL 545
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLD-------IETIewleGFLKTFQGSIIFISHdRSFIRNMATRIVDLDRGKL 231
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
356-549 |
3.96e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 356 IPAGSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAeirqyeretlgpRIGYLPQDIELFAGtvaeniarfgevqa 435
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYIDLSGG-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 436 dkvveaarlagvhELvlrlpqgydtvlgvggaglsggqrQRIALARALYGAPTLVVLDEPNSNLDDSGEQALLAAIQALK 515
Cdd:cd03222 76 -------------EL------------------------QRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 15596443 516 ARGC-TVLLITHRAGVLG-CADRLLALNaGQLHLYG 549
Cdd:cd03222 119 EEGKkTALVVEHDLAVLDyLSDRIHVFE-GEPGVYG 153
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
476-526 |
4.72e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 4.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15596443 476 RIALARALYGAPTLVVLDEPNSNLDdsgeqalLAAI----QALKARGCTVLLITH 526
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-------INTIrwleDVLNERNSTMIIISH 210
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
349-375 |
4.97e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.97e-03
10 20
....*....|....*....|....*..
gi 15596443 349 LRGLTLAIPAGSVVGVIGPSGSGKSSL 375
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
148-298 |
6.99e-03 |
|
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: 38.60 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 148 LLVIFLFDPWLGLLSLVGALALMALAWFNERATRaplaKAG-ELSIKSGQLASN---NLRNAEVIEAMGMLGSMRGRWER 223
Cdd:cd18545 132 VIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRAR----KAWqRVRKKISNLNAYlheSISGIRVIQSFAREDENEEIFDE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596443 224 LHQAFLDqqslASERAARINAL----SKYLRIALQSLVLGLGAWLAVEGRITPGMMIAGSILMGRALGPIDQLIGVWKQ 298
Cdd:cd18545 208 LNRENRK----ANMRAVRLNALfwplVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQ 282
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
366-435 |
7.39e-03 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 37.46 E-value: 7.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596443 366 GPSGSGKSSLARVV------LGIWPTLhgsvrLDGAEIrqyeRETLGPRIGYLPQDIElfagtvaENIARFGEVQA 435
Cdd:cd02027 6 GLSGSGKSTIARALeeklfqRGRPVYV-----LDGDNV----RHGLNKDLGFSREDRE-------ENIRRIAEVAK 65
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-554 |
7.46e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.07 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 359 GSVVGVIGPSGSGKSSLARVVLGIWPTLHGSVRLDGAEIRQYERETLGPrigyLPQDIEL-----FAG-----TVAENIA 428
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQA----LRRDIQFifqdpYASldprqTVGDSIM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596443 429 R--------FGEVQADKVVEAARLAGVH-ELVLRLPQGYDtvlgvggaglsGGQRQRIALARALYGAPTLVVLDEPNSNL 499
Cdd:PRK10261 426 EplrvhgllPGKAAAARVAWLLERVGLLpEHAWRYPHEFS-----------GGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596443 500 DDSGEQALLAAIQAL-KARGCTVLLITHRAGVLG-CADRLLALNAGQLHLYGERDQV 554
Cdd:PRK10261 495 DVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAV 551
|
|
| |
