NCBI Conserved Domain Search

Conserved domains on [gi|496950271|ref|WP_009417562|]

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ABC transporter ATP-binding protein [Capnocytophaga sp. oral taxon 335]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438555)

ABC transporter ATP-binding protein ABC transporter ATP-binding protein containing both ATPase and permease components of an ABC-type transport system

CATH: 3.40.50.300

EC: 7.-.-.-

Gene Ontology: GO:0055052|GO:0140359|GO:0042626|GO:0005524|GO:0016887

PubMed: 19234479|26517916|10529352|24638992|25750732

SCOP: 4003976

TCDB: 3.A.1

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

MdlB

COG1132

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

5-583

0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 692.68 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   5 TSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLF 84
Cdd:COG1132    2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  85 SYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDW 164
Cdd:COG1132   82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 165 KLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTI 244
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 245 WYNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDT 324
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL-TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 325 ETD-TETGGEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYID 403
Cdd:COG1132  321 PPEiPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 404 GVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAG 483
Cdd:COG1132  401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 484 QRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEE 563
Cdd:COG1132  481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560

                        570       580
                 ....*....|....*....|
gi 496950271 564 LLQiENGYYRNLYEVQFLEE 583
Cdd:COG1132  561 LLA-RGGLYARLYRLQFGEE 579

Name

Accession

Description

Interval

E-value

MdlB

COG1132

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

5-583

0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 692.68 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   5 TSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLF 84
Cdd:COG1132    2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  85 SYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDW 164
Cdd:COG1132   82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 165 KLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTI 244
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 245 WYNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDT 324
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL-TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 325 ETD-TETGGEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYID 403
Cdd:COG1132  321 PPEiPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 404 GVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAG 483
Cdd:COG1132  401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 484 QRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEE 563
Cdd:COG1132  481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560

                        570       580
                 ....*....|....*....|
gi 496950271 564 LLQiENGYYRNLYEVQFLEE 583
Cdd:COG1132  561 LLA-RGGLYARLYRLQFGEE 579

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

11-582

1.05e-138

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: 414.88 E-value: 1.05e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   11 TFRQLSRFVKPYRGVFIAVALFAVLssiFSTAQPYL---IKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYY 87
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMIL---VAATESTLaalLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   88 SNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLA 167
Cdd:TIGR02203  78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  168 LISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYN 247
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  248 SIFFPIGDLCVSITIALIVWFGGRQIiGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETD 327
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIALFQA-QAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  328 TETGGeKELKEVKGNIKFEDVRFEYV-AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVN 406
Cdd:TIGR02203 317 KDTGT-RAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  407 IEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPA-ITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQR 485
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  486 QLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555

                         570
                  ....*....|....*..
gi 496950271  566 QiENGYYRNLYEVQFLE 582
Cdd:TIGR02203 556 A-RNGLYAQLHNMQFRE 571

ABC_6TM_TmrA_like

cd18544

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...

26-318

3.16e-121

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 359.78 E-value: 3.16e-121

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITP--KDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKL 103
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 104 FAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRW 183
Cdd:cd18544   81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 184 FQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIA 263
Cdd:cd18544  161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 264 LIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18544  241 LVLWYGGGQVLSGAV-TLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294

PRK11176

lipid A ABC transporter ATP-binding protein/permease MsbA;

1-580

1.45e-118

lipid A ABC transporter ATP-binding protein/permease MsbA;

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 363.18 E-value: 1.45e-118

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   1 MSEKTSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTM 80
Cdd:PRK11176   2 HNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGIT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  81 QFLFSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLF----EMASdILKMFvit 156
Cdd:PRK11176  82 SFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALItvvrEGAS-IIGLF--- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 157 IVMFVIDWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKH 236
Cdd:PRK11176 158 IMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 237 KQAWLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASD 316
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTL-TAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 317 RVFAILDTETDTETGgEKELKEVKGNIKFEDVRFEYVAGEEI-LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL 395
Cdd:PRK11176 317 TLFAILDLEQEKDEG-KRVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 396 TSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITL-KNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVK 474
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 475 ERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGK 554
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555

                        570       580
                 ....*....|....*....|....*.
gi 496950271 555 IVEIGNHEELLQiENGYYRNLYEVQF 580
Cdd:PRK11176 556 IVERGTHAELLA-QNGVYAQLHKMQF 580

ABC_membrane

pfam00664

ABC transporter transmembrane region; This family represents a unit of six transmembrane ...

26-298

1.89e-49

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: 172.44 E-value: 1.89e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYE--GLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKL 103
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  104 FAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRW 183
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  184 FQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIA 263
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 496950271  264 LIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPI 298
Cdd:pfam00664 241 LALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274

GguA

NF040905

sugar ABC transporter ATP-binding protein;

359-557

2.02e-12

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 2.02e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTS--GAIYIDGvniEEYTLCSLR--EH--IATVLQDVFLFAD- 431
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRdsEAlgIVIIHQELALIPYl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 SIYNNITLKNP-----AITEEEVIAAAKSigvhnfLMS---LPEGYHYNVKERGAmlsaGQRQLIAFLRAYVHKPQILIL 503
Cdd:NF040905  94 SIAENIFLGNErakrgVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 504 DEATSSV-DSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:NF040905 164 DEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

354-550

5.94e-10

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.78 E-value: 5.94e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieEYTLCSLREHIA-------TVLQDV 426
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEvpdslplTVRDLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FL--FAD-SIYNNITLKNPAIteeeVIAAAKSIGVHNFLmslpegyhynvKERGAMLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:NF040873  79 AMgrWARrGLWRRLTRDDRAA----VDDALERVGLADLA-----------GRQLGELSGGQRQRALLAQGLAQEADLLLL 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 504 DEATSSVDSHSE----KLIQEATDkmtEGRTSIIIAHRLTTVKKADRIIVL 550
Cdd:NF040873 144 DEPTTGLDAESReriiALLAEEHA---RGATVVVVTHDLELVRRADPCVLL 191

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

369-552

3.29e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 3.29e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   369 GETIAIVGATGAGKTTITNLLNRFYDLTS-GAIYIDGVNIEEYTLCSLREHIatvlqdvflfadsiynnitlknpaitee 447
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII---------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   448 eviaaaksigvhnflmslpegyhynVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATD---- 523
Cdd:smart00382  54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108

                          170       180       190
                   ....*....|....*....|....*....|..
gi 496950271   524 ---KMTEGRTSIIIAHRLTTVKKADRIIVLDK 552
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRFDR 140

GguA

NF040905

sugar ABC transporter ATP-binding protein;

354-556

1.16e-04

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 1.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTIT-NLLNRFYDL-TSGAIYIDGVNIEEYTLCSLREH-IATVLQDV---- 426
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAgLAYVTEDRkgyg 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FLFADSIYNNITLKN-PAITEEEVIAAAKSIGVhnflmslPEGYHY-------NVKERGAMLSAGQRQLIAFLRAYVHKP 498
Cdd:NF040905 351 LNLIDDIKRNITLANlGKVSRRGVIDENEEIKV-------AEEYRKkmniktpSVFQKVGNLSGGNQQKVVLSKWLFTDP 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 499 QILILDEATSSVDSHSE----KLIQEATDkmtEGRTSIIIAHRLTTV-KKADRIIVLDKGKIV 556
Cdd:NF040905 424 DVLILDEPTRGIDVGAKyeiyTIINELAA---EGKGVIVISSELPELlGMCDRIYVMNEGRIT 483

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

480-511

4.41e-04

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 4.41e-04

                         10        20        30
                 ....*....|....*....|....*....|..
gi 496950271 480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

40850658_otr

NF000106

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;

477-564

7.05e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.95 E-value: 7.05e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 477 GAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGK 554
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGR 221

                         90
                 ....*....|
gi 496950271 555 IVEIGNHEEL 564
Cdd:NF000106 222 VIADGKVDEL 231

Name

Accession

Description

Interval

E-value

MdlB

COG1132

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

5-583

0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 692.68 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   5 TSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLF 84
Cdd:COG1132    2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  85 SYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDW 164
Cdd:COG1132   82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 165 KLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTI 244
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 245 WYNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDT 324
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL-TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 325 ETD-TETGGEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYID 403
Cdd:COG1132  321 PPEiPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 404 GVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAG 483
Cdd:COG1132  401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 484 QRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEE 563
Cdd:COG1132  481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560

                        570       580
                 ....*....|....*....|
gi 496950271 564 LLQiENGYYRNLYEVQFLEE 583
Cdd:COG1132  561 LLA-RGGLYARLYRLQFGEE 579

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

3-579

1.17e-165

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: 488.57 E-value: 1.17e-165

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   3 EKTSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQF 82
Cdd:COG2274  135 DKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  83 LFSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVI 162
Cdd:COG2274  215 LRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR-FRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFY 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 163 DWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLK 242
Cdd:COG2274  294 SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 243 TIWYNSIFFPIGDLCVSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAIL 322
Cdd:COG2274  374 LRRLSNLLSTLSGLLQQLATVALLWLGAYLVI-DGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL 452

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 323 DTETDTETGGEK-ELKEVKGNIKFEDVRFEY-VAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAI 400
Cdd:COG2274  453 DLPPEREEGRSKlSLPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI 532

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 401 YIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAML 480
Cdd:COG2274  533 LIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 481 SAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGN 560
Cdd:COG2274  613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692

                        570
                 ....*....|....*....
gi 496950271 561 HEELLQiENGYYRNLYEVQ 579
Cdd:COG2274  693 HEELLA-RKGLYAELVQQQ 710

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

11-582

1.05e-138

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 414.88 E-value: 1.05e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   11 TFRQLSRFVKPYRGVFIAVALFAVLssiFSTAQPYL---IKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYY 87
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMIL---VAATESTLaalLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   88 SNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLA 167
Cdd:TIGR02203  78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  168 LISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYN 247
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  248 SIFFPIGDLCVSITIALIVWFGGRQIiGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETD 327
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIALFQA-QAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  328 TETGGeKELKEVKGNIKFEDVRFEYV-AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVN 406
Cdd:TIGR02203 317 KDTGT-RAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  407 IEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPA-ITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQR 485
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  486 QLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555

                         570
                  ....*....|....*..
gi 496950271  566 QiENGYYRNLYEVQFLE 582
Cdd:TIGR02203 556 A-RNGLYAQLHNMQFRE 571

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

13-580

6.51e-126

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: 382.13 E-value: 6.51e-126

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   13 RQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLG 92
Cdd:TIGR02204   7 AALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   93 QTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGlFEMASDILKMFV-ITIVMFVIDWKLALISY 171
Cdd:TIGR02204  87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSS-LSMALRNALMCIgGLIMMFITSPKLTSLVL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  172 ATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEK---------HKQAWLK 242
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKayeaarqriRTRALLT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  243 TIwynSIFFPIGdlcvsiTIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAIL 322
Cdd:TIGR02204 246 AI---VIVLVFG------AIVGVLWVGAHDVIAGKM-SAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  323 DTETDTETGGEKEL--KEVKGNIKFEDVRFEYVAGEE--ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSG 398
Cdd:TIGR02204 316 QAEPDIKAPAHPKTlpVPLRGEIEFEQVNFAYPARPDqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  399 AIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGA 478
Cdd:TIGR02204 396 RILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGV 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  479 MLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEI 558
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQ 555

                         570       580
                  ....*....|....*....|..
gi 496950271  559 GNHEELLQiENGYYRNLYEVQF 580
Cdd:TIGR02204 556 GTHAELIA-KGGLYARLARLQF 576

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

13-566

1.69e-125

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: 380.64 E-value: 1.69e-125

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  13 RQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPK-DYEGLVRIVYILIALLCAEVTMQFLFSYYSNWL 91
Cdd:COG4988    6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  92 GQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISY 171
Cdd:COG4988   86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 172 ATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKT--IWYNSI 249
Cdd:COG4988  166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVlrVAFLSS 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 250 FfpIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETDTE 329
Cdd:COG4988  246 A--VLEFFASLSIALVAVYIGFRLLGGSL-TLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 330 TGGEKELKEVKGN-IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIE 408
Cdd:COG4988  323 PAGTAPLPAAGPPsIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 409 EYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLI 488
Cdd:COG4988  403 DLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRL 482

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 489 AFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG4988  483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560

ABC_6TM_TmrA_like

cd18544

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...

26-318

3.16e-121

Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 359.78 E-value: 3.16e-121

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITP--KDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKL 103
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 104 FAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRW 183
Cdd:cd18544   81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 184 FQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIA 263
Cdd:cd18544  161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 264 LIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18544  241 LVLWYGGGQVLSGAV-TLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294

PRK11176

lipid A ABC transporter ATP-binding protein/permease MsbA;

1-580

1.45e-118

lipid A ABC transporter ATP-binding protein/permease MsbA;

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 363.18 E-value: 1.45e-118

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   1 MSEKTSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTM 80
Cdd:PRK11176   2 HNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGIT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  81 QFLFSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLF----EMASdILKMFvit 156
Cdd:PRK11176  82 SFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALItvvrEGAS-IIGLF--- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 157 IVMFVIDWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKH 236
Cdd:PRK11176 158 IMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 237 KQAWLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASD 316
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTL-TAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 317 RVFAILDTETDTETGgEKELKEVKGNIKFEDVRFEYVAGEEI-LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL 395
Cdd:PRK11176 317 TLFAILDLEQEKDEG-KRVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 396 TSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITL-KNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVK 474
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 475 ERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGK 554
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555

                        570       580
                 ....*....|....*....|....*.
gi 496950271 555 IVEIGNHEELLQiENGYYRNLYEVQF 580
Cdd:PRK11176 556 IVERGTHAELLA-QNGVYAQLHKMQF 580

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

22-579

6.93e-117

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: 359.90 E-value: 6.93e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  22 YRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYeglvrIVYILIALLCAEVTMQF---LFSYYSNWL----GQT 94
Cdd:COG5265   34 RRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAA-----LLVVPVGLLLAYGLLRLlsvLFGELRDALfarvTQR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  95 VIRDVREKLFAHLLRFKMRY-FDKSSIGVlvTRavnDMER----IGEIFSSGLFEMASDILKM-FVITIVMFVIDWKLAL 168
Cdd:COG5265  109 AVRRLALEVFRHLHALSLRFhLERQTGGL--SR---DIERgtkgIEFLLRFLLFNILPTLLEIaLVAGILLVKYDWWFAL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 169 ISYATmpLILY------FTRW---FQRSMNAAFVEVRHQVAN--LNAfvqERIsgikvlQLFAQEREELENFKKINEKHK 237
Cdd:COG5265  184 ITLVT--VVLYiaftvvVTEWrtkFRREMNEADSEANTRAVDslLNY---ETV------KYFGNEAREARRYDEALARYE 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 238 QAWLKTiwYNSIFF-PIG-DLCVSITIALIVWFGGRQI------IGDNVydLGNIFLfIQLSQQL------FRPIRHiad 303
Cdd:COG5265  253 RAAVKS--QTSLALlNFGqALIIALGLTAMMLMAAQGVvagtmtVGDFV--LVNAYL-IQLYIPLnflgfvYREIRQ--- 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 304 kfntlqmGIIASDRVFAILDTETD-TETGGEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGK 382
Cdd:COG5265  325 -------ALADMERMFDLLDQPPEvADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 383 TTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFL 462
Cdd:COG5265  398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 463 MSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVK 542
Cdd:COG5265  478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557

                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 496950271 543 KADRIIVLDKGKIVEIGNHEELLQiENGYYRNLYEVQ 579
Cdd:COG5265  558 DADEILVLEAGRIVERGTHAELLA-QGGLYAQMWARQ 593

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

341-567

1.14e-112

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: 335.35 E-value: 1.14e-112

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 341 GNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIA 420
Cdd:cd03254    1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQI 500
Cdd:cd03254   81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 501 LILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQI 567
Cdd:cd03254  161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

343-576

4.13e-109

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: 326.50 E-value: 4.13e-109

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYV-AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIAT 421
Cdd:cd03251    1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQIL 501
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 502 ILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNLY 576
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKLH 234

3a01208

TIGR00958

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]

6-572

1.81e-103

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 328.22 E-value: 1.81e-103

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    6 SRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFS 85
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRG 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   86 YYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWK 165
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  166 LALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIW 245
Cdd:TIGR00958 303 LTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKAL 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  246 YNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDTE 325
Cdd:TIGR00958 383 AYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKV-SSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRK 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  326 TDTETGGEKELKEVKGNIKFEDVRFEYVAGEE--ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYID 403
Cdd:TIGR00958 462 PNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  404 GVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAG 483
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  484 QRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEatDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEE 563
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699


                  ....*....
gi 496950271  564 LLQIENGYY 572
Cdd:TIGR00958 700 LMEDQGCYK 708

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

343-579

4.98e-103

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: 311.09 E-value: 4.98e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:cd03253    1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNLYEVQ 579
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

343-579

2.09e-101

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: 306.77 E-value: 2.09e-101

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVA--GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIA 420
Cdd:cd03249    1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQI 500
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 501 LILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNLYEVQ 579
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

11-577

1.50e-96

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: 305.92 E-value: 1.50e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  11 TFRQLSRFVKPYRGVFIAVALFAVLSSIFSTA--------------QPylikvAIDNYITPKdyeGLVRivyiliallca 76
Cdd:COG4987    2 DLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGllalsgwliaaaalAP-----PILNLFVPI---VGVR----------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  77 evtmqfLFSyysnwLGQTVIR----------------DVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSS 140
Cdd:COG4987   63 ------AFA-----IGRTVFRylerlvshdatlrllaDLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLR 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 141 GLFEMASDILKMFVITIVMFVIDWKLALISYATMPLIL----YFTRWFQRSMNAAFVEVRhqvANLNAFVQERISGIKVL 216
Cdd:COG4987  132 VLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGlllpLLAARLGRRAGRRLAAAR---AALRARLTDLLQGAAEL 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 217 QLFAQEREELENFKKINEK-----HKQAWLkTIWYNSIFFpigdLCVSITIALIVWFGGRQIiGDNVYDLGNIFLFIQLS 291
Cdd:COG4987  209 AAYGALDRALARLDAAEARlaaaqRRLARL-SALAQALLQ----LAAGLAVVAVLWLAAPLV-AAGALSGPLLALLVLAA 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 292 QQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETDTETGGEKELKEVKGNIKFEDVRFEYV-AGEEILHGISFEVKEGE 370
Cdd:COG4987  283 LALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPgAGRPVLDGLSLTLPPGE 362

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 371 TIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVI 450
Cdd:COG4987  363 RVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELW 442

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 451 AAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRT 530
Cdd:COG4987  443 AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT 522

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 496950271 531 SIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNLYE 577
Cdd:COG4987  523 VLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA-QNGRYRQLYQ 568

PRK10790

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;

11-579

1.90e-91

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 293.16 E-value: 1.90e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  11 TFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYE-----GLVrIVYILIALLCAevTMQFLFS 85
Cdd:PRK10790  10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPlglvaGLA-AAYVGLQLLAA--GLHYAQS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  86 YYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIF---SSGLFEMASDILKMFVitiVMFVI 162
Cdd:PRK10790  87 LLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYvtvVATVLRSAALIGAMLV---AMFSL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 163 DWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLK 242
Cdd:PRK10790 164 DWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQ 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 243 TIWYN--------SIFFPIgDLCvsitiALIVWFG--GRQIIGdnvydLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGI 312
Cdd:PRK10790 244 TLRLDgfllrpllSLFSAL-ILC-----GLLMLFGfsASGTIE-----VGVLYAFISYLGRLNEPLIELTTQQSMLQQAV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 313 IASDRVFAILDTETdtETGGEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRF 392
Cdd:PRK10790 313 VAGERVFELMDGPR--QQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 393 YDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPaITEEEVIAAAKSIGVHNFLMSLPEGYHYN 472
Cdd:PRK10790 391 YPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTP 469

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 473 VKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDK 552
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549

                        570       580
                 ....*....|....*....|....*..
gi 496950271 553 GKIVEIGNHEELLQiENGYYRNLYEVQ 579
Cdd:PRK10790 550 GQAVEQGTHQQLLA-AQGRYWQMYQLQ 575

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

147-581

1.47e-90

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 290.71 E-value: 1.47e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 147 SDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREEL 226
Cdd:PRK13657 139 ATLVALVVLLPLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAET 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 227 ENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIaLIVWFGGRQIIGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFN 306
Cdd:PRK13657 219 QALRDIADNLLAAQMPVLSWWALASVLNRAASTITM-LAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFIN 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 307 TLQMGIIASDRVFAILDTETDT-ETGGEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTI 385
Cdd:PRK13657 298 QVFMAAPKLEEFFEVEDAVPDVrDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 386 TNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSL 465
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERK 457

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 466 PEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKAD 545
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNAD 537

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 496950271 546 RIIVLDKGKIVEIGNHEELLQiENGYYRNLYEVQFL 581
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVA-RGGRFAALLRAQGM 572

ABC_6TM_YknV_like

cd18545

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...

26-318

3.19e-88

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: 275.12 E-value: 3.19e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18545    2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18545   82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18545  162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18545  242 YWYGGKLVLGGAI-TVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

343-579

9.48e-86

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: 266.66 E-value: 9.48e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVA-GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIAT 421
Cdd:cd03252    1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQIL 501
Cdd:cd03252   81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 502 ILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNLYEVQ 579
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQLQ 237

ABC_6TM_exporters

cd07346

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...

26-318

1.05e-85

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: 268.26 E-value: 1.05e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd07346   81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd07346  161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd07346  241 LLYGGYLVLQGSL-TIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

22-550

5.55e-85

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: 274.55 E-value: 5.55e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   22 YRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKdyEGLVRIVyILIALLCAEVTMQFLFSYYSNWLGQT----VIR 97
Cdd:TIGR02857   1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAG--EPLAELL-PALGALALVLLLRALLGWLQERAAARaaaaVKS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   98 DVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLI 177
Cdd:TIGR02857  78 QLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  178 LYFTrWFQRSMNAAFVEVRHQV-ANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKT--IWYNSIFfpIG 254
Cdd:TIGR02857 158 PIFM-ILIGWAAQAAARKQWAAlSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVlrIAFLSSA--VL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  255 DLCVSITIALI-VWFGGRQIIGDnvYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETDTETGGE 333
Cdd:TIGR02857 235 ELFATLSVALVaVYIGFRLLAGD--LDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  334 KELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLC 413
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  414 SLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRA 493
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271  494 YVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVL 550
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529

NHLM_micro_ABC1

TIGR03796

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...

4-575

1.17e-77

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: 259.88 E-value: 1.17e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    4 KTSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVriVYILIALLCAevtmqfL 83
Cdd:TIGR03796 134 KGGRKPSLLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLR--PLLLGMGLTA------L 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   84 FSYYSNWLGQTVIRDVREKL--------FAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVI 155
Cdd:TIGR03796 206 LQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASR-VQLNDQVAEFLSGQLATTALDAVMLVFY 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  156 TIVMFVIDWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVqerISGIKVLQLFAQEREELENF------ 229
Cdd:TIGR03796 285 ALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVA---ISGLQSIETLKASGLESDFFsrwagy 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  230 --KKINEKHK----QAWLKTiwynsifFPigDLCVSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIAD 303
Cdd:TIGR03796 362 qaKLLNAQQElgvlTQILGV-------LP--TLLTSLNSALILVVGGLRVM-EGQLTIGMLVAFQSLMSSFLEPVNNLVG 431

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  304 KFNTLQM---GIIASDRVF----AILDTETDTETGGEKELKEVKGNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIV 375
Cdd:TIGR03796 432 FGGTLQElegDLNRLDDVLrnpvDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSPLEPpLIENFSLTLQPGQRVALV 511

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  376 GATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKS 455
Cdd:TIGR03796 512 GGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKD 591

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  456 IGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKmtEGRTSIIIA 535
Cdd:TIGR03796 592 AAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVA 669

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 496950271  536 HRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNL 575
Cdd:TIGR03796 670 HRLSTIRDCDEIIVLERGKVVQRGTHEELWA-VGGAYARL 708

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

343-554

2.54e-74

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: 234.20 E-value: 2.54e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEY-VAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIAT 421
Cdd:cd03228    1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFADSIYNNItlknpaiteeeviaaaksigvhnflmslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQIL 501
Cdd:cd03228   81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 502 ILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGK 554
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

341-556

1.17e-71

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: 229.40 E-value: 1.17e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 341 GNIKFEDVRFEYVAGE-EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHI 419
Cdd:cd03245    1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:cd03245   81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 500 ILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIV 556
Cdd:cd03245  161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

341-560

9.72e-71

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: 226.99 E-value: 9.72e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 341 GNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHI 419
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFADSIYNNITLKNPAiTEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:cd03244   81 SIIPQDPVLFSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 500 ILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGN 560
Cdd:cd03244  160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220

PRK10789

SmdA family multidrug ABC transporter permease/ATP-binding protein;

29-582

1.41e-70

SmdA family multidrug ABC transporter permease/ATP-binding protein;

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 237.69 E-value: 1.41e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  29 VALFAVLSsIFSTAQPYLIKVAIDNyITPKDYEGLVRIVYILIALLCAEVTmqFLFSY-YSNWLGQTVIR---DVREKLF 104
Cdd:PRK10789   1 VALLIIIA-MLQLIPPKVVGIIVDG-VTEQHMTTGQILMWIGTMVLIAVVV--YLLRYvWRVLLFGASYQlavELREDFY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 105 AHLLRFKMRYFDKSSIGVLVTRAVNDMERIgeIFSSG---LFEMASDILKMFVItIVMFV-IDWKLALISYATMPLIL-- 178
Cdd:PRK10789  77 RQLSRQHPEFYLRHRTGDLMARATNDVDRV--VFAAGegvLTLVDSLVMGCAVL-IVMSTqISWQLTLLALLPMPVMAim 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 179 ---YFTRWFQR--SMNAAFvevrhqvANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPi 253
Cdd:PRK10789 154 ikrYGDQLHERfkLAQAAF-------SSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 254 gdlcvSITIA-----LIVWFGGRQIIGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDtETDT 328
Cdd:PRK10789 226 -----TIYIAigmanLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLA-EAPV 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 329 ETGGEKELKEVKGNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI 407
Cdd:PRK10789 300 VKDGSEPVPEGRGELDVNIRQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 408 EEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQL 487
Cdd:PRK10789 380 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQR 459

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 488 IAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQi 567
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ- 538

                        570
                 ....*....|....*
gi 496950271 568 ENGYYRNLYEVQFLE 582
Cdd:PRK10789 539 QSGWYRDMYRYQQLE 553

ABC_6TM_YknU_like

cd18542

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...

26-318

1.13e-69

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: 226.54 E-value: 1.13e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18542    1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18542   81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18542  161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18542  241 LWVGGYLVINGEI-TLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

5-578

5.56e-69

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]

Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 236.56 E-value: 5.56e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    5 TSRTKHTFRQLSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYItPKDYEGLVRIVYI-LIALLCAEVTMQFL 83
Cdd:TIGR01193 137 IKEKENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYI-PHKMMGTLGIISIgLIIAYIIQQILSYI 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   84 FSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVID 163
Cdd:TIGR01193 216 QIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSR-FTDASSIIDALASTILSLFLDMWILVIVGLFLVRQN 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  164 WKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREeleNFKKINEKHKQAWLKT 243
Cdd:TIGR01193 295 MLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAE---RYSKIDSEFGDYLNKS 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  244 IWYNSIFFPIGDLCVSITIALIV---WFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFA 320
Cdd:TIGR01193 372 FKYQKADQGQQAIKAVTKLILNVvilWTGAYLVMRGKL-TLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNE 450

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  321 ILDTETDTETGGEK-ELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGA 399
Cdd:TIGR01193 451 VYLVDSEFINKKKRtELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  400 IYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITL-KNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGA 478
Cdd:TIGR01193 531 ILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGS 610

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  479 MLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEgRTSIIIAHRLTTVKKADRIIVLDKGKIVEI 558
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689

                         570       580
                  ....*....|....*....|
gi 496950271  559 GNHEELLQiENGYYRNLYEV 578
Cdd:TIGR01193 690 GSHDELLD-RNGFYASLIHN 708

ABC_6TM_Rv0194_D2_like

cd18546

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...

26-318

8.17e-69

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: 224.29 E-value: 8.17e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18546    1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18546   81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18546  161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18546  241 LLVGAWRVAAGTL-TVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292

NHLM_micro_ABC2

TIGR03797

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...

11-579

1.26e-68

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: 235.24 E-value: 1.26e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   11 TFRQLSRF-VKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYysn 89
Cdd:TIGR03797 122 GLRDLLRFaLRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSL--- 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   90 wlgqTVIR-------DVREKLFAHLLRFKMRYFDKSSIGVLVTRAvNDMERIGEIFS-SGLFEMASDILKMFVItIVMFV 161
Cdd:TIGR03797 199 ----AVLRletrmdaSLQAAVWDRLLRLPVSFFRQYSTGDLASRA-MGISQIRRILSgSTLTTLLSGIFALLNL-GLMFY 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  162 IDWKLALISYATMPLILYFTRW---FQRSMNAAFVEVRhqvANLNAFVQERISGIKVL--------------QLFAQERE 224
Cdd:TIGR03797 273 YSWKLALVAVALALVAIAVTLVlglLQVRKERRLLELS---GKISGLTVQLINGISKLrvagaenrafarwaKLFSRQRK 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  225 ELENFKKInekhkQAWLKTIwyNSIFfPIgdlcvsITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADK 304
Cdd:TIGR03797 350 LELSAQRI-----ENLLTVF--NAVL-PV------LTSAALFAAAISLLGGAGL-SLGSFLAFNTAFGSFSGAVTQLSNT 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  305 FNTLQMGIIASDRVFAILDTETdtETGGEKELK-EVKGNIKFEDVRFEYVA-GEEILHGISFEVKEGETIAIVGATGAGK 382
Cdd:TIGR03797 415 LISILAVIPLWERAKPILEALP--EVDEAKTDPgKLSGAIEVDRVTFRYRPdGPLILDDVSLQIEPGEFVAIVGPSGSGK 492

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  383 TTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPaITEEEVIAAAKSIGVHNFL 462
Cdd:TIGR03797 493 STLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDI 571

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  463 MSLPEGYHYNVKERGAMLSAGQRQ--LIAflRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMteGRTSIIIAHRLTT 540
Cdd:TIGR03797 572 RAMPMGMHTVISEGGGTLSGGQRQrlLIA--RALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLST 647

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 496950271  541 VKKADRIIVLDKGKIVEIGNHEELLQIEnGYYRNLYEVQ 579
Cdd:TIGR03797 648 IRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685

ABC_6TM_Tm288_like

cd18547

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...

26-318

4.11e-68

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 222.66 E-value: 4.11e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPK------DYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDV 99
Cdd:cd18547    1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 100 REKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILY 179
Cdd:cd18547   81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 180 FTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVS 259
Cdd:cd18547  161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 260 ITIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18547  241 LGYVLVAVVGGLLVINGAL-TVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

337-555

9.74e-66

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: 214.26 E-value: 9.74e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 337 KEVKGNIKFEDVRFEYV--AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCS 414
Cdd:cd03248    6 DHLKGIVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAY 494
Cdd:cd03248   86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKI 555
Cdd:cd03248  166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

PRK11174

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed

31-576

5.59e-65

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 223.18 E-value: 5.59e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFSTAQPYLI-----KVAIDNyiTPKdyEGLVRIVYILIALlcaevtmqFLFSYYSNWL--------GQTVIR 97
Cdd:PRK11174  29 LLGFLSGLLLIAQAWLLatilqALIIEN--IPR--EALLPPFILLILL--------FVLRALLAWLrervgfkaGQHIRQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  98 DVREKLFAHLLRFKMRYFDKS---SIGVLVTRAVNDMErigEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATM 174
Cdd:PRK11174  97 QIRQQVLDKLQQLGPAWIQGKpagSWATLVLEQVEDMH---DFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 175 PLILYFTRWFqrSMNAAFVEVRHQVA--NLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQ---AWLKTIWYNSI 249
Cdd:PRK11174 174 PLIPLFMALV--GMGAADANRRNFLAlaRLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQrtmEVLRMAFLSSA 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 250 ---FFpigdlcVSITIALI-VWFG----GRQIIGDnvYDLGnIFLFIQ-----LSQQLFRPIR----HIADKfntlQMGI 312
Cdd:PRK11174 252 vleFF------ASISIALVaVYFGfsylGELNFGH--YGTG-VTLFAGffvliLAPEFYQPLRdlgtFYHAK----AQAV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 313 IASDRVFAILDTETDTETGGEKELKEVKGN-IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNR 391
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQGEKELASNDPVtIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 392 F--YdltSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGY 469
Cdd:PRK11174 399 FlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGL 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 470 HYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIV 549
Cdd:PRK11174 476 DTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWV 555

                        570       580
                 ....*....|....*....|....*..
gi 496950271 550 LDKGKIVEIGNHEELLQiENGYYRNLY 576
Cdd:PRK11174 556 MQDGQIVQQGDYAELSQ-AGGLFATLL 581

ABC_6TM_MsbA_like

cd18552

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...

26-318

6.05e-64

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 211.51 E-value: 6.05e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18552    1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18552   81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18552  161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18552  241 LWYGGYQVISGEL-TPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292

PRK11160

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed

145-573

9.71e-62

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 213.92 E-value: 9.71e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 145 MASDILKMFVITIVMFVIDWKLALISYATM-------PLILYFT-RWFQRSMNAAFVEVRHQvanLNAFVQerisGIKVL 216
Cdd:PRK11160 141 LVAALVVILVLTIGLSFFDLTLALTLGGILlllllllPLLFYRLgKKPGQDLTHLRAQYRVQ---LTEWLQ----GQAEL 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 217 QLFAQEREELENFKKINEK-----HKQAWLkTIWYNSIFFpigdLCVSITIALIVWFGGrQIIGDNVYDLGNIFLFIQLS 291
Cdd:PRK11160 214 TLFGAEDRYRQQLEQTEQQwlaaqRRQANL-TGLSQALMI----LANGLTVVLMLWLAA-GGVGGNAQPGALIALFVFAA 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 292 QQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETDTETGGEKELKEVKGNIKFEDVRFEYVAGEE-ILHGISFEVKEGE 370
Cdd:PRK11160 288 LAAFEALMPVAGAFQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGE 367

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 371 TIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVI 450
Cdd:PRK11160 368 KVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALI 447

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 451 AAAKSIGVHNfLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRT 530
Cdd:PRK11160 448 EVLQQVGLEK-LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKT 526

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 496950271 531 SIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQIENGYYR 573
Cdd:PRK11160 527 VLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569

ABC_6TM_exporter_like

cd18540

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

23-318

3.04e-61

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 204.64 E-value: 3.04e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18540    1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18540   81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITI 262
Cdd:cd18540  161 YFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIAT 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 263 ALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18540  241 ALVLWYGGILVL-AGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295

ABC_6TM_TmrB_like

cd18541

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...

26-318

2.30e-60

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 202.26 E-value: 2.30e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPK-DYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLF 104
Cdd:cd18541    1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 105 AHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFeMASDILKMFVITIV-MFVIDWKLALISYATMPLILYFTRW 183
Cdd:cd18541   81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGIL-YLVDALFLGVLVLVmMFTISPKLTLIALLPLPLLALLVYR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 184 FQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIA 263
Cdd:cd18541  160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 264 LIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18541  240 IVLWYGGRLVI-RGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293

ABC_6TM_exporter_like

cd18778

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

26-318

6.63e-59

Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 198.53 E-value: 6.63e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDN-YITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLF 104
Cdd:cd18778    1 LILTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 105 AHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWF 184
Cdd:cd18778   81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 185 QRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIAL 264
Cdd:cd18778  161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496950271 265 IVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18778  241 VLGFGGRLVLAGEL-TIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293

ABC_6TM_exporter_like

cd18564

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

27-318

6.29e-58

Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 196.19 E-value: 6.29e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  27 IAVALFAVL-SSIFSTAQPYLIKVAIDNYITPKDYEGLVR-----------------IVYILIALLCAEVTmqFLFSYYS 88
Cdd:cd18564    1 LALALLALLlETALRLLEPWPLKVVIDDVLGDKPLPGLLGlapllgpdplallllaaAALVGIALLRGLAS--YAGTYLT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  89 NWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLAL 168
Cdd:cd18564   79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 169 ISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNS 248
Cdd:cd18564  159 IALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQA 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 249 IFFPIGDLCVSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18564  239 LLSPVVDVLVAVGTALVLWFGAWLVL-AGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307

ABC_6TM_exporter_like

cd18563

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

26-318

9.20e-57

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 192.72 E-value: 9.20e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPK----DYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVRE 101
Cdd:cd18563    1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLgpggNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 102 KLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFT 181
Cdd:cd18563   81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 182 RWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSIT 261
Cdd:cd18563  161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 262 IALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18563  241 TLIVWYFGGRQVLSGTM-TLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296

ABC_6TM_YwjA_like

cd18549

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...

23-312

6.35e-56

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 190.35 E-value: 6.35e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18549    1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18549   81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITI 262
Cdd:cd18549  161 YFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLN 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 496950271 263 ALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGI 312
Cdd:cd18549  241 LVVLVAGGYFIIKGEI-TLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGM 289

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

341-559

5.39e-54

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: 182.61 E-value: 5.39e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 341 GNIKFEDVRFEYVAG-EEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHI 419
Cdd:cd03369    5 GEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFADSIYNNITLKNpAITEEEVIAAAKsigvhnflmslpegyhynVKERGAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:cd03369   85 TIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 500 ILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIG 559
Cdd:cd03369  146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

30-318

9.72e-53

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.

Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 181.91 E-value: 9.72e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  30 ALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLLR 109
Cdd:cd18576    2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 110 FKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSMN 189
Cdd:cd18576   82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 190 AAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALIVWFG 269
Cdd:cd18576  162 KLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 496950271 270 GRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18576  242 GRLVLAGEL-TAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

13-538

9.79e-53

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: 188.72 E-value: 9.79e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   13 RQLSRFVKPYRGVFIAVALFAVLSSIFSTA----QPYLIKVAidnYITPKdyeglvrivyiLIALLCAEVTMQFL----- 83
Cdd:TIGR02868   2 LRILPLLKPRRRRLALAVLLGALALGSAVAllgvSAWLISRA---AEMPP-----------VLYLSVAAVAVRAFgigra 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   84 -FSYYSNWLGQ-TVIR---DVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIV 158
Cdd:TIGR02868  68 vFRYLERLVGHdAALRslgALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  159 MFVIDWKLALISYATMPLILYFTRW-FQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHK 237
Cdd:TIGR02868 148 IAVLSVPAALILAAGLLLAGFVAPLvSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELT 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  238 QAWLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIiGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDR 317
Cdd:TIGR02868 228 RAERRAAAATALGAALTLLAAGLAVLGALWAGGPAV-ADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAER 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  318 VFAILDTETDTETG---GEKELKEVKGNIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYD 394
Cdd:TIGR02868 307 IVEVLDAAGPVAEGsapAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  395 LTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVK 474
Cdd:TIGR02868 387 PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLG 466

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271  475 ERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRL 538
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

335-566

5.33e-50

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];

Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 181.48 E-value: 5.33e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 335 ELKEVKGNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLC 413
Cdd:COG4618  323 PLPRPKGRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 414 SLREHIATVLQDVFLFADSIYNNITlKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRA 493
Cdd:COG4618  403 ELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARA 481

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 494 YVHKPQILILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG4618  482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555

ABC_membrane

pfam00664

ABC transporter transmembrane region; This family represents a unit of six transmembrane ...

26-298

1.89e-49

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: 172.44 E-value: 1.89e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYE--GLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKL 103
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  104 FAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRW 183
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  184 FQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIA 263
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 496950271  264 LIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPI 298
Cdd:pfam00664 241 LALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

97-572

2.79e-48

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: 181.68 E-value: 2.79e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    97 RDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEifssglfeMASDILKMF-------VITIVMFVIDWKLALI 169
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDS--------MIPPVIKMFmgslfnvIGALIVILLATPIAAV 1109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   170 SYATMPLILYFTRWFqrsmnaaFVEVRHQVANLNAFVQ--------ERISGIKVLQLF-AQEREELENFKKINEKHKqAW 240
Cdd:TIGR00957 1110 IIPPLGLLYFFVQRF-------YVASSRQLKRLESVSRspvyshfnETLLGVSVIRAFeEQERFIHQSDLKVDENQK-AY 1181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   241 LKTIWYNSiFFPIGDLCVSITIALIVWFGGrqIIGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFA 320
Cdd:TIGR00957 1182 YPSIVANR-WLAVRLECVGNCIVLFAALFA--VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE 1258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   321 ILDTETDT----ETGGEKELKEVKGNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL 395
Cdd:TIGR00957 1259 YSETEKEApwqiQETAPPSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES 1338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   396 TSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNItlkNP--AITEEEVIAAAKSIGVHNFLMSLPEGYHYNV 473
Cdd:TIGR00957 1339 AEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHEC 1415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   474 KERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKG 553
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1495

                          490
                   ....*....|....*....
gi 496950271   554 KIVEIGNHEELLQIENGYY 572
Cdd:TIGR00957 1496 EVAEFGAPSNLLQQRGIFY 1514

PTZ00265

multidrug resistance protein (mdr1); Provisional

66-573

5.42e-48

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.00 E-value: 5.42e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   66 IVYILIALLCAEVtmqfLFSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFD--KSSIGVLVTRAVNDMErigeIFSSGLF 143
Cdd:PTZ00265  872 ILVIAIAMFISET----LKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH----LLKTGLV 943

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  144 EMASDILKMFVITIVMFVIDWKLALISYATMPLILY-FTRWFQ-RSMNAAFVEVRHQVANLNA----------------- 204
Cdd:PTZ00265  944 NNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFiFMRVFAiRARLTANKDVEKKEINQPGtvfaynsddeifkdpsf 1023

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  205 FVQERISGIKVLQLFAqereeLENF------KKINEKHKQAWLKTIwYNSIFFPIGDLCVSITIALIVWFGGRQII-GDN 277
Cdd:PTZ00265 1024 LIQEAFYNMNTVIIYG-----LEDYfcnlieKAIDYSNKGQKRKTL-VNSMLWGFSQSAQLFINSFAYWFGSFLIRrGTI 1097

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  278 VYD--LGNIFLFIQLSQQLFRPIRHIADKFNTLqmgiIASDRVFAIL--DTETDTETGGEKELK---EVKGNIKFEDVRF 350
Cdd:PTZ00265 1098 LVDdfMKSLFTFLFTGSYAGKLMSLKGDSENAK----LSFEKYYPLIirKSNIDVRDNGGIRIKnknDIKGKIEIMDVNF 1173

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  351 EYVAGEE--ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL--------------------------------- 395
Cdd:PTZ00265 1174 RYISRPNvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmk 1253

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  396 ---------------------TSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAK 454
Cdd:PTZ00265 1254 nvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACK 1333

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  455 SIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSI 532
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTII 1413

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 496950271  533 IIAHRLTTVKKADRIIVLDK----GKIVEI-GNHEELLQIENGYYR 573
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVYK 1459

ABC_6TM_Rv0194_D1_like

cd18543

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...

26-318

8.83e-48

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: 168.43 E-value: 8.83e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18543    1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFeMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18543   81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18543  160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18543  240 LALGGWLVANGSL-TLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

343-565

9.69e-47

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: 163.66 E-value: 9.69e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:COG1122    1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQ--DVFLFADSIYNNIT--LKNPAITEEE----VIAAAKSIGVHNFLmslpegyHYNVKErgamLSAGQRQLIAFLRAY 494
Cdd:COG1122   81 FQnpDDQLFAPTVEEDVAfgPENLGLPREEirerVEEALELVGLEHLA-------DRPPHE----LSGGQKQRVAIAGVL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIA-HRLTTV-KKADRIIVLDKGKIVEIGNHEELL 565
Cdd:COG1122  150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVF 222

ABC_6TM_exporter_like

cd18550

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

26-298

5.73e-46

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 163.81 E-value: 5.73e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18550    1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18550   81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQER--ISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIA 263
Cdd:cd18550  161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 496950271 264 LIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPI 298
Cdd:cd18550  241 LVYWVGGLLVIGGGL-TIGTLVAFTALLGRLYGPL 274

ABC_6TM_LmrA_like

cd18551

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...

26-318

1.58e-43

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: 157.21 E-value: 1.58e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPkdyEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18551    1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQ 185
Cdd:cd18551   78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18551  158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 266 VWFGGRQiIGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18551  238 LGVGGAR-VASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289

PTZ00265

multidrug resistance protein (mdr1); Provisional

201-550

2.27e-43

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.13 E-value: 2.27e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  201 NLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIIGD---- 276
Cdd:PTZ00265  234 NTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDlsnq 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  277 ---NVYDLGN---IFLFIQLSQQLFRPI-RHIADKFNTLQmgiiASDRVFAILDTETDTETGGE-KELKEVKgNIKFEDV 348
Cdd:PTZ00265  314 qpnNDFHGGSvisILLGVLISMFMLTIIlPNITEYMKSLE----ATNSLYEIINRKPLVENNDDgKKLKDIK-KIQFKNV 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  349 RFEYVAGE--EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYI-DGVNIEEYTLCSLREHIATVLQD 425
Cdd:PTZ00265  389 RFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQD 468

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  426 VFLFADSIYNNI-----TLKN----------------------------------------------------PAITEEE 448
Cdd:PTZ00265  469 PLLFSNSIKNNIkyslySLKDlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQTIKDSE 548

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  449 VIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATD--KMT 526
Cdd:PTZ00265  549 VVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGN 628

                         410       420
                  ....*....|....*....|....
gi 496950271  527 EGRTSIIIAHRLTTVKKADRIIVL 550
Cdd:PTZ00265  629 ENRITIIIAHRLSTIRYANTIFVL 652

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

343-555

8.58e-43

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: 151.21 E-value: 8.58e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIAT 421
Cdd:cd03246    1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFADSIYNNItlknpaiteeeviaaaksigvhnflmslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQIL 501
Cdd:cd03246   81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 502 ILDEATSSVDSHSEKLIQEATDKMTE-GRTSIIIAHRLTTVKKADRIIVLDKGKI 555
Cdd:cd03246  119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173

ABC_6TM_TAP_ABCB8_10_like

cd18557

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...

31-318

1.33e-42

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: 154.64 E-value: 1.33e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLLRF 110
Cdd:cd18557    3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 111 KMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSMNA 190
Cdd:cd18557   83 EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 191 AFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALIVWFGG 270
Cdd:cd18557  163 LSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 496950271 271 RQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18557  243 YLVLSGQL-TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

19-566

4.52e-42

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: 159.05 E-value: 4.52e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   19 VKPYRGVFIAVALFAVLSSIFSTAQP-YLIKVaIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIR 97
Cdd:TIGR01842   1 LAKVKRTFIIVGLFSFVINILMLAPPlYMLQV-YDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   98 DVREKLFAHLLRFKMRYFDKSSigvlvTRAVNDMERIGEIFSS-GLFEMAsDILKMFVITIVMFVIDWKLALISYATMpL 176
Cdd:TIGR01842  80 ALNQPIFAASFSATLRRGSGDG-----LQALRDLDQLRQFLTGpGLFAFF-DAPWMPIYLLVCFLLHPWIGILALGGA-V 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  177 ILYFTRWF-QRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIffpIGD 255
Cdd:TIGR01842 153 VLVGLALLnNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGM---LSN 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  256 LCVSITIAL--IVWFGGRQIIGDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRVFAILDTETDTETggE 333
Cdd:TIGR01842 230 LSKYFRIVLqsLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDP--A 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  334 KELKEVKGNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTL 412
Cdd:TIGR01842 308 MPLPEPEGHLSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  413 CSLREHIATVLQDVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLR 492
Cdd:TIGR01842 388 ETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALAR 467

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271  493 AYVHKPQILILDEATSSVDSHSEKLIQEA-TDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAiKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

344-554

2.69e-41

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: 148.38 E-value: 2.69e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 344 KFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:cd03225    1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQ--DVFLFADSIYNNI--TLKNPAITEEE----VIAAAKSIGVHNFLmslpegyHYNVKErgamLSAGQRQLIAFLRAY 494
Cdd:cd03225   81 FQnpDDQFFGPTVEEEVafGLENLGLPEEEieerVEEALELVGLEGLR-------DRSPFT----LSGGQKQRVAIAGVL 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIIAHRLTTVKK-ADRIIVLDKGK 554
Cdd:cd03225  150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211

PLN03232

ABC transporter C family member; Provisional

15-565

6.50e-41

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 159.76 E-value: 6.50e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   15 LSRFVKPYRGVFIAVALFA--VLSSIFSTAQPYLIKVAIDNYiTPKDYE-GLVRIVYILIALlcAEVTMQFLFSYysnWL 91
Cdd:PLN03232  901 LMRYNKAVGGLWVVMILLVcyLTTEVLRVSSSTWLSIWTDQS-TPKSYSpGFYIVVYALLGF--GQVAVTFTNSF---WL 974

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   92 GQTVI---RDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDmerIGEIfSSGLFEMASDILKMFVITIVMFVIDWKLAL 168
Cdd:PLN03232  975 ISSSLhaaKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKD---IGDI-DRNVANLMNMFMNQLWQLLSTFALIGTVST 1050

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  169 IS-YATMPLILYFTRWFQRSMNAAfVEVRhqvanlnafvqeRISGIKVLQLFAQEREELENFKKINEKHKQAWLKTI--- 244
Cdd:PLN03232 1051 ISlWAIMPLLILFYAAYLYYQSTS-REVR------------RLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKIngk 1117

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  245 -----------------WYNSIFFPIGDLCVSITIALIVWFGGRQiigDNVYDLGNIFLFI-----QLSQQLFRPIRHIA 302
Cdd:PLN03232 1118 smdnnirftlantssnrWLTIRLETLGGVMIWLTATFAVLRNGNA---ENQAGFASTMGLLlsytlNITTLLSGVLRQAS 1194

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  303 DKFNTLQmgiiASDRVFAILDTETDTeTGGEKELKEV-----KGNIKFEDVRFEYVAG-EEILHGISFEVKEGETIAIVG 376
Cdd:PLN03232 1195 KAENSLN----SVERVGNYIDLPSEA-TAIIENNRPVsgwpsRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVG 1269

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  377 ATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNI---TLKNPAiteeEVIAAA 453
Cdd:PLN03232 1270 RTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdpfSEHNDA----DLWEAL 1345

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  454 KSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSII 533
Cdd:PLN03232 1346 ERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLV 1425

                         570       580       590
                  ....*....|....*....|....*....|..
gi 496950271  534 IAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:PLN03232 1426 IAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

343-559

8.00e-41

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: 145.92 E-value: 8.00e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTlCSLREHIAT 421
Cdd:cd03247    1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFADSIYNNItlknpaiteeeviaaaksigvhnflmslpegyhynvkerGAMLSAGQRQLIAFLRAYVHKPQIL 501
Cdd:cd03247   80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 502 ILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIG 559
Cdd:cd03247  121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

ABC_6TM_exporter_like

cd18565

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

26-318

1.61e-40

Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 149.64 E-value: 1.61e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEG---------------LVRIVYILIALLCAEVTMQFLFSYYSNW 90
Cdd:cd18565    1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLplvpaslgpadprgqLWLLGGLTVAAFLLESLFQYLSGVLWRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  91 LGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGlfemASDILKMFV----ITIVMFVIDWKL 166
Cdd:cd18565   81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDG----ANSIIRVVVtvlgIGAILFYLNWQL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 167 ALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWY 246
Cdd:cd18565  157 ALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRL 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 247 NSIFFPIGDLCVSITIALIVWFGGRQIIGDNVYDLGNI-------FLFiqLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18565  237 RAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLtvgtlvtFLF--YTQRLLWPLTRLGDLIDQYQRAMASAKRV 313

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

343-564

6.88e-40

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).

Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 145.02 E-value: 6.88e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL-----TSGAIYIDGVNI--EEYTLCSL 415
Cdd:cd03260    1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 416 REHIATVLQDVFLFADSIYNNITL-------KNPAITEEEVIAAAKSIGvhnflmsLPEgyhyNVKER--GAMLSAGQRQ 486
Cdd:cd03260   80 RRRVGMVFQKPNPFPGSIYDNVAYglrlhgiKLKEELDERVEEALRKAA-------LWD----EVKDRlhALGLSGGQQQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 487 LIAFLRAYVHKPQILILDEATSSVDSHS----EKLIQEATDKMtegrTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNH 561
Cdd:cd03260  149 RLCLARALANEPEVLLLDEPTSALDPIStakiEELIAELKKEY----TIVIVTHNMQQAARvADRTAFLLNGRLVEFGPT 224


                 ...
gi 496950271 562 EEL 564
Cdd:cd03260  225 EQI 227

ABC_6TM_Tm287_like

cd18548

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...

26-295

3.93e-39

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 145.23 E-value: 3.93e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18548    1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILkMFVITIVM-FVIDWKLALISYATMPLILYFTRWF 184
Cdd:cd18548   81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI-MLIGAIIMaFRINPKLALILLVAIPILALVVFLI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 185 QRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIAL 264
Cdd:cd18548  160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVA 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 496950271 265 IVWFGGRQIIGDNVyDLGNIFLFIQ-LSQQLF 295
Cdd:cd18548  240 ILWFGGHLINAGSL-QVGDLVAFINyLMQILM 270

PLN03130

ABC transporter C family member; Provisional

341-570

8.35e-39

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 153.36 E-value: 8.35e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  341 GNIKFEDVRFEYVAG-EEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHI 419
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  420 ATVLQDVFLFADSIYNNITLKNPAiTEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271  500 ILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQIENG 570
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

343-566

1.45e-38

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: 148.90 E-value: 1.45e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGE----EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLRE- 417
Cdd:COG1123  261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 418 --HIATVLQDVF--LFA-DSIYNNIT-------LKNPAITEEEVIAAAKSIGvhnflmsLPEGYhynvKER-GAMLSAGQ 484
Cdd:COG1123  341 rrRVQMVFQDPYssLNPrMTVGDIIAeplrlhgLLSRAERRERVAELLERVG-------LPPDL----ADRyPHELSGGQ 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 485 RQLIAFLRAYVHKPQILILDEATSSVDSHSE----KLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:COG1123  410 RQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRDLQREL--GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487


                 ....*..
gi 496950271 560 NHEELLQ 566
Cdd:COG1123  488 PTEEVFA 494

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

341-575

8.96e-38

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: 140.43 E-value: 8.96e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 341 GNIKFED--VRFEYVAgEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREH 418
Cdd:cd03288   18 GEIKIHDlcVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQDVFLFADSIYNNITLKNPAiTEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKP 498
Cdd:cd03288   97 LSIILQDPILFSGSIRFNLDPECKC-TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 499 QILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQIENGYYRNL 575
Cdd:cd03288  176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

343-559

7.76e-36

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: 134.17 E-value: 7.76e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGE---EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT---LCSLR 416
Cdd:cd03257    2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQDVF-----------LFADSIYNNITLKNPAITEEEVIAAAKSIGvhnflmsLPEGYhynVKERGAMLSAGQR 485
Cdd:cd03257   82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLLVGVG-------LPEEV---LNRYPHELSGGQR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 486 QLIAFLRAYVHKPQILILDEATSSVDSHSE----KLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03257  152 QRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLKKLQEEL--GLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

343-565

9.11e-35

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 131.65 E-value: 9.11e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:cd03295    1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNITLKnPAI---TEEEVIAAAKSigvhnfLMSL----PEGYhynvKER-GAMLSAGQRQLIAFLRA 493
Cdd:cd03295   81 IQQIGLFPHmTVEENIALV-PKLlkwPKEKIRERADE------LLALvgldPAEF----ADRyPHELSGGQQQRVGVARA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 494 YVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRL-TTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:cd03295  150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

344-554

2.25e-34

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: 127.75 E-value: 2.25e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 344 KFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVL 423
Cdd:cd00267    1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 424 QdvflfadsiynnitlknpaiteeeviaaaksigvhnflmslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:cd00267   80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 504 DEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKKA-DRIIVLDKGK 554
Cdd:cd00267  105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157

PTZ00243

ABC transporter; Provisional

341-577

9.24e-34

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 137.60 E-value: 9.24e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  341 GNIKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHI 419
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  420 ATVLQDVFLFADSIYNNItlkNPAI--TEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHK 497
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNV---DPFLeaSSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  498 PQILIL-DEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQIENGYYRNLY 576
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543


                  .
gi 496950271  577 E 577
Cdd:PTZ00243 1544 E 1544

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

343-566

2.02e-33

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.88 E-value: 2.02e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGE-EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLT---SGAIYIDGVNIEEYTLCSLREH 418
Cdd:COG1123    5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQDVF--LFADSIYNNI--TLKNPAITEEE----VIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAF 490
Cdd:COG1123   85 IGMVFQDPMtqLNPVTVGDQIaeALENLGLSRAEararVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 491 LRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTV-KKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG1123  154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232

NatA

COG4555

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...

343-566

2.18e-33

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: 127.67 E-value: 2.18e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLcSLREHIATV 422
Cdd:COG4555    2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNITLKNPA--ITEEEVIAAAKSIgVHNFLMSlpEGYHYNVKErgamLSAGQRQLIAFLRAYVHKPQ 499
Cdd:COG4555   80 PDERGLYDRlTVRENIRYFAELygLFDEELKKRIEEL-IELLGLE--EFLDRRVGE----LSTGMKKKVALARALVHDPK 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 500 ILILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG4555  153 VLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

355-577

2.89e-33

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];

Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 127.61 E-value: 2.89e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFL------ 428
Cdd:COG1124   17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhprh 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 429 -FADSIYNNITLKNPAITEEEVIAAAKSIGvhnflmsLPEGYHYNvkeRGAMLSAGQRQLIAFLRAYVHKPQILILDEAT 507
Cdd:COG1124   97 tVDRILAEPLRIHGLPDREERIAELLEQVG-------LPPSFLDR---YPHQLSGGQRQRVAIARALILEPELLLLDEPT 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 508 SSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ-IENGYYRNLYE 577
Cdd:COG1124  167 SALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAgPKHPYTRELLA 240

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

343-555

3.46e-33

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: 126.45 E-value: 3.46e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE---ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT---LCSLR 416
Cdd:cd03255    1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 -EHIATVLQDVFLFAD-SIYNNITL------KNPAITEEEVIAAAKSIGvhnflmsLPEGYHYNVKErgamLSAGQRQLI 488
Cdd:cd03255   81 rRHIGFVFQSFNLLPDlTALENVELplllagVPKKERRERAEELLERVG-------LGDRLNHYPSE----LSGGQQQRV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 489 AFLRAYVHKPQILILDEATSSVDSHSEK----LIQEATDKMteGRTSIIIAHRLTTVKKADRIIVLDKGKI 555
Cdd:cd03255  150 AIARALANDPKIILADEPTGNLDSETGKevmeLLRELNKEA--GTTIVVVTHDPELAEYADRIIELRDGKI 218

ABC_6TM_PCAT1_LagD_like

cd18570

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...

23-318

5.12e-33

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.

Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 127.95 E-value: 5.12e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18570    1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18570   81 YFKHLLKLPLSFFETRKTGEIISR-FNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITI 262
Cdd:cd18570  160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 263 ALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18570  240 LLILWIGSYLVI-KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

359-508

5.31e-33

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 123.53 E-value: 5.31e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFAD-SIYNNI 437
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271  438 TLknpAITEEEVIAAAKSIGVHNFL--MSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATS 508
Cdd:pfam00005  81 RL---GLLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

FtsE

COG2884

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];

343-557

2.16e-32

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.39 E-value: 2.16e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVN---IEEYTLCSLREHI 419
Cdd:COG2884    2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFAD-SIYNNITL------KNPAITEEEVIAAAKSIGVHNFLMSLPEgyhynvkergaMLSAGQRQLIAFLR 492
Cdd:COG2884   82 GVVFQDFRLLPDrTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIAR 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 493 AYVHKPQILILDEATSSVD-SHSEKLIqEATDKMTEGRTSIIIA-HRLTTVKKAD-RIIVLDKGKIVE 557
Cdd:COG2884  151 ALVNRPELLLADEPTGNLDpETSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVR 217

CcmA

COG1131

ABC-type multidrug transport system, ATPase component [Defense mechanisms];

343-584

2.18e-32

ABC-type multidrug transport system, ATPase component [Defense mechanisms];

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.79 E-value: 2.18e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLcSLREHIATV 422
Cdd:COG1131    1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNITL------KNPAITEEEVIAAAKSIGVHNFLmslpegyhynvKERGAMLSAGQRQLIAFLRAYV 495
Cdd:COG1131   79 PQEPALYPDlTVRENLRFfarlygLPRKEARERIDELLELFGLTDAA-----------DRKVGTLSGGMKQRLGLALALL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIA-HRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQiengyyr 573
Cdd:COG1131  148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA------- 220

                        250
                 ....*....|.
gi 496950271 574 nlyevQFLEEV 584
Cdd:COG1131  221 -----RLLEDV 226

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

343-555

4.95e-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: 118.65 E-value: 4.95e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLcSLREHIATV 422
Cdd:cd03230    1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLfadsiYNNITlknpaiteeeviaaaksigVHNFLMslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:cd03230   79 PEEPSL-----YENLT-------------------VRENLK----------------LSGGMKQRLALAQALLHDPELLI 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGKI 555
Cdd:cd03230  119 LDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

15-566

7.05e-31

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: 126.84 E-value: 7.05e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  15 LSRFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIdNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSyysnWLGQT 94
Cdd:COG4615    4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALINQAL-NATGAALARLLLLFAGLLVLLLLSRLASQLLLT----RLGQH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  95 VIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIgeifsSGLFEMASDILKMFVITIV----MFVIDWKLALIS 170
Cdd:COG4615   79 AVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-----SQAFVRLPELLQSVALVLGclayLAWLSPPLFLLT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 171 YATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREEL---------ENFKKINEK-HKQAW 240
Cdd:COG4615  154 LVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFfdedlqptaERYRDLRIRaDTIFA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 241 LKTIWYNSIFFpigdlcvsITIALIVwFGGRQIIGDNVYDLGNI---FLFiqlsqqLFRPIRHIADKFNTLQMGIIASDR 317
Cdd:COG4615  234 LANNWGNLLFF--------ALIGLIL-FLLPALGWADPAVLSGFvlvLLF------LRGPLSQLVGALPTLSRANVALRK 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 318 VfAILDTETDTETGGEKELKEVKGN-----IKFEDVRFEYVAGEE----ILHGISFEVKEGETIAIVGATGAGKTTITNL 388
Cdd:COG4615  299 I-EELELALAAAEPAAADAAAPPAPadfqtLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKL 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 389 LNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFaDSIYNnitLKNPAITEEeviaaaksigVHNFL--MSLp 466
Cdd:COG4615  378 LTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-DRLLG---LDGEADPAR----------ARELLerLEL- 442

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 467 egyHYNVKERGAM-----LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSH-----SEKLIQEATDKmteGRTSIIIAH 536
Cdd:COG4615  443 ---DHKVSVEDGRfsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELLPELKAR---GKTVIAISH 516

                        570       580       590
                 ....*....|....*....|....*....|..
gi 496950271 537 --RLTTVkkADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG4615  517 ddRYFDL--ADRVLKMDYGKLVELTGPAALAA 546

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

343-574

7.43e-31

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: 120.30 E-value: 7.43e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT---LCSLREHI 419
Cdd:cd03261    1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFAD-SIYNNITL---KNPAITEEEV--IAAAK--SIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFL 491
Cdd:cd03261   80 GMLFQSGALFDSlTVFENVAFplrEHTRLSEEEIreIVLEKleAVGLRGAEDLYP-----------AELSGGMKKRVALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 492 RAYVHKPQILILDEATSSVDSHSEKLIQE--ATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQIE 568
Cdd:cd03261  149 RALALDPELLLYDEPTAGLDPIASGVIDDliRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228


                 ....*.
gi 496950271 569 NGYYRN 574
Cdd:cd03261  229 DPLVRQ 234

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

343-559

8.67e-31

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: 119.55 E-value: 8.67e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeyTLCSLREHIATV 422
Cdd:cd03259    1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNIT--LKNPAITEEE----VIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYV 495
Cdd:cd03259   78 FQDYALFPHlTVAENIAfgLKLRGVPKAEirarVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALA 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIG 559
Cdd:cd03259  147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213

ABC_6TM_bac_exporter_ABCB8_10_like

cd18575

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

30-274

1.35e-30

Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 121.05 E-value: 1.35e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  30 ALFAVLSSIFST-AQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLL 108
Cdd:cd18575    1 ALIALLIAAAATlALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 109 RFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLfemaSDILKMFVI----TIVMFVIDWKLALISYATMPLILYFTRWF 184
Cdd:cd18575   81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSL----SIALRNLLLliggLVMLFITSPKLTLLVLLVIPLVVLPIILF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 185 QRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIAL 264
Cdd:cd18575  157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236

                        250
                 ....*....|
gi 496950271 265 IVWFGGRQII 274
Cdd:cd18575  237 VLWLGAHDVL 246

ABC_6TM_TAP

cd18572

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...

31-318

1.46e-30

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.

Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 121.11 E-value: 1.46e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLLRF 110
Cdd:cd18572    3 VFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 111 KMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSMNA 190
Cdd:cd18572   83 DIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 191 AFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFK-------KINEKHKQAWLKTIWYNSIFFpigdlcvSITIA 263
Cdd:cd18572  163 LSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYEraldkalKLSVRQALAYAGYVAVNTLLQ-------NGTQV 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 264 LIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18572  236 LVLFYGGHLVLSGRM-SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

343-566

1.52e-30

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 1.52e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYV-AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHI-- 419
Cdd:PRK13635   6 IRVEHISFRYPdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVgm 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 -----------ATVLQDVfLFAdsiynnitLKNPAITEEEVI----AAAKSIGVHNFLMSLPegyhynvkergAMLSAGQ 484
Cdd:PRK13635  86 vfqnpdnqfvgATVQDDV-AFG--------LENIGVPREEMVervdQALRQVGMEDFLNREP-----------HRLSGGQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 485 RQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHE 562
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225


                 ....
gi 496950271 563 ELLQ 566
Cdd:PRK13635 226 EIFK 229

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

343-558

3.87e-30

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: 117.96 E-value: 3.87e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGE---EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytlcsLREHI 419
Cdd:cd03293    1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFA-DSIYNNITL------KNPAITEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLR 492
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALglelqgVPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 493 AYVHKPQILILDEATSSVDSHSEKLIQEATDKM--TEGRTSIIIAHRLT-TVKKADRIIVLDK--GKIVEI 558
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

343-569

4.15e-30

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: 118.61 E-value: 4.15e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:COG1120    2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQD---VFLF--ADSI------YNNItLKNPAITEEEVIAAA-KSIGVHNFlmslpegyhynvKERG-AMLSAGQRQLIA 489
Cdd:COG1120   81 PQEppaPFGLtvRELValgrypHLGL-FGRPSAEDREAVEEAlERTGLEHL------------ADRPvDELSGGERQRVL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 490 FLRAYVHKPQILILDEATSSVD-SHSE---KLIQEATDKmtEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:COG1120  148 IARALAQEPPLLLLDEPTSHLDlAHQLevlELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEV 225


                 ....*
gi 496950271 565 LQIEN 569
Cdd:COG1120  226 LTPEL 230

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

343-554

5.14e-30

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: 116.80 E-value: 5.14e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE----ILHGISFEVKEGETIAIVGATGAGKTTITN-LLNRFyDLTSGAIYIDGvnieeytlcslre 417
Cdd:cd03250    1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 418 HIATVLQDVFLFADSIYNNITLKNPAITE--EEVIAAAksiGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYV 495
Cdd:cd03250   67 SIAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 496 HKPQILILDEATSSVDSH-SEKLIQEA-TDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGK 554
Cdd:cd03250  144 SDADIYLLDDPLSAVDAHvGRHIFENCiLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

346-559

1.06e-29

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.

Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 115.23 E-value: 1.06e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 346 EDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQd 425
Cdd:cd03214    3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 vflfadsiynnitlknpaiteeeviaAAKSIGVHNFlmslpegyhynvKERGAM-LSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:cd03214   81 --------------------------ALELLGLAHL------------ADRPFNeLSGGERQRVLLARALAQEPPILLLD 122

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 505 EATSSVDSHSE----KLIQEATDKmtEGRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIG 559
Cdd:cd03214  123 EPTSHLDIAHQiellELLRRLARE--RGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

343-555

1.67e-29

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.

Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 115.70 E-value: 1.67e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI--EEYTLCSLREHIA 420
Cdd:cd03262    1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQDVFLFAD-SIYNNITL---KNPAITEEEVIAAA----KSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLR 492
Cdd:cd03262   80 MVFQQFNLFPHlTVLENITLapiKVKGMSKAEAEERAlellEKVGLADKADAYP-----------AQLSGGQQQRVAIAR 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 493 AYVHKPQILILDEATSSVDShseKLIQEATDKMT----EGRTSIIIAHRLTTVKK-ADRIIVLDKGKI 555
Cdd:cd03262  149 ALAMNPKVMLFDEPTSALDP---ELVGEVLDVMKdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

343-556

2.08e-29

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: 116.51 E-value: 2.08e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT---LCSLREHI 419
Cdd:cd03256    1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDvflfadsiYNNI----TLKNpaiteeeVIAAAksIGVHNFLMSLPEGYHYNVKE-----------------RGA 478
Cdd:cd03256   81 GMIFQQ--------FNLIerlsVLEN-------VLSGR--LGRRSTWRSLFGLFPKEEKQralaalervglldkayqRAD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 479 MLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQE--ATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKI 555
Cdd:cd03256  144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDllKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223


                 .
gi 496950271 556 V 556
Cdd:cd03256  224 V 224

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

343-554

2.36e-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: 114.21 E-value: 2.36e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCS--LREHIA 420
Cdd:cd03229    1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQDVFLFAD-SIYNNITLKnpaiteeeviaaaksigvhnflmslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQ 499
Cdd:cd03229   80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 500 ILILDEATSSVDSHS----EKLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGK 554
Cdd:cd03229  121 VLLLDEPTSALDPITrrevRALLKSLQAQL--GITVVLVTHDLDEAARlADRVVVLRDGK 178

ThiQ

COG3840

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];

342-569

4.70e-29

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.24 E-value: 4.70e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 342 NIKFEDVRFEYvaGEEILHgISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEyTLCSLREhIAT 421
Cdd:COG3840    1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFAD-SIYNNITLK-NPA--ITEEE---VIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAY 494
Cdd:COG3840   76 LFQENNLFPHlTVAQNIGLGlRPGlkLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 495 VHKPQILILDEATSSVDS--HSE--KLIQEATDKmtEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQIEN 569
Cdd:COG3840  145 VRKRPILLLDEPFSALDPalRQEmlDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

344-555

1.03e-28

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: 113.78 E-value: 1.03e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 344 KFEDVRFEYVaGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytlcsLREHIATVL 423
Cdd:cd03235    1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 424 Q-------------DVFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLmslpegyHYNVKErgamLSAGQRQLIAF 490
Cdd:cd03235   75 QrrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVLL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 491 LRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTV-KKADRIIVLDKGKI 555
Cdd:cd03235  144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

343-565

3.26e-28

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 3.26e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIAT 421
Cdd:PRK13632   8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDvflfADSIYNNIT--------LKNPAITEEE----VIAAAKSIGVHNFLMSLPEGyhynvkergamLSAGQRQLIA 489
Cdd:PRK13632  88 IFQN----PDNQFIGATveddiafgLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGR--TSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230

ABC_6TM_Pgp_ABCB1_D2_like

cd18578

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...

17-327

4.74e-28

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.

Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 114.47 E-value: 4.74e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  17 RFVKPYRGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRI-----VYILIALLCAeVTMqFLFSYYSNWL 91
Cdd:cd18578    2 KLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEAnfwalMFLVLAIVAG-IAY-FLQGYLFGIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  92 GQTVIRDVREKLFAHLLRFKMRYFDKS--SIGVLVTRAVNDMERIGEIFSSGLFEMASDILkMFVITIVM-FVIDWKLAL 168
Cdd:cd18578   80 GERLTRRLRKLAFRAILRQDIAWFDDPenSTGALTSRLSTDASDVRGLVGDRLGLILQAIV-TLVAGLIIaFVYGWKLAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 169 ISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNS 248
Cdd:cd18578  159 VGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 249 IFFPIGDLCVSITIALIVWFGGRQIIgDNVYDLGNIF----LFIQLSQQLFRPIRHIADkfntLQMGIIASDRVFAILDT 324
Cdd:cd18578  239 LGFGLSQSLTFFAYALAFWYGGRLVA-NGEYTFEQFFivfmALIFGAQSAGQAFSFAPD----IAKAKAAAARIFRLLDR 313


                 ...
gi 496950271 325 ETD 327
Cdd:cd18578  314 KPE 316

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

2-575

4.97e-28

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 120.05 E-value: 4.97e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271     2 SEKTSRTKHTFRQLSRFVKPYrgvFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPK--DYEGLVrivYILIALLCAEVT 79
Cdd:TIGR00957  298 SPHKPRKPSLFKVLYKTFGPY---FLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMapDWQGYF---YTGLLFVCACLQ 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    80 MQFLFSYYsnwlgqtvirdvrEKLFAHLLRFKMryfdkSSIGV------LVTRAVNDMERIGEIFSSglfeMASDILK-M 152
Cdd:TIGR00957  372 TLILHQYF-------------HICFVSGMRIKT-----AVMGAvyrkalVITNSARKSSTVGEIVNL----MSVDAQRfM 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   153 FVITIVMFVIDWKLALIsyatmpLILYFTrWFQRS---------------MNAAF-VEVR-HQVANLNA------FVQER 209
Cdd:TIGR00957  430 DLATYINMIWSAPLQVI------LALYFL-WLNLGpsvlagvavmvlmvpLNAVMaMKTKtYQVAHMKSkdnrikLMNEI 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   210 ISGIKVLQLFAQEREELENFKKINEKHKQAwLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIIGDNVYDLGNIFLFIQ 289
Cdd:TIGR00957  503 LNGIKVLKLYAWELAFLDKVEGIRQEELKV-LKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLA 581

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   290 LSQQLFRPIRHIADKFNTLQMGIIASDRVFAILD-TETDTETGGEKELKEVKGN-IKFEDVRFEYVAGEE-ILHGISFEV 366
Cdd:TIGR00957  582 LFNILRFPLNILPMVISSIVQASVSLKRLRIFLShEELEPDSIERRTIKPGEGNsITVHNATFTWARDLPpTLNGITFSI 661

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   367 KEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieeytlcslreHIATVLQDVFLFADSIYNNItLKNPAITE 446
Cdd:TIGR00957  662 PEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI-LFGKALNE 727

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   447 EEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQE---ATD 523
Cdd:TIGR00957  728 KYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhviGPE 807

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 496950271   524 KMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQiENGYYRNL 575
Cdd:TIGR00957  808 GVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ-RDGAFAEF 858

ABC_6TM_Sav1866_like

cd18554

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...

44-318

5.52e-28

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.

Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 114.05 E-value: 5.52e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  44 PYLIKVAIDNYI------TPKDYEGLVRIVYI-LIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFD 116
Cdd:cd18554   19 PLILKYIVDDVIqgssltLDEKVYKLFTIIGImFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 117 KSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSMNAAFVEVR 196
Cdd:cd18554   99 NNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERS 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 197 HQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIIGD 276
Cdd:cd18554  179 QALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEG 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 496950271 277 NVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18554  259 NL-TVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

343-564

2.77e-27

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: 110.02 E-value: 2.77e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytLCSLREHIATV 422
Cdd:cd03300    1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNI----TLK--NPAITEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYV 495
Cdd:cd03300   78 FQNYALFPHlTVFENIafglRLKklPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALV 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAH----RLTTvkkADRIIVLDKGKIVEIGNHEEL 564
Cdd:cd03300  147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdqeeALTM---SDRIAVMNKGKIQQIGTPEEI 218

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

343-565

3.88e-27

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: 109.59 E-value: 3.88e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILH---GISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI---EEYTLCSLR 416
Cdd:cd03258    2 IELKNVSKVFGDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQDVFLFAD-SIYNNITL------KNPAITEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIA 489
Cdd:cd03258   82 RRIGMIFQHFNLLSSrTVFENVALpleiagVPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSE----KLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:cd03258  151 IARALANNPKVLLCDEATSALDPETTqsilALLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228


                 .
gi 496950271 565 L 565
Cdd:cd03258  229 F 229

ZnuC

COG1121

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...

343-569

4.24e-27

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 4.24e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytlcsLREHIATV 422
Cdd:COG1121    7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQ-------------DVFLFadSIYNNI-TLKNPAITEEEVIAAA-KSIGVHNFLmslpegyHYNVKErgamLSAGQRQ- 486
Cdd:COG1121   81 PQraevdwdfpitvrDVVLM--GRYGRRgLFRRPSRADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQr 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 487 -LIAflRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEiGNHEE 563
Cdd:COG1121  148 vLLA--RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEE 224


                 ....*.
gi 496950271 564 LLQIEN 569
Cdd:COG1121  225 VLTPEN 230

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

355-565

2.08e-26

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: 107.81 E-value: 2.08e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeyTLCSLREHIATVLQDVFLFAD-SI 433
Cdd:cd03299   11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNIT-----LKNPAIT-EEEVIAAAKSIGVHNFLMSLPEgyhynvkergaMLSAGQRQLIAFLRAYVHKPQILILDEAT 507
Cdd:cd03299   89 YKNIAyglkkRKVDKKEiERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPF 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 508 SSVDSHS-EKLIQEATDKMTEGRTSII-IAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:cd03299  158 SALDVRTkEKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

343-555

2.43e-26

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: 107.11 E-value: 2.43e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEY---TLCSLREHI 419
Cdd:cd03292    1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFAD-SIYNNITL------KNPAITEEEVIAAAKSIGVHNFLMSLPEGyhynvkergamLSAGQRQLIAFLR 492
Cdd:cd03292   81 GVVFQDFRLLPDrNVYENVAFalevtgVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 493 AYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIA-HR---LTTVKKadRIIVLDKGKI 555
Cdd:cd03292  150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAkelVDTTRH--RVIALERGKL 214

cbiO

PRK13637

energy-coupling factor transporter ATPase;

343-584

2.47e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.98 E-value: 2.47e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAG----EEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI--EEYTLCSLR 416
Cdd:PRK13637   3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQ--DVFLFADSIYNNITL--KNPAITEEE----VIAAAKSIGVHNflmslpEGYhynvKERGAM-LSAGQRQL 487
Cdd:PRK13637  83 KKVGLVFQypEYQLFEETIEKDIAFgpINLGLSEEEienrVKRAMNIVGLDY------EDY----KDKSPFeLSGGQKRR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 488 IAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232

                        250       260
                 ....*....|....*....|
gi 496950271 565 LQiengyyrnlyEVQFLEEV 584
Cdd:PRK13637 233 FK----------EVETLESI 242

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

346-556

3.90e-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: 106.19 E-value: 3.90e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 346 EDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTlcsLREHIATVLQD 425
Cdd:cd03226    3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 V--FLFADSIYNNITLKNPAITEEEVIAAAksigvhnfLMSLPEGYHYnvKERGAM-LSAGQRQLIAFLRAYVHKPQILI 502
Cdd:cd03226   80 VdyQLFTDSVREELLLGLKELDAGNEQAET--------VLKDLDLYAL--KERHPLsLSGGQKQRLAIAAALLSGKDLLI 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:cd03226  150 FDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205

MglA

COG1129

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];

359-564

6.62e-26

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 6.62e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCS----LREHIATVLQDVFLFAD-SI 433
Cdd:COG1129   20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprdaQAAGIAIIHQELNLVPNlSV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITL-----KNPAITEEEVIAAAKSIgvhnfLMSLpeGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATS 508
Cdd:COG1129   97 AENIFLgreprRGGLIDWRAMRRRAREL-----LARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTA 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 509 SVDSH-SEKL---IQEATDkmtEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:COG1129  170 SLTEReVERLfriIRRLKA---QGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227

ABC_6TM_ABCB10_like

cd18573

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...

28-273

1.89e-25

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.

Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 106.44 E-value: 1.89e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  28 AVALFAVLSSIfSTAQPYLIKVAID-----NYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18573    1 ALALLLVSSAV-TMSVPFAIGKLIDvaskeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLfemaSDILKMFVITIV----MFVIDWKLALISYATMPLIL 178
Cdd:cd18573   80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL----SDGLRSLVSGVGgigmMLYISPKLTLVMLLVVPPIA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 179 YFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENF-KKINEKHKQAwLKTIWYNSIFFPIGDLC 257
Cdd:cd18573  156 VGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYaKKVDEVFDLA-KKEALASGLFFGSTGFS 234

                        250
                 ....*....|....*.
gi 496950271 258 VSITIALIVWFGGRQI 273
Cdd:cd18573  235 GNLSLLSVLYYGGSLV 250

ABC_6TM_Pgp_ABCB1_D1_like

cd18577

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...

31-285

2.35e-25

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.

Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 106.40 E-value: 2.35e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFS-TAQPYLIKV----------AIDNYITPKD-YEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRD 98
Cdd:cd18577    2 IIGLLAAIAAgAALPLMTIVfgdlfdaftdFGSGESSPDEfLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  99 VREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERI----GEIFSSGLFEMAsdilkMFVITIVM-FVIDWKLALISYAT 173
Cdd:cd18577   82 IRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIqdgiGEKLGLLIQSLS-----TFIAGFIIaFIYSWKLTLVLLAT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 174 MPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPI 253
Cdd:cd18577  157 LPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGL 236

                        250       260       270
                 ....*....|....*....|....*....|..
gi 496950271 254 GDLCVSITIALIVWFGGRQIIgDNVYDLGNIF 285
Cdd:cd18577  237 LFFIIFAMYALAFWYGSRLVR-DGEISPGDVL 267

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

359-566

5.24e-25

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: 104.65 E-value: 5.24e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLRE----HIATVLQDVFLFAD-SI 433
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITL------KNPAITEEEVIAAAKSIGVHNFLMSLPegyhynvKErgamLSAGQRQLIAFLRAYVHKPQILILDEAT 507
Cdd:cd03294  120 LENVAFglevqgVPRAEREERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 508 SSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:cd03294  189 SALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250

PRK11264

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional

355-565

8.07e-25

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 8.07e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI--------EEYTLCSLREHIATVLQDV 426
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FLFAD-SIYNNItLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERgamLSAGQRQLIAFLRAYVHKPQILILDE 505
Cdd:PRK11264  95 NLFPHrTVLENI-IEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDE 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 506 ATSSVDShseKLIQEATDKM----TEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK11264 171 PTSALDP---ELVGEVLNTIrqlaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

94-565

1.66e-24

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 108.84 E-value: 1.66e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    94 TVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFemasDILKMFVITI-VMFVIDWKLALISYA 172
Cdd:TIGR01271  955 TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLF----DFIQLTLIVLgAIFVVSVLQPYIFIA 1030

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   173 TMPLILYFTrwfqrSMNAAFVEVRHQVANLNAFVQERI--------SGIKVLQLFAQEREELENFKKINEKHKQAW---L 241
Cdd:TIGR01271 1031 AIPVAVIFI-----MLRAYFLRTSQQLKQLESEARSPIfshlitslKGLWTIRAFGRQSYFETLFHKALNLHTANWflyL 1105

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   242 KTI-WYNsiffpigdlcVSITIALIVWFGGRQII--GDNVYDLGNIFLFIQLSQQLFrpirhiadkfNTLQMGIIAS--- 315
Cdd:TIGR01271 1106 STLrWFQ----------MRIDIIFVFFFIAVTFIaiGTNQDGEGEVGIILTLAMNIL----------STLQWAVNSSidv 1165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   316 -------DRVFAILDTETD----TETGGEKELKEV--------------KGNIKFEDVRFEYV-AGEEILHGISFEVKEG 369
Cdd:TIGR01271 1166 dglmrsvSRVFKFIDLPQEeprpSGGGGKYQLSTVlvienphaqkcwpsGGQMDVQGLTAKYTeAGRAVLQDLSFSVEGG 1245

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   370 ETIAIVGATGAGKTTITNLLNRFYDlTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNITlKNPAITEEEV 449
Cdd:TIGR01271 1246 QRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEI 1323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   450 IAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGR 529
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 496950271   530 TSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

343-559

1.81e-24

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: 101.42 E-value: 1.81e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvaGEEILHgISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeyTLCSLREHIATV 422
Cdd:cd03298    1 VRLDKIRFSY--GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSML 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNITL-KNP-----AITEEEVIAAAKSIGVHNFLMSLPEgyhynvkergaMLSAGQRQLIAFLRAYV 495
Cdd:cd03298   76 FQENNLFAHlTVEQNVGLgLSPglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 496 HKPQILILDEATSSVDShseKLIQEATDKMTE-----GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03298  145 RDKPVLLLDEPFAALDP---ALRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

341-565

3.36e-24

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: 102.63 E-value: 3.36e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 341 GNIKFEDVRFEYV-AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDlTSGAIYIDGVNIEEYTLCSLREHI 419
Cdd:cd03289    1 GQMTVKDLTAKYTeGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFADSIYNNITlKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:cd03289   80 GVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 500 ILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:cd03289  159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224

cbiO

PRK13640

energy-coupling factor transporter ATPase;

343-566

3.37e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 3.37e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFY---DLTSGAIYIDGVNIEEYTLCSLREH 418
Cdd:PRK13640   6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQ--DVFLFADSIYNNIT--LKNPAITEEEVIA----AAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAF 490
Cdd:PRK13640  86 VGIVFQnpDNQFVGATVGDDVAfgLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 491 LRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKKADRIIVLDKGKI------VEIGNHE 562
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLlaqgspVEIFSKV 234


                 ....
gi 496950271 563 ELLQ 566
Cdd:PRK13640 235 EMLK 238

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

342-556

4.17e-24

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: 99.93 E-value: 4.17e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 342 NIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLN--RFYDLTSGAIYIDGVNIEEYtlcSLREHI 419
Cdd:cd03213    8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKR---SFRKII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDvflfaDSIYNNITlknpaiteeeviaaaksigVHNFLMslpegyhYNVKERGamLSAGQRQLIAFLRAYVHKPQ 499
Cdd:cd03213   85 GYVPQD-----DILHPTLT-------------------VRETLM-------FAAKLRG--LSGGERKRVSIALELVSNPS 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 500 ILILDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTT--VKKADRIIVLDKGKIV 556
Cdd:cd03213  132 LLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

355-556

4.60e-24

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: 98.65 E-value: 4.60e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCSLREH----IATVLQdvflfa 430
Cdd:cd03216   12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDArragIAMVYQ------ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 431 dsiynnitlknpaiteeeviaaaksigvhnflmslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQILILDEATSSV 510
Cdd:cd03216   83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 496950271 511 DSH-SEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:cd03216  114 TPAeVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

357-566

4.79e-24

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: 100.59 E-value: 4.79e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeytlcSLREH------IATVLQDVFLFA 430
Cdd:cd03224   14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPPHeraragIGYVPEGRRIFP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 431 D-SIYNNITLknpaiteeeviaAAKSIGVHNFLMSLPEGYHY--NVKER----GAMLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:cd03224   89 ElTVEENLLL------------GAYARRRAKRKARLERVYELfpRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 504 DEATSSVdshSEKLIQEATDKMT----EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:cd03224  157 DEPSEGL---APKIVEEIFEAIRelrdEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221

cbiO

PRK13650

energy-coupling factor transporter ATPase;

343-564

6.21e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 6.21e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE--ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIA 420
Cdd:PRK13650   5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQ--DVFLFADSIYNNIT--LKNPAITEEE----VIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLR 492
Cdd:PRK13650  85 MVFQnpDNQFVGATVEDDVAfgLENKGIPHEEmkerVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 493 AYVHKPQILILDEATSSVDSHSE-KLIQEATD-KMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

343-569

2.70e-23

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];

Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 99.00 E-value: 2.70e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGA-IYI-----DGVNIEEytlcsLR 416
Cdd:COG1119    4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWE-----LR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQDvflFADSIYNNITLknpaiteEEVIAAAK--SIGVHNF-----------LMSLPEGYHYnvKERG-AMLSA 482
Cdd:COG1119   78 KRIGLVSPA---LQLRFPRDETV-------LDVVLSGFfdSIGLYREptdeqrerareLLELLGLAHL--ADRPfGTLSQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 483 GQRQ--LIAflRAYVHKPQILILDEATSSVDSHSEKLIQEATDK-MTEGRTSII-IAHRL------TTvkkadRIIVLDK 552
Cdd:COG1119  146 GEQRrvLIA--RALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeippgIT-----HVLLLKD 218

                        250
                 ....*....|....*..
gi 496950271 553 GKIVEIGNHEELLQIEN 569
Cdd:COG1119  219 GRVVAAGPKEEVLTSEN 235

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

346-566

6.13e-23

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];

Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 99.74 E-value: 6.13e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 346 EDVRFEYVAGEEILH---GISFEVKEGETIAIVGATGAGKTTITNLLNRFYD---LTSGAIYIDGVNIEEYT---LCSLR 416
Cdd:COG0444    5 RNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSekeLRKIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 -EHIATVLQD-------VF----LFADSIYNNiTLKNPAITEEEVIAAAKSIGvhnflMSLPEGY-----HynvkergaM 479
Cdd:COG0444   85 gREIQMIFQDpmtslnpVMtvgdQIAEPLRIH-GGLSKAEARERAIELLERVG-----LPDPERRldrypH--------E 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEK----LIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGK 554
Cdd:COG0444  151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAqilnLLKDLQREL--GLAILFITHDLGVVAEiADRVAVMYAGR 228

                        250
                 ....*....|..
gi 496950271 555 IVEIGNHEELLQ 566
Cdd:COG0444  229 IVEEGPVEELFE 240

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

343-570

9.62e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 9.62e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEI-LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIAT 421
Cdd:PRK13648   8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDV-FLFADSIYN---NITLKNPAITEEE----VIAAAKSIGVHNFLMSLPEGyhynvkergamLSAGQRQLIAFLRA 493
Cdd:PRK13648  88 VFQNPdNQFVGSIVKydvAFGLENHAVPYDEmhrrVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 494 YVHKPQILILDEATSSVDSHSEK----LIQEAtdKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELLQIEN 569
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234


                 .
gi 496950271 570 G 570
Cdd:PRK13648 235 E 235

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

343-566

9.71e-23

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 9.71e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDV--RFeyvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG--VNIEEYTLCSLREH 418
Cdd:PRK09493   2 IEFKNVskHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQDVFLFAdsiynNIT-LKNPAITEEEVIAAAKSIG---VHNFL--MSLPEGYHYNVKErgamLSAGQRQLIAFLR 492
Cdd:PRK09493  79 AGMVFQQFYLFP-----HLTaLENVMFGPLRVRGASKEEAekqARELLakVGLAERAHHYPSE----LSGGQQQRVAIAR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 493 AYVHKPQILILDEATSSVDShseKLIQEATDKM----TEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDP---ELRHEVLKVMqdlaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225

PhnK

COG1101

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

358-556

1.18e-22

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 1.18e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeytlcSLREH-----IATVLQDvflfads 432
Cdd:COG1101   21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-----KLPEYkrakyIGRVFQD------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 iynniTLKN--PAITEEE--VIAAAK------SIGVHN-----F---LMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAY 494
Cdd:COG1101   89 -----PMMGtaPSMTIEEnlALAYRRgkrrglRRGLTKkrrelFrelLATLGLGLENRLDTKVGLLSGGQRQALSLLMAT 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKmtegrtsIIIAHRLTT----------VKKADRIIVLDKGKIV 556
Cdd:COG1101  164 LTKPKLLLLDEHTAALDPKTAALVLELTEK-------IVEENNLTTlmvthnmeqaLDYGNRLIMMHEGRII 228

MalK

COG3839

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...

343-564

1.65e-22

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.99 E-value: 1.65e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI-----EEytlcslRe 417
Cdd:COG3839    4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppKD------R- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 418 HIATVLQDVFLFAD-SIYNNIT--LKN----PAITEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAF 490
Cdd:COG3839   76 NIAMVFQSYALYPHmTVYENIAfpLKLrkvpKAEIDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVAL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 491 LRAYVHKPQILILDEATSSVDSH------SE-KLIQEATdkmteGRTSIIIAHRLT---TVkkADRIIVLDKGKIVEIGN 560
Cdd:COG3839  145 GRALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217


                 ....
gi 496950271 561 HEEL 564
Cdd:COG3839  218 PEEL 221

cbiO

PRK13646

energy-coupling factor transporter ATPase;

343-564

3.27e-22

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.27e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAG----EEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT----LCS 414
Cdd:PRK13646   3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LREHIATVLQ--DVFLFADSIYNNITL--KNPAITEEEVIAAAksigvHNFLMSLpeGYHYNVKERGAM-LSAGQRQLIA 489
Cdd:PRK13646  83 VRKRIGMVFQfpESQLFEDTVEREIIFgpKNFKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSPFqMSGGQMRKIA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMT--EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

357-565

3.37e-22

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: 95.43 E-value: 3.37e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTT----ITNLLNRfydlTSGAIYIDGVNIEeytlcSLREH------IATVLQDV 426
Cdd:COG0410   17 HVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLLPP----RSGSIRFDGEDIT-----GLPPHriarlgIGYVPEGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FLFAD-SIYNNITLknpaiteeeviAAAKSIGVHNFLMSLPEGYHY--NVKER----GAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:COG0410   88 RIFPSlTVEENLLL-----------GAYARRDRAEVRADLERVYELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 500 ILILDEAtssvdshSE----KLIQE---ATDKMTEGRTSIII----AHRLTTVkkADRIIVLDKGKIVEIGNHEELL 565
Cdd:COG0410  157 LLLLDEP-------SLglapLIVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELL 224

ABC_6TM_CyaB_HlyB_like

cd18588

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...

23-318

5.62e-22

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: 96.41 E-value: 5.62e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTM----QFLFSYYSNWLgqtvirD 98
Cdd:cd18588    1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLsglrTYLFSHTTNRI------D 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  99 VR--EKLFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPL 176
Cdd:cd18588   75 AElgARLFRHLLRLPLSYFESRQVGDTVAR-VRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 177 ILYFTRW----FQRSMNAAFveVRHqvANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFP 252
Cdd:cd18588  154 YALLSLLvtpiLRRRLEEKF--QRG--AENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQ 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 253 IGDLCVSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18588  230 IVQLIQKLTTLAILWFGAYLVM-DGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

343-554

6.07e-22

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: 94.08 E-value: 6.07e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTT----ITNLLNrfydLTSGAIYIDGVNIEEYTLcSLREH 418
Cdd:COG4133    3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDARE-DYRRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQDVFLFAD-SIYNNIT----LKNPAITEEEVIAAAKSIGVHNFLmslpegyhynvKERGAMLSAGQRQLIAFLRA 493
Cdd:COG4133   77 LAYLGHADGLKPElTVRENLRfwaaLYGLRADREAIDEALEAVGLAGLA-----------DLPVRQLSAGQKRRVALARL 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 494 YVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIA-HRLTTVkKADRIIVLDKGK 554
Cdd:COG4133  146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLEL-AAARVLDLGDFK 206

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

343-559

6.26e-22

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.

Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 94.24 E-value: 6.26e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytLCSLREHIATV 422
Cdd:cd03301    1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAD-SIYNNIT--LK----NPAITEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYV 495
Cdd:cd03301   78 FQNYALYPHmTVYDNIAfgLKlrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAH-RLTTVKKADRIIVLDKGKIVEIG 559
Cdd:cd03301  147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213

PRK13633

energy-coupling factor transporter ATPase;

343-564

7.33e-22

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 7.33e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEE-----ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI-EEYTLCSLR 416
Cdd:PRK13633   5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsDEENLWDIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQDvflfADsiyNNITlknPAITEEEVIAAAKSIGVhnflmsLPEGYHYNVKE-----------RGA--MLSAG 483
Cdd:PRK13633  85 NKAGMVFQN----PD---NQIV---ATIVEEDVAFGPENLGI------PPEEIRERVDEslkkvgmyeyrRHAphLLSGG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 484 QRQLIAFLRAYVHKPQILILDEATSSVDSHSEK----LIQEATDKmtEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIG 559
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRevvnTIKELNKK--YGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226


                 ....*
gi 496950271 560 NHEEL 564
Cdd:PRK13633 227 TPKEI 231

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

343-564

7.60e-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: 97.09 E-value: 7.60e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeytlcSL---REHI 419
Cdd:COG3842    6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLppeKRNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFAD-SIYNNIT--LKNPAITEEEviAAAKsigVHNFL--MSLpEGYHynvKERGAMLSAGQRQLIAFLRAY 494
Cdd:COG3842   80 GMVFQDYALFPHlTVAENVAfgLRMRGVPKAE--IRAR---VAELLelVGL-EGLA---DRYPHQLSGGQQQRVALARAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 495 VHKPQILILDEATSSVDSH------SE-KLIQEATdkmteGRTSIIIAHR----LTTvkkADRIIVLDKGKIVEIGNHEE 563
Cdd:COG3842  151 APEPRVLLLDEPLSALDAKlreemrEElRRLQREL-----GITFIYVTHDqeeaLAL---ADRIAVMNDGRIEQVGTPEE 222


                 .
gi 496950271 564 L 564
Cdd:COG3842  223 I 223

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

358-575

9.92e-22

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 9.92e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieeyTLCSLRE------HIATVLQDVFLFAd 431
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLElgagfhPELTGRENIYLNG- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 SIYnNITLKNPAITEEEVIAAAksiGVHNFLMsLPegyhynVKergaMLSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:COG1134  114 RLL-GLSRKEIDEKFDEIVEFA---ELGDFID-QP------VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 512 SH-SEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQiengYYRNL 575
Cdd:COG1134  179 AAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA----AYEAL 240

ABC_6TM_HetC_like

cd18568

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...

23-318

1.16e-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: 95.70 E-value: 1.16e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18568    1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18568   81 FYKHLLSLPLSFFASRKVGDIITR-FQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITI 262
Cdd:cd18568  160 LSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGT 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 263 ALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18568  240 IAVLWYGAYLVISGQL-TIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

359-566

1.35e-21

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: 98.60 E-value: 1.35e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTT----ITNLLNrfydlTSGAIYIDGVNIEEYT---LCSLREHIATVLQDVF---- 427
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPFgsls 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 428 ---LFADSIYNNITLKNPAITEEE----VIAAAKSIGvhnflmsLPEGY-----HynvkErgamLSAGQRQLIAFLRAYV 495
Cdd:COG4172  377 prmTVGQIIAEGLRVHGPGLSAAErrarVAEALEEVG-------LDPAArhrypH----E----FSGGQRQRIAIARALI 441

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 496 HKPQILILDEATSSVDSHSEK----LIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG4172  442 LEPKLLVLDEPTSALDVSVQAqildLLRDLQREH--GLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

347-564

1.44e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 1.44e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 347 DVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI--EEYTLCSLREHIATVLQ 424
Cdd:PRK13639   6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 425 --DVFLFADSIYNNITLK--NPAITEEE----VIAAAKSIGVHNFLMSLPegYHynvkergamLSAGQRQLIAFLRAYVH 496
Cdd:PRK13639  86 npDDQLFAPTVEEDVAFGplNLGLSKEEvekrVKEALKAVGMEGFENKPP--HH---------LSGGQKKRVAIAGILAM 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 497 KPQILILDEATSSVD----SHSEKLIQEATDkmtEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13639 155 KPEIIVLDEPTSGLDpmgaSQIMKLLYDLNK---EGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224

PRK10070

proline/glycine betaine ABC transporter ATP-binding protein ProV;

363-576

1.68e-21

proline/glycine betaine ABC transporter ATP-binding protein ProV;

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 1.68e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 363 SFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLRE----HIATVLQDVFLFA-----DSI 433
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhmtvlDNT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITLKNPAITE--EEVIAAAKSIGVHNFLMSLPEgyhynvkergaMLSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:PRK10070 128 AFGMELAGINAEErrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 512 SHSEKLIQEATDKM--TEGRTSIIIAHRL-TTVKKADRIIVLDKGKIVEIGNHEELL-QIENGYYRNLY 576
Cdd:PRK10070 197 PLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILnNPANDYVRTFF 265

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

343-565

2.35e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 2.35e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG--VNIEEYTLCSLREHIA 420
Cdd:PRK13636   6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQ--DVFLFADSIYNNITLK--NPAITEEE----VIAAAKSIGVHnflmslpegyHYNVKERGAmLSAGQRQLIAFLR 492
Cdd:PRK13636  86 MVFQdpDNQLFSASVYQDVSFGavNLKLPEDEvrkrVDNALKRTGIE----------HLKDKPTHC-LSFGQKKRVAIAG 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 493 AYVHKPQILILDEATSSVD----SHSEKLIQEATDKMteGRTSIIIAHRLTTVK-KADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230

AbcC

COG1135

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];

343-565

4.69e-21

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 94.76 E-value: 4.69e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGE---EILHGISFEVKEGETIAIVGATGAGKTT----ItNLLNRFydlTSGAIYIDGVNIEEYT---L 412
Cdd:COG1135    2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTlircI-NLLERP---TSGSVLVDGVDLTALSereL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 413 CSLREHIATVLQDVFLFaDS--IYNNITL-------KNPAITE--EEVIAaaksigvhnfLMSLPE-GYHYNvkergAML 480
Cdd:COG1135   78 RAARRKIGMIFQHFNLL-SSrtVAENVALpleiagvPKAEIRKrvAELLE----------LVGLSDkADAYP-----SQL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 481 SAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEK----LIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKI 555
Cdd:COG1135  142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRI 219

                        250
                 ....*....|
gi 496950271 556 VEIGNHEELL 565
Cdd:COG1135  220 VEQGPVLDVF 229

cbiO

PRK13641

energy-coupling factor transporter ATPase;

343-557

4.69e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 4.69e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEI----LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT----LCS 414
Cdd:PRK13641   3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LREHIATVLQ--DVFLFADSIYNNITL--KNPAITEEEVIAAA----KSIGVHNFLMSlpegyhynvkERGAMLSAGQRQ 486
Cdd:PRK13641  83 LRKKVSLVFQfpEAQLFENTVLKDVEFgpKNFGFSEDEAKEKAlkwlKKVGLSEDLIS----------KSPFELSGGQMR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 487 LIAFLRAYVHKPQILILDEATSSVDSHSEK-LIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIK 225

cbiO

PRK13644

energy-coupling factor transporter ATPase;

343-565

5.20e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 5.20e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT-LCSLREHIAT 421
Cdd:PRK13644   2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQ--DVFLFADSIYNNITL--KN----PAITEEEVIAAAKSIGVHNFLMSLPEgyhynvkergaMLSAGQRQLIAFLRA 493
Cdd:PRK13644  82 VFQnpETQFVGRTVEEDLAFgpENlclpPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 494 YVHKPQILILDEATSSVDSHSEKLIQEATDKMTE-GRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

343-565

8.00e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 8.00e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:PRK13647   5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDV--FLFADSIYNNITL--KNPAITEEEVI----AAAKSIGVHNFLMSLPegYHynvkergamLSAGQRQLIAFLRAY 494
Cdd:PRK13647  85 FQDPddQVFSSTVWDDVAFgpVNMGLDKDEVErrveEALKAVRMWDFRDKPP--YH---------LSYGQKKRVAIAGVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

329-559

8.23e-21

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: 91.44 E-value: 8.23e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 329 ETGGEKELKEVKGNIKFEDVRFEYVageEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnie 408
Cdd:cd03220   11 PTYKGGSSSLKKLGILGRKGEVGEF---WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 409 eyTLCSLRE------HIATVLQDVFLFAdSIYnNITLKNPAITEEEVIAAAKsigvhnflmsLPEGYHYNVKErgamLSA 482
Cdd:cd03220   84 --RVSSLLGlgggfnPELTGRENIYLNG-RLL-GLSRKEIDEKIDEIIEFSE----------LGDFIDLPVKT----YSS 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 483 GQRQLIAFLRAYVHKPQILILDEATSSVDSH-SEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03220  146 GMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224

ABC_6TM_CvaB_RaxB_like

cd18567

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...

23-310

9.82e-21

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: 92.91 E-value: 9.82e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18567    1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILkMFVIT-IVMFVIDWKLALISYATMplILYFT 181
Cdd:cd18567   81 LFRHLLRLPLSYFEKRHLGDIVSR-FGSLDEIQQTLTTGFVEALLDGL-MAILTlVMMFLYSPKLALIVLAAV--ALYAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 182 -RW--FQRSMNAAFVEVRHQvANLNAFVQERISGIKVLQLFAQEREELENF-----KKINEKHKQAWLkTIWYNSiffpI 253
Cdd:cd18567  157 lRLalYPPLRRATEEQIVAS-AKEQSHFLETIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRL-QILFSA----A 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 254 GDLCVSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQM 310
Cdd:cd18567  231 NGLLFGLENILVIYLGALLVL-DGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELRM 286

ugpC

PRK11650

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

342-564

1.25e-20

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 1.25e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 342 NIKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG--VNIEEytlCSLREhI 419
Cdd:PRK11650   3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELE---PADRD-I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFAD-SIYNNIT--LKNPAITEEE----VIAAAKSIGVHNFLmslpegyhynvKERGAMLSAGQRQLIAFLR 492
Cdd:PRK11650  79 AMVFQNYALYPHmSVRENMAygLKIRGMPKAEieerVAEAARILELEPLL-----------DRKPRELSGGQRQRVAMGR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 493 AYVHKPQILILDEATSSVDShseKL-------IQEATDKMteGRTSIIIAH-RLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA---KLrvqmrleIQRLHRRL--KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222

ABC_6TM_PrtD_LapB_HlyB_like

cd18782

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

23-298

1.58e-20

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: 92.27 E-value: 1.58e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18782    1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18782   81 IIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGI---KVLQLFAQEREELENF--KKINEKHKQAWLKTIWYNSIFFpIGDLc 257
Cdd:cd18782  160 LFGPILRRQIRRRAEASAKTQSYLVESLTGIqtvKAQNAELKARWRWQNRyaRSLGEGFKLTVLGTTSGSLSQF-LNKL- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 496950271 258 vsiTIALIVWFGGRQIIGdNVYDLGNIFLFIQLSQQLFRPI 298
Cdd:cd18782  238 ---SSLLVLWVGAYLVLR-GELTLGQLIAFRILSGYVTGPI 274

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

343-571

2.42e-20

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: 89.12 E-value: 2.42e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEyVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLL--NRFYDLTSGAIYIDGVNIEEYTLcSLRehia 420
Cdd:cd03217    1 LEIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPP-EER---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 tVLQDVFLfadsiynniTLKNPaiteeeviAAAKSIGVHNFLMSLPEGyhynvkergamLSAGQRQLIAFLRAYVHKPQI 500
Cdd:cd03217   75 -ARLGIFL---------AFQYP--------PEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDL 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 501 LILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIIAH--RLTTVKKADRIIVLDKGKIVEIGNHEELLQIE-NGY 571
Cdd:cd03217  126 AILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALEIEkKGY 200

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

355-557

3.57e-20

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: 89.20 E-value: 3.57e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytLCSLREHIATVLQdvflfADSIY 434
Cdd:cd03268   12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIE-----APGFY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 435 NNITlknpaiTEEEVIAAAKSIGV-HNFLMSLPE--GYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:cd03268   85 PNLT------ARENLRLLARLLGIrKKRIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 496950271 512 SHSEKLIQE-ATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:cd03268  159 PDGIKELRElILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIE 206

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

343-559

4.37e-20

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 88.88 E-value: 4.37e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTlcslREHIA-- 420
Cdd:cd03269    1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGyl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 ----------TVLQDVFLFADsiynnitLKNPAITEeeviaAAKSIgvHNFLMSLPEGYHYNVKERgaMLSAGQRQLIAF 490
Cdd:cd03269   76 peerglypkmKVIDQLVYLAQ-------LKGLKKEE-----ARRRI--DEWLERLELSEYANKRVE--ELSKGNQQKVQF 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 491 LRAYVHKPQILILDEATSSVDSHSEKLIQEA-TDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03269  140 IAAVIHDPELLILDEPFSGLDPVNVELLKDViRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

359-563

7.50e-20

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: 89.33 E-value: 7.50e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeytlcSLREH-IA----------------- 420
Cdd:COG0411   20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-----GLPPHrIArlgiartfqnprlfpel 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQDVFLFADS------IYNNITLKNPAITEEEVIAAAKSI----GVHNFLmslpegyhynvKERGAMLSAGQRQLIAF 490
Cdd:COG0411   95 TVLENVLVAAHArlgrglLAALLRLPRARREEREARERAEELlervGLADRA-----------DEPAGNLSYGQQRRLEI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 491 LRAYVHKPQILILDEATSSVdSHSEK-----LIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV------EI 558
Cdd:COG0411  164 ARALATEPKLLLLDEPAAGL-NPEETeelaeLIRRLRDER--GITILLIEHDMDLVMGlADRIVVLDFGRVIaegtpaEV 240


                 ....*
gi 496950271 559 GNHEE 563
Cdd:COG0411  241 RADPR 245

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

361-563

9.00e-20

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: 88.65 E-value: 9.00e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 361 GISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIeeytlCSLREH------IATVLQDVflfadSIY 434
Cdd:cd03219   18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-----TGLPPHeiarlgIGRTFQIP-----RLF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 435 NNITLknpaitEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERgAM------------------LSAGQRQLIAFLRAYVH 496
Cdd:cd03219   88 PELTV------LENVMVAAQARTGSGLLLARARREEREARER-AEellervgladladrpageLSYGQQRRLEIARALAT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 497 KPQILILDEATSSVdSHSEK-----LIQEATDKmteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV------EIGNHEE 563
Cdd:cd03219  161 DPKLLLLDEPAAGL-NPEETeelaeLIRELRER---GITVLLVEHDMDVVMSlADRVTVLDQGRVIaegtpdEVRNNPR 235

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

355-584

9.36e-20

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.16 E-value: 9.36e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCslREHIATVLQDVFLFAD-SI 433
Cdd:PRK09452  26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPHmTV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITL-----KNPAI-TEEEVIAAAKSIGVHNFlmslpegyhynVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEAT 507
Cdd:PRK09452 104 FENVAFglrmqKTPAAeITPRVMEALRMVQLEEF-----------AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 508 SSVDSHSEKLIQEATDKM--TEGRTSIIIAH----RLTTvkkADRIIVLDKGKIVEIGNHEELlqiengyY---RNLYEV 578
Cdd:PRK09452 173 SALDYKLRKQMQNELKALqrKLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREI-------YeepKNLFVA 242


                 ....*.
gi 496950271 579 QFLEEV 584
Cdd:PRK09452 243 RFIGEI 248

cbiO

PRK13642

energy-coupling factor transporter ATPase;

343-565

1.45e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 1.45e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEI--LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIA 420
Cdd:PRK13642   5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQ--DVFLFADSIYNNIT--LKNPAITEEEVIA----AAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLR 492
Cdd:PRK13642  85 MVFQnpDNQFVGATVEDDVAfgMENQGIPREEMIKrvdeALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 493 AYVHKPQILILDEATSSVD----SHSEKLIQEATDKMTegRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228

ABC_6TM_T1SS_like

cd18555

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...

23-318

1.71e-19

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: 89.11 E-value: 1.71e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18555    1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRAvNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLI---LY 179
Cdd:cd18555   81 FFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIvllLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 180 FTRWFQRSMNAafVEVRHQvANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFfpigdLCVS 259
Cdd:cd18555  160 LTRKKIKKLNQ--EEIVAQ-TKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNIL-----NSIS 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 260 ITI-----ALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18555  232 SSIqfiapLLILWIGAYLVINGEL-TLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294

ABC_6TM_AtABCB27_like

cd18780

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...

31-274

2.90e-19

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.

Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 88.46 E-value: 2.90e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFSTAQPYLIKVAID---NYITPKDYEGLVRIVYILIALLCAEV---TMQFLFSYYSNWLGQTVIRDVREKLF 104
Cdd:cd18780    3 IALLVSSGTNLALPYFFGQVIDavtNHSGSGGEEALRALNQAVLILLGVVLigsIATFLRSWLFTLAGERVVARLRKRLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 105 AHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWF 184
Cdd:cd18780   83 SAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIY 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 185 QRsmnaaFV-EVRHQV----ANLNAFVQERISGIKVLQLFAQEREELENF-KKINEKHKQAwLKTIWYNSIFFPIGDLCV 258
Cdd:cd18780  163 GK-----YVrKLSKKFqdalAAASTVAEESISNIRTVRSFAKETKEVSRYsEKINESYLLG-KKLARASGGFNGFMGAAA 236

                        250
                 ....*....|....*.
gi 496950271 259 SITIALIVWFGGRQII 274
Cdd:cd18780  237 QLAIVLVLWYGGRLVI 252

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

343-566

4.14e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.77 E-value: 4.14e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEI----LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT----LCS 414
Cdd:PRK13634   3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkkLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LREHIATVLQdvF----LFADSIYNNITL--KNPAITEEEVIAAAKSIgvhNFLMSLPEgyhyNVKERGAM-LSAGQRQL 487
Cdd:PRK13634  83 LRKKVGIVFQ--FpehqLFEETVEKDICFgpMNFGVSEEDAKQKAREM---IELVGLPE----ELLARSPFeLSGGQMRR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 488 IAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKM--TEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233


                 ..
gi 496950271 565 LQ 566
Cdd:PRK13634 234 FA 235

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

346-556

4.56e-19

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 4.56e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 346 EDVRFEYVAGEE---ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEY---TLCSL-REH 418
Cdd:PRK10535   8 KDIRRSYPSGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLrREH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQDVFLFAD-SIYNNITLknPAI----TEEEVIAAAKSIGVHnflMSLPEGYHYnvkeRGAMLSAGQRQLIAFLRA 493
Cdd:PRK10535  88 FGFIFQRYHLLSHlTAAQNVEV--PAVyaglERKQRLLRAQELLQR---LGLEDRVEY----QPSQLSGGQQQRVSIARA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 494 YVHKPQILILDEATSSVDSHSEKLIQEATDKMTE-GRTSIIIAHRLTTVKKADRIIVLDKGKIV 556
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

361-564

5.13e-19

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: 86.02 E-value: 5.13e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 361 GISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIeEYTLCSLREHIATVLQDvflfaDSIYNNIT-- 438
Cdd:cd03263   20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQF-----DALFDELTvr 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 439 --------LKNPAITEEEVIAAAKSIGVhnflmSLPEgyHYNVKERgaMLSAGQRQLIAFLRAYVHKPQILILDEATSSV 510
Cdd:cd03263   94 ehlrfyarLKGLPKSEIKEEVELLLRVL-----GLTD--KANKRAR--TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 511 DSHSEKLIQEATDKMTEGRTSIIIAH------RLttvkkADRIIVLDKGKIVEIGNHEEL 564
Cdd:cd03263  165 DPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIGSPQEL 219

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

359-566

6.85e-19

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.28 E-value: 6.85e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIeeYTLCSLRE-HIATVLQDVFLFAD-SIYNN 436
Cdd:COG1118   18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRErRVGFVFQHYALFPHmTVAEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 437 I--TLKNPAITEEEviAAAKsigVHNFL--MSLpEGYHynvKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDS 512
Cdd:COG1118   96 IafGLRVRPPSKAE--IRAR---VEELLelVQL-EGLA---DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 513 HSEK--------LIQEatdkmtEGRTSIIIAH------RLttvkkADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG1118  167 KVRKelrrwlrrLHDE------LGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYD 223

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

353-564

8.74e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 8.74e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 353 VAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDlTSGAIYIDGVNIEEYT---LCSLREHIATVLQDvflf 429
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQD---- 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 430 ADSIYN-----------NITLKNPAIT----EEEVIAAAKSIGVHnflmslPEGYHYNVKErgamLSAGQRQLIAFLRAY 494
Cdd:PRK15134 371 PNSSLNprlnvlqiieeGLRVHQPTLSaaqrEQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARAL 440

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMTEGR--TSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

344-559

1.41e-18

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.

Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 84.73 E-value: 1.41e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 344 KFEDVRFEYVAgeeiLHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIeeytlcsLREHIATVL 423
Cdd:cd03266   10 RFRDVKKTVQA----VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-------VKEPAEARR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 424 QDVFLFA-DSIYNNITLKnpaiteEEVIAAAKSIGVH--------NFLMSLPEGYHYnVKERGAMLSAGQRQLIAFLRAY 494
Cdd:cd03266   79 RLGFVSDsTGLYDRLTAR------ENLEYFAGLYGLKgdeltarlEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARAL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIA-HRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03266  152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218

cbiO

PRK13649

energy-coupling factor transporter ATPase;

343-585

2.71e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.18 E-value: 2.71e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEI----LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT----LCS 414
Cdd:PRK13649   3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LREHIATVLQ--DVFLFADSIYNNITL--KNPAITEEEVIAAAKSigvHNFLMSLPEgyhyNVKERGAM-LSAGQRQLIA 489
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFgpQNFGVSQEEAEALARE---KLALVGISE----SLFEKNPFeLSGGQMRRVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE-GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQi 567
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ- 234

                        250
                 ....*....|....*...
gi 496950271 568 engyyrnlyEVQFLEEVK 585
Cdd:PRK13649 235 ---------DVDFLEEKQ 243

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

343-564

3.52e-18

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: 83.93 E-value: 3.52e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCSLRE-HIAT 421
Cdd:cd03296    3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFAD-SIYNNIT----LKNPAITEEEVIAAAKsigVHNFL--MSLpEGYHynvKERGAMLSAGQRQLIAFLRAY 494
Cdd:cd03296   79 VFQHYALFRHmTVFDNVAfglrVKPRSERPPEAEIRAK---VHELLklVQL-DWLA---DRYPAQLSGGQRQRVALARAL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 495 VHKPQILILDEATSSVDSHSEK----LIQEATDKMteGRTSIIIAH-RLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:cd03296  152 AVEPKVLLLDEPFGALDAKVRKelrrWLRRLHDEL--HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

359-556

3.99e-18

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 3.99e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCS----LREHIATVLQDvFLFAD--S 432
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIALGIGMVHQH-FMLVPnlT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 IYNNITL-----KNPAITEEEVIAAAKSIGvhnflmslpEGYHYNV--KERGAMLSAGQRQLIAFLRAYVHKPQILILDE 505
Cdd:COG3845   97 VAENIVLgleptKGGRLDRKAARARIRELS---------ERYGLDVdpDAKVEDLSVGEQQRVEILKALYRGARILILDE 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 506 ATsSV--DSHSEKLIqEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:COG3845  168 PT-AVltPQEADELF-EILRRLAaEGKSIIFITHKLREVMAiADRVTVLRRGKVV 220

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

357-564

4.70e-18

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: 83.19 E-value: 4.70e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLcSLREHIATVLQD----------- 425
Cdd:cd03265   14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDlsvddeltgwe 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 -VFLFAdSIYNnitLKNPAITE--EEVIAaaksigvhnfLMSLPEGYHYNVKErgamLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:cd03265   93 nLYIHA-RLYG---VPGAERREriDELLD----------FVGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLF 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKM--TEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:cd03265  155 LDEPTIGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

343-562

4.92e-18

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 4.92e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAgEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG------VNIEEYTLCSLR 416
Cdd:PRK11124   3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQDVFLFAD-SIYNNIT---LKNPAITEEEVIAAAKSIgvhnfLMSLPEGYHynvKERGAM-LSAGQRQLIAFL 491
Cdd:PRK11124  82 RNVGMVFQQYNLWPHlTVQQNLIeapCRVLGLSKDQALARAEKL-----LERLRLKPY---ADRFPLhLSGGQQQRVAIA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 492 RAYVHKPQILILDEATSSVD----SHSEKLIQEATDKmteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHE 562
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDpeitAQIVSIIRELAET---GITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

343-559

1.13e-17

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.47 E-value: 1.13e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEY-VAGEEI--LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI---EEYTLCSLR 416
Cdd:PRK11153   2 IELKNISKVFpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQDVFLFAD-SIYNNITLknP---AITEEEVIAAAksigVHNFL--MSLPEGYH-YNvkergAMLSAGQRQLIA 489
Cdd:PRK11153  82 RQIGMIFQHFNLLSSrTVFDNVAL--PlelAGTPKAEIKAR----VTELLelVGLSDKADrYP-----AQLSGGQKQRVA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

358-559

1.47e-17

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: 81.93 E-value: 1.47e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLN---RFYDLTSGAIYIDGVNIEEYTlcsLREHIATVLQDVFLF----- 429
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQ---FQKCVAYVRQDDILLpgltv 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 430 ADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGyHYNVKErgamLSAGQRQLIAFLRAYVHKPQILILDEATSS 509
Cdd:cd03234   99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-GNLVKG----ISGGERRRVSIAVQLLWDPKVLILDEPTSG 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 510 VDSHSE-KLIQEATDKMTEGRTSIIIAH--RLTTVKKADRIIVLDKGKIVEIG 559
Cdd:cd03234  174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226

PRK10908

cell division ATP-binding protein FtsE;

343-561

1.53e-17

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 1.53e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI---EEYTLCSLREHI 419
Cdd:PRK10908   2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 420 ATVLQDVFLFAD-SIYNNITLknPAI--------TEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAF 490
Cdd:PRK10908  82 GMIFQDHHLLMDrTVYDNVAI--PLIiagasgddIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGI 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 491 LRAYVHKPQILILDEATSSVDSH-SEKLIQEATDKMTEGRTSIIIAHRLTTVKKAD-RIIVLDKGKIVeiGNH 561
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH--GGV 219

ABC_6TM_PrtD_LapB_HlyB_like

cd18566

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...

23-274

1.65e-17

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: 83.40 E-value: 1.65e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREK 102
Cdd:cd18566    1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18566   81 AFEHLLSLPLSFFEREPSGAHLER-LNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITI 262
Cdd:cd18566  160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM 239

                        250
                 ....*....|..
gi 496950271 263 ALIVWFGGRQII 274
Cdd:cd18566  240 VAVVAFGALLVI 251

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

353-569

1.84e-17

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 1.84e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 353 VAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQdvflfads 432
Cdd:PRK13548  12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ-------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 iYNNITLknpAITEEEVIAaaksIGvhnfLMSLPEGYHyNVKE--RGAM---------------LSAGQRQLIAFLRA-- 493
Cdd:PRK13548  84 -HSSLSF---PFTVEEVVA----MG----RAPHGLSRA-EDDAlvAAALaqvdlahlagrdypqLSGGEQQRVQLARVla 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 494 ----YVHKPQILILDEATSSVD-SHSEKLIQEATDK-MTEGRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:PRK13548 151 qlwePDGPPRWLLLDEPTSALDlAHQHHVLRLARQLaHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230


                 ...
gi 496950271 567 IEN 569
Cdd:PRK13548 231 PET 233

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

363-566

2.03e-17

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 2.03e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 363 SFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNieeYTLCS-LREHIATVLQDVFLFAD-SIYNNITLK 440
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPpSRRPVSMLFQENNLFSHlTVAQNIGLG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 441 -NPAIT-----EEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDS-- 512
Cdd:PRK10771  96 lNPGLKlnaaqREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPal 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 513 HSE--KLIQEATDkmTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:PRK10771 165 RQEmlTLVSQVCQ--ERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

336-550

2.32e-17

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 2.32e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 336 LKEVKGNIKFEDVRFEyVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSL 415
Cdd:PRK10247   1 MQENSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 416 REHIATVLQDVFLFADSIYNNIT----LKNPAITEEEVIAAAKSIGvhnflmsLPEGYhynVKERGAMLSAGQRQLIAFL 491
Cdd:PRK10247  80 RQQVSYCAQTPTLFGDTVYDNLIfpwqIRNQQPDPAIFLDDLERFA-------LPDTI---LTKNIAELSGGEKQRISLI 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 492 RAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKKADRIIVL 550
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVITL 210

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

359-564

2.42e-17

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.48 E-value: 2.42e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEY---TLCSLREHIATVLQDVF-------- 427
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNPYgslnprkk 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 428 ---LFADSIYNNITLkNPAITEEEVIAAAKSIGVHnflmslPEgyHYnvKERGAMLSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:PRK11308 111 vgqILEEPLLINTSL-SAAERREKALAMMAKVGLR------PE--HY--DRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 505 EATSSVD-SHSEKLIQEATDKMTEGRTS-IIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK11308 180 EPVSALDvSVQAQVLNLMMDLQQELGLSyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

357-565

2.88e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.88 E-value: 2.88e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL-----TSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFAD 431
Cdd:PRK14247  17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 -SIYNNITL--------KNPAITEEEVIAAAKSIGVHNflmslpegyhyNVKER----GAMLSAGQRQLIAFLRAYVHKP 498
Cdd:PRK14247  97 lSIFENVALglklnrlvKSKKELQERVRWALEKAQLWD-----------EVKDRldapAGKLSGGQQQRLCIARALAFQP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 499 QILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233

ABC_6TM_AarD_CydDC_like

cd18561

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...

29-316

3.42e-17

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).

Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 82.33 E-value: 3.42e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  29 VALFAVLSSIFSTAQPYLIKVAIDNYITPKDYE------GLVRIVYILIALL--CAEVtmqflFSYYSnwlGQTVIRDVR 100
Cdd:cd18561    1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEdimpplAGIAGVIVLRAALlwLRER-----VAHRA---AQRVKQHLR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 101 EKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYF 180
Cdd:cd18561   73 RRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 181 TRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSI 260
Cdd:cd18561  153 PALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATAL 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 261 TIALIVWFGGRQIIGDNVyDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASD 316
Cdd:cd18561  233 GTALALGVGALRVLGGQL-TLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAAD 287

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

352-565

4.67e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 4.67e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 352 YVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGV------NIEEYTLCSLREHIATVLQD 425
Cdd:PRK14246  19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 VFLFAD-SIYNNIT--LKNPAITEEEVIAAAKSIGVHNflMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:PRK14246  99 PNPFPHlSIYDNIAypLKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240

PRK14239

phosphate transporter ATP-binding protein; Provisional

352-564

5.63e-17

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.98 E-value: 5.63e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 352 YVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL-----TSGAIYIDGVNIeeYT----LCSLREHIATV 422
Cdd:PRK14239  14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNI--YSprtdTVDLRKEIGMV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFADSIYNNIT-------LKNPAITEEEVIAAAKSIGVHNflmslpegyhyNVKER---GAM-LSAGQRQLIAFL 491
Cdd:PRK14239  92 FQQPNPFPMSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIWD-----------EVKDRlhdSALgLSGGQQQRVCIA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 492 RAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

358-557

7.05e-17

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 7.05e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTlcslREHIATVLQDVFL-FADSiynn 436
Cdd:PRK10419  27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN----RAQRKAFRRDIQMvFQDS---- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 437 ITLKNPAITEEEVIA-----------AAKSIGVHNFL--MSLPEGYhynVKERGAMLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:PRK10419  99 ISAVNPRKTVREIIReplrhllsldkAERLARASEMLraVDLDDSV---LDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 504 DEATSSVDSHSE-KLIQEATDKMTEGRTS-IIIAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:PRK10419 176 DEAVSNLDLVLQaGVIRLLKKLQQQFGTAcLFITHDLRLVERfCQRVMVMDNGQIVE 232

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

362-559

7.16e-17

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: 79.65 E-value: 7.16e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVkEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGV-------NIEeytLCSLREHIATVLQDVFLFAD-SI 433
Cdd:cd03297   17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKIN---LPPQQRKIGLVFQQYALFPHlNV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNIT--LKNPAITEEEVIAAAKSIgvhnfLMSLPEgyhynVKERG-AMLSAGQRQLIAFLRAYVHKPQILILDEATSSV 510
Cdd:cd03297   93 RENLAfgLKRKRNREDRISVDELLD-----LLGLDH-----LLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496950271 511 DSHS-EKLIQEATDKMTE-GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03297  163 DRALrLQLLPELKQIKKNlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

362-566

8.60e-17

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.07 E-value: 8.60e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCSLREH-IATVLQDVFLFAD-SIYNNIT- 438
Cdd:PRK11432  25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFPHmSLGENVGy 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 439 -LKNPAITEEEVIAaaksigvhnflmslpegyhyNVKERGAM-------------LSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:PRK11432 102 gLKMLGVPKEERKQ--------------------RVKEALELvdlagfedryvdqISGGQQQRVALARALILKPKVLLFD 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 505 EATSSVD-----SHSEKlIQEATDKMteGRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:PRK11432 162 EPLSNLDanlrrSMREK-IRELQQQF--NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYR 226

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

298-565

1.29e-16

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: 82.93 E-value: 1.29e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  298 IRHIADKFNTLQMGIIA----SDRVFAILdTETDTETGGEKELKEVKGNIKFEDVRFEYVAGE----EILHGISFEVKEG 369
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKeegtPDEVVAVF-MEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDrgvvKAVDNVSLEVKEG 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  370 ETIAIVGATGAGKTTITNLLNRFYDLTSGAIY-------ID----------------GVNIEEYTLC-------SLREHI 419
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDmtkpgpdgrgrakryiGILHQEYDLYphrtvldNLTEAI 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  420 ATVLQDVFLFADSIYnniTLKNPAITEEEviaaAKSIgvhnfLMSLPEgyhynvkergaMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:TIGR03269 391 GLELPDELARMKAVI---TLKMVGFDEEK----AEEI-----LDKYPD-----------ELSEGERHRVALAQVLIKEPR 447

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271  500 ILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

350-553

2.00e-16

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: 78.53 E-value: 2.00e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 350 FEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSL----REHIATVLQD 425
Cdd:cd03290    8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 VFLFADSIYNNITLKNPaITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDE 505
Cdd:cd03290   88 PWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 506 ATSSVDSH-SEKLIQEATDKM--TEGRTSIIIAHRLTTVKKADRIIVLDKG 553
Cdd:cd03290  167 PFSALDIHlSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAMKDG 217

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

355-572

2.22e-16

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 2.22e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytLCSLREHIATVLQDVFLFAD-SI 433
Cdd:PRK11607  31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFPHmTV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNIT--LKNPAITEEEVIAAAKSigvhnfLMSLPEGYHYnVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:PRK11607 109 EQNIAfgLKQDKLPKAEIASRVNE------MLGLVHMQEF-AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 512 SHSEKLIQ-EATDKMTE-GRTSIIIAH-RLTTVKKADRIIVLDKGKIVEIGNHEELLQIENGYY 572
Cdd:PRK11607 182 KKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245

PRK10619

histidine ABC transporter ATP-binding protein HisP;

357-565

2.61e-16

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 2.61e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI-------------EEYTLCSLREHIATVL 423
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 424 QDVFLFAdsiyNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEgyhYNVKERG-----AMLSAGQRQLIAFLRAYVHKP 498
Cdd:PRK10619  99 QHFNLWS----HMTVLENVMEAPIQVLGLSKQEARERAVKYLAK---VGIDERAqgkypVHLSGGQQQRVSIARALAMEP 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 499 QILILDEATSSVDShseKLIQEATDKMT----EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK10619 172 EVLLFDEPTSALDP---ELVGEVLRIMQqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240

YhaQ

COG4152

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

359-580

4.89e-16

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.00 E-value: 4.89e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytlcSLREHIA------------TVLQDV 426
Cdd:COG4152   17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGylpeerglypkmKVGEQL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FLFAdsiynniTLKNpaITEEEVIAAAKsigvhnFLMS---LPEGYHYNVKErgamLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:COG4152   93 VYLA-------RLKG--LSKAEAKRRAD------EWLErlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLIL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 504 DEATSSVDSHS-EKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNheeLLQIENGYYRNLYEVQF 580
Cdd:COG4152  154 DEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS---VDEIRRQFGRNTLRLEA 229

PRK13651

cobalt transporter ATP-binding subunit; Provisional

343-583

5.06e-16

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 5.06e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEI----LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAI---YIDGVN------IEE 409
Cdd:PRK13651   3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNkkktkeKEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 410 YT---------------LCSLREHIATVLQ--DVFLFADSIynnitlknpaitEEEVIAAAKSIGVHNF----------- 461
Cdd:PRK13651  83 VLeklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTI------------EKDIIFGPVSMGVSKEeakkraakyie 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 462 LMSLPEGYhynVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIIAHRLTT 540
Cdd:PRK13651 151 LVGLDESY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDN 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 496950271 541 V-KKADRIIVLDKGKIVEIGNHEELLQiengyyrnlyEVQFLEE 583
Cdd:PRK13651 228 VlEWTKRTIFFKDGKIIKDGDTYDILS----------DNKFLIE 261

PRK15112

peptide ABC transporter ATP-binding protein SapF;

357-565

5.50e-16

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.29 E-value: 5.50e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIE--EYTLCSLRehIATVLQDV-------- 426
Cdd:PRK15112  27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPstslnprq 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 ----FLFADSIYNniTLKNPAITEEEVIAAAKSIGVhnflmsLPEGYHYNVKergaMLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:PRK15112 105 risqILDFPLRLN--TDLEPEQREKQIIETLRQVGL------LPDHASYYPH----MLAPGQKQRLGLARALILRPKVII 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 503 LDEATSSVD----SHSEKLIQEATDKmtEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK15112 173 ADEALASLDmsmrSQLINLMLELQEK--QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238

cbiO

PRK13643

energy-coupling factor transporter ATPase;

343-566

1.02e-15

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 1.02e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVA----GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI----EEYTLCS 414
Cdd:PRK13643   2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LREHIATVLQ--DVFLFADSIYNNITL--KNPAITEEEviaaAKSIGVHNFLMSlpeGYHYNVKERGAM-LSAGQRQLIA 489
Cdd:PRK13643  82 VRKKVGVVFQfpESQLFEETVLKDVAFgpQNFGIPKEK----AEKIAAEKLEMV---GLADEFWEKSPFeLSGGQMRRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE-GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

343-552

1.19e-15

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).

Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.88 E-value: 1.19e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieeytlcslREHIATV 422
Cdd:cd03223    1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLfadsiynnitlknPAITEEEVIAaaksigvhnflmslpegYHYnvkerGAMLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:cd03223   70 PQRPYL-------------PLGTLREQLI-----------------YPW-----DDVLSGGEQQRLAFARLLLHKPKFVF 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKMteGRTSIIIAHRLTTVKKADRIIVLDK 552
Cdd:cd03223  115 LDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLDG 162

ABC_6TM_AarD_CydD

cd18584

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...

29-243

1.31e-15

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).

Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 77.45 E-value: 1.31e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  29 VALFAVLSSIFSTAQPYLIKVAIDNYITPK-DYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHL 107
Cdd:cd18584    1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 108 LRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFT----RW 183
Cdd:cd18584   81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMiligKA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 184 FQRSMNAAFVEVRHqvanLNAFVQERISGIKVLQLFAQEREELENFKKINEKHKQAWLKT 243
Cdd:cd18584  161 AQAASRRQWAALSR----LSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKV 216

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

354-565

1.40e-15

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 1.40e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIY-----IDGVNIEEY-TLCSLREHIATVLQDVF 427
Cdd:PRK14271  32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYrDVLEFRRRVGMLFQRPN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 428 LFADSIYNNITlknPAITEEEVIAAAKSIGVHNFLMSlPEGYHYNVKERGA----MLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:PRK14271 112 PFPMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLT-EVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLL 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 504 DEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250

PTZ00243

ABC transporter; Provisional

323-566

1.53e-15

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.59 E-value: 1.53e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  323 DTETDTETGGEKELKEVKgnikfeDVRFEYVAgEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYI 402
Cdd:PTZ00243  647 HEATPTSERSAKTPKMKT------DDFFELEP-KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  403 DgvnieeytlcslrEHIATVLQDVFLFADSIYNNITLknpaITEEEVIAAAKSIGVHNF---LMSLPEGYHYNVKERGAM 479
Cdd:PTZ00243  720 E-------------RSIAYVPQQAWIMNATVRGNILF----FDEEDAARLADAVRVSQLeadLAQLGGGLETEIGEKGVN 782

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSH-SEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEI 558
Cdd:PTZ00243  783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFS 862


                  ....*...
gi 496950271  559 GNHEELLQ 566
Cdd:PTZ00243  863 GSSADFMR 870

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

343-562

1.76e-15

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.63 E-value: 1.76e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFADSIYNNITLKNPAITEEEViaaaKSIGVHNFLmSLPEGYHYNVKergamLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALVEKWL----ERLKMAHKL-ELEDGRISNLK-----LSKGQKKRLALLLALAEERDILL 472

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 503 LDEATSSVDSHSEKLI-QEATDKMTE-GRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHE 562
Cdd:PRK10522 473 LDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEE 534

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

348-565

1.91e-15

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: 79.34 E-value: 1.91e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 348 VRFEYVAGE-EILHGISFEVKEGETIAIVGATGAGKT----TITNLLNRFYDLTSGAIYIDGVNI---EEYTLCSLR-EH 418
Cdd:COG4172   14 VAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 419 IATVLQD-------VFLFADSIYNNITLK---NPAITEEEVIAAAKSIGVHNflmslPEG----Y-HynvkergaMLSAG 483
Cdd:COG4172   94 IAMIFQEpmtslnpLHTIGKQIAEVLRLHrglSGAAARARALELLERVGIPD-----PERrldaYpH--------QLSGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 484 QRQ--LIAFlrAYVHKPQILILDEATSSVDSHSE----KLIQEATDKMtegRTSII-IAHRLTTVKK-ADRIIVLDKGKI 555
Cdd:COG4172  161 QRQrvMIAM--ALANEPDLLIADEPTTALDVTVQaqilDLLKDLQREL---GMALLlITHDLGVVRRfADRVAVMRQGEI 235

                        250
                 ....*....|
gi 496950271 556 VEIGNHEELL 565
Cdd:COG4172  236 VEQGPTAELF 245

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

9-553

2.42e-15

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 2.42e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   9 KHTFRQLSRFVKPY---RGVFIAVALFAVL--SSIFSTAqpylIKVAIdNY--------ITPKDYEGLVR--IVYILIAL 73
Cdd:COG4178    1 RSLLRQFWRLARPYwrsEEKWKAWGLLALLllLTLASVG----LNVLL-NFwnrdfydaLQARDAAAFWQqlGVFALLAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  74 LCAevtmqfLFSYYSNWLGQTVIRDVREKLFAHLLRfkmRYFDKSS---IGVLVTRAVNDMERIGE---IFSSGLFEMAS 147
Cdd:COG4178   76 ISI------LLAVYQTYLRQRLQIRWREWLTERLLD---RWLSNRAyyrLQLSGGEIDNPDQRIAEdirLFTETTLSLSL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 148 DILKMfVITIVMFV-IDWKL---------------------ALISYATM----------PLI-LYFTRwfQRSmNAAFve 194
Cdd:COG4178  147 GLLSS-VVTLISFIgILWSLsgsltftlggysitipgymvwAALIYAIIgtllthligrPLIrLNFEQ--QRR-EADF-- 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 195 vRHQVANLN------AFVQ-ERISGIKVLQLFAQEreeLENFKKINEKHKQ-AWLKTIwYN--SIFFPIGdlcvsitIAL 264
Cdd:COG4178  221 -RFALVRVRenaesiALYRgEAAERRRLRRRFDAV---IANWRRLIRRQRNlTFFTTG-YGqlAVIFPIL-------VAA 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 265 IVWFGGrQIigdnvyDLGniflfiQLSQqlfrpirhIADKFNTLQ---------MGIIAS-----DRV--FAILDTETDT 328
Cdd:COG4178  289 PRYFAG-EI------TLG------GLMQ--------AASAFGQVQgalswfvdnYQSLAEwratvDRLagFEEALEAADA 347

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 329 ETGGEKELKEVKGN-IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTitnLLnRfydltsgAI-----YI 402
Cdd:COG4178  348 LPEAASRIETSEDGaLALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST---LL-R-------AIaglwpYG 416

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 403 DGvnieEYTLCSLrEHIATVLQDVFLFADSIYNNITLKNPA--ITEEEVIAAAKSIGVHNFLMSLPEgyhynVKERGAML 480
Cdd:COG4178  417 SG----RIARPAG-ARVLFLPQRPYLPLGTLREALLYPATAeaFSDAELREALEAVGLGHLAERLDE-----EADWDQVL 486

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 481 SAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKG 553
Cdd:COG4178  487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

354-565

2.80e-15

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 2.80e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFL-FADS 432
Cdd:PRK09536  14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 IYNNITL-KNPAIT---------EEEVIAAAKSIGVHNFlmslpegyhynVKERGAMLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:PRK09536  94 VRQVVEMgRTPHRSrfdtwtetdRAAVERAMERTGVAQF-----------ADRPVTSLSGGERQRVLLARALAQATPVLL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 503 LDEATSSVD-SHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK09536 163 LDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

343-564

3.49e-15

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 3.49e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAgEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTS-----GAIYIDGVNIEE--YTLCSL 415
Cdd:PRK14258   8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 416 REHIATVLQDVFLFADSIYNNITLK------NPAITEEEVIAAAksIGVHNFLMSLPEGYHYNVKErgamLSAGQRQLIA 489
Cdd:PRK14258  87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESA--LKDADLWDEIKHKIHKSALD----LSGGQQQRLC 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHS----EKLIQeaTDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQ--SLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEF 237

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

343-564

5.59e-15

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 5.59e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATV 422
Cdd:PRK13652   4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQ--DVFLFADSIYNNITLK--NPAITEE----EVIAAAKSIGVHNFLMSLPegYHynvkergamLSAGQRQLIAFLRAY 494
Cdd:PRK13652  84 FQnpDDQIFSPTVEQDIAFGpiNLGLDEEtvahRVSSALHMLGLEELRDRVP--HH---------LSGGEKKRVAIAGVI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

343-559

8.80e-15

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: 73.38 E-value: 8.80e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGeTIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLcSLREHIATV 422
Cdd:cd03264    1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVflfadSIYNNIT----------LK--NPAITEEEVIAAAKSIGVHNFLmslpegyhynvKERGAMLSAGQRQLIAF 490
Cdd:cd03264   78 PQEF-----GVYPNFTvrefldyiawLKgiPSKEVKARVDEVLELVNLGDRA-----------KKKIGSLSGGMRRRVGI 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 491 LRAYVHKPQILILDEATSSVDShSEK-----LIQEatdkMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:cd03264  142 AQALVGDPSILIVDEPTAGLDP-EERirfrnLLSE----LGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211

ABC_6TM_TAP1

cd18589

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...

29-318

9.60e-15

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.

Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 74.82 E-value: 9.60e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  29 VALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLL 108
Cdd:cd18589    1 VLGLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 109 RFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSM 188
Cdd:cd18589   81 RQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 189 NAAFVEVRHQVANLNAFVQERISGIKVLQLFAQE-------REELENFKKINEKHKQAWLKTIWYNSI---FFPIGdlcv 258
Cdd:cd18589  161 QSLAVQVQKSLARANQVAVETFSAMKTVRSFANEegeaqryRQRLQKTYRLNKKEAAAYAVSMWTSSFsglALKVG---- 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 259 sitialIVWFGGRQIIGDNVYDlGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18589  237 ------ILYYGGQLVTAGTVSS-GDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289

PLN03130

ABC transporter C family member; Provisional

359-564

1.19e-14

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 1.19e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  359 LHGISFEVKEGETIAIVGATGAGKTT-ITNLLNRFYDLTSGAIYIDGVnieeytlcslrehIATVLQDVFLFADSIYNNI 437
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSlISAMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNATVRDNI 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  438 TLKNP--AITEEEVIAAAksiGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHS- 514
Cdd:PLN03130  700 LFGSPfdPERYERAIDVT---ALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVg 776

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 496950271  515 ----EKLIQEAtdkmTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PLN03130  777 rqvfDKCIKDE----LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

354-566

1.29e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.29e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytLCSLREH---IATVLQDVFLFA 430
Cdd:PRK15439  22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR--LTPAKAHqlgIYLVPQEPLLFP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 431 D-SIYNNIT--LKNPAITEEEVIAAAKSIGVhnflmslpegyHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEAT 507
Cdd:PRK15439 100 NlSVKENILfgLPKRQASMQKMKQLLAALGC-----------QLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 508 SSVDSH-SEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG-----NHEELLQ 566
Cdd:PRK15439 169 ASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQ 234

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

352-566

1.74e-14

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.72 E-value: 1.74e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 352 YVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLT-----SGAIYIDGVNI--EEYTLCSLREHIATVLQ 424
Cdd:PRK14267  13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 425 DVFLFAD-SIYNNITL--------KNPAITEEEVIAAAKSigvhnflMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYV 495
Cdd:PRK14267  93 YPNPFPHlTIYDNVAIgvklnglvKSKKELDERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQRQRLVIARALA 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

355-520

1.95e-14

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 1.95e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCSLREHIA------------TV 422
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHylghrnamkpalTV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFADsIYNNitlknpaiTEEEVIAAAKSIGVHNfLMSLPEGYhynvkergamLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:PRK13539  91 AENLEFWAA-FLGG--------EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150

                        170
                 ....*....|....*...
gi 496950271 503 LDEATSSVDSHSEKLIQE 520
Cdd:PRK13539 151 LDEPTAALDAAAVALFAE 168

PLN03232

ABC transporter C family member; Provisional

359-564

2.52e-14

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 2.52e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  359 LHGISFEVKEGETIAIVGATGAGKTT-ITNLLNRFYDLTSGAIYIDGVnieeytlcslrehIATVLQDVFLFADSIYNNI 437
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSlISAMLGELSHAETSSVVIRGS-------------VAYVPQVSWIFNATVRENI 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  438 tLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSH-SEK 516
Cdd:PLN03232  700 -LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQ 778

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 496950271  517 LIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PLN03232  779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

343-562

2.71e-14

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 2.71e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSlREHIATV 422
Cdd:PRK13536  42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQdvflfadsiYNNITLKNPAitEEEVIAAAKSIGVHN-----FLMSLPEGYHYNVKE--RGAMLSAGQRQLIAFLRAYV 495
Cdd:PRK13536 120 PQ---------FDNLDLEFTV--RENLLVFGRYFGMSTreieaVIPSLLEFARLESKAdaRVSDLSGGMKRRLTLARALI 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDK-MTEGRTSIIIAHRLTTVKK-ADRIIVLDKG-KIVEIGNHE 562
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHA 258

livG

PRK11300

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional

361-564

2.72e-14

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.72e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 361 GISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSL-REHIATVLQDVFLFadsiynnitl 439
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLF---------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 440 KNPAITEEEVIAAAKSIGVhNFLMSLPEGYHYNVKERGAM----------------------LSAG-QRQL-IAflRAYV 495
Cdd:PRK11300  93 REMTVIENLLVAQHQQLKT-GLFSGLLKTPAFRRAESEALdraatwlervgllehanrqagnLAYGqQRRLeIA--RCMV 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241

livF

PRK11614

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

343-576

3.83e-14

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 3.83e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvaGE-EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEY-TLCSLREHIA 420
Cdd:PRK11614   6 LSFDKVSAHY--GKiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 421 TVLQDVFLFAD-SIYNNITLKNPAITEEEViaAAKSIGVHNFLMSLPEGYHynvkERGAMLSAGQRQLIAFLRAYVHKPQ 499
Cdd:PRK11614  84 IVPEGRRVFSRmTVEENLAMGGFFAERDQF--QERIKWVYELFPRLHERRI----QRAGTMSGGEQQMLAIGRALMSQPR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 500 ILILDEATSSVdshSEKLIQEATDKM----TEGRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIGNHEELLQieNGYYRN 574
Cdd:PRK11614 158 LLLLDEPSLGL---APIIIQQIFDTIeqlrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA--NEAVRS 232


                 ..
gi 496950271 575 LY 576
Cdd:PRK11614 233 AY 234

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

358-564

6.21e-14

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.96 E-value: 6.21e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLN-----RFYDLTSGAIYIDGVNIEEYTLCS-----------LREHIAT 421
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNgliksKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSM 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQ--DVFLFADSIYNNITLkNPAITEEEVIAAAKSIGVHNFLMSLPEGYhynvKERGAM-LSAGQRQLIAFLRAYVHKP 498
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMF-GPVALGVKKSEAKKLAKFYLNKMGLDDSY----LERSPFgLSGGQKRRVAIAGILAIQP 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 499 QILILDEATSSVDSHSEK-LIQEATDKMTEGRTSIIIAHRLTTV-KKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

357-546

6.60e-14

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 6.60e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCS---LREH-IATVLQDVFLFAD- 431
Cdd:PRK11629  23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDf 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 SIYNNITL------KNPAITEEEVIAAAKSIGVHNflmslpEGYHynvkeRGAMLSAGQRQLIAFLRAYVHKPQILILDE 505
Cdd:PRK11629 103 TALENVAMplligkKKPAEINSRALEMLAAVGLEH------RANH-----RPSELSGGERQRVAIARALVNNPRLVLADE 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 496950271 506 ATSSVDSHSEKLIQEATDK--MTEGRTSIIIAHRLTTVKKADR 546
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSR 214

PRK03695

vitamin B12-transporter ATPase; Provisional

362-580

6.75e-14

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 6.75e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVKEGETIAIVGATGAGKTTitnLLNRFYDLT--SGAIYIDGVNIEEYTLCSLREHIATVLQDVF-LFADSIYNNIT 438
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLLpgSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 439 LKNPAITEEEVIAAAKSIgVHNFLMsLPEGYHYNVKErgamLSAG--QRQLIA--FLRayVHK---P--QILILDEATSS 509
Cdd:PRK03695  92 LHQPDKTRTEAVASALNE-VAEALG-LDDKLGRSVNQ----LSGGewQRVRLAavVLQ--VWPdinPagQLLLLDEPMNS 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 510 VDSHSEKLIQEATDKMTE-GRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIGNHEELLQIENgyYRNLYEVQF 580
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN--LAQVFGVNF 234

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

358-557

7.23e-14

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 7.23e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNI---EEYTLCSLR-EHIATVLQDVFLFAD-S 432
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRaKHVGFVFQSFMLIPTlN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 IYNNITLknPAI--------TEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:PRK10584 105 ALENVEL--PALlrgessrqSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFAD 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 505 EATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKKADRIIVLDKGKIVE 557
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226

ABC_6TM_ATM1_ABCB7

cd18582

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...

30-298

7.86e-14

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.

Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 72.15 E-value: 7.86e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  30 ALFAVLSSIFSTAQ-PYLIKVAIDNYITPKDyeglvRIVYILIALLCAEVTMQFL---FSYYSNWL----GQTVIRDVRE 101
Cdd:cd18582    1 ALLLLVLAKLLNVAvPFLLKYAVDALSAPAS-----ALLAVPLLLLLAYGLARILsslFNELRDALfarvSQRAVRRLAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 102 KLFAHLLRFKMRYFDKSSIGVLvTRAVndmER----IGEIFSSGLFEMASDILKMFVITIVMFVI-DWKLALISYATMpl 176
Cdd:cd18582   76 RVFRHLHSLSLRFHLSRKTGAL-SRAI---ERgtrgIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTV-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 177 ILY------FTRW---FQRSMNAAFVEVRHQVAN--LNAFVqerisgIKvlqLFAQEREELENFKKINEKHKQAWLKTIW 245
Cdd:cd18582  150 ALYvaftikVTEWrtkFRREMNEADNEANAKAVDslLNYET------VK---YFNNEEYEAERYDKALAKYEKAAVKSQT 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 246 YNSIFFPIGDLCVSITIALIVWFGGRQIIGDNvYDLGNIFLFIQLSQQLFRPI 298
Cdd:cd18582  221 SLALLNIGQALIISLGLTAIMLLAAQGVVAGT-LTVGDFVLVNTYLLQLYQPL 272

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

354-511

1.51e-13

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 1.51e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDL---TSGAIYIDGVNIeeYTLCSLREHIATVLQDVFLFA 430
Cdd:COG4136   12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAEQRRIGILFQDDLLFP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 431 D-SIYNNITLKNPA-ITEEE----VIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:COG4136   90 HlSVGENLAFALPPtIGRAQrrarVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLD 158


                 ....*..
gi 496950271 505 EATSSVD 511
Cdd:COG4136  159 EPFSKLD 165

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

343-564

1.57e-13

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 1.57e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRF--YDLTSG-AIY------------------ 401
Cdd:TIGR03269   1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGrIIYhvalcekcgyverpskvg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  402 --------------IDGVNIEEYTLCSLREHIATVLQDVFlfadSIYNNITLKNPAIT--EEEVIAAAKSIGVHNFLMSL 465
Cdd:TIGR03269  80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTF----ALYGDDTVLDNVLEalEEIGYEGKEAVGRAVDLIEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  466 PEGYHyNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMT--EGRTSIIIAHRLTTVKK 543
Cdd:TIGR03269 156 VQLSH-RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIED 234

                         250       260
                  ....*....|....*....|..
gi 496950271  544 -ADRIIVLDKGKIVEIGNHEEL 564
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEV 256

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

357-556

2.23e-13

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: 70.05 E-value: 2.23e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieeytLCSLREHIATVLQDVFLFADSiyNN 436
Cdd:cd03267   35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIGVVFGQK--TQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 437 ITLKNPAITEEEVIAAAKSIGvhnflmslPEGYHYNVKERGAM-------------LSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:cd03267  106 LWWDLPVIDSFYLLAAIYDLP--------PARFKKRLDELSELldleelldtpvrqLSLGQRMRAEIAAALLHEPEILFL 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 504 DEATSSVDSHSEKLIQEATDKMTEGR--TSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:cd03267  178 DEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

320-542

2.89e-13

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: 72.86 E-value: 2.89e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  320 AILDTETDTETGGEKELKEVKGNIKFED--VRFEYV-----AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRF 392
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQDngIKFENIplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  393 YDLTSGAIYIDGVNIEEY-------TLCSLREHIatvlqdvfLFADSIYNnitLKNPAITEEEVIAAAKSIGVHNFLMSl 465
Cdd:TIGR00954 502 WPVYGGRLTKPAKGKLFYvpqrpymTLGTLRDQI--------IYPDSSED---MKRRGLSDKDLEQILDNVQLTHILER- 569

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271  466 pEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMteGRTSIIIAHRLTTVK 542
Cdd:TIGR00954 570 -EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643

PRK10261

glutathione transporter ATP-binding protein; Provisional

323-559

3.87e-13

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 3.87e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 323 DTETDTETGGEKELK--------EVKGNIkFEDVRFEYVAGEEIlhgiSFEVKEGETIAIVGATGAGKTTITNLLNRFYD 394
Cdd:PRK10261 301 PIEQDTVVDGEPILQvrnlvtrfPLRSGL-LNRVTREVHAVEKV----SFDLWPGETLSLVGESGSGKSTTGRALLRLVE 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 395 LTSGAIYIDGVNIE---EYTLCSLREHIATVLQDVFLFAD-------SIYNNITLKNPAITEEeviAAAKSIGVHNFLMS 464
Cdd:PRK10261 376 SQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDPYASLDprqtvgdSIMEPLRVHGLLPGKA---AAARVAWLLERVGL 452

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 465 LPE-GYHYNVKergamLSAGQRQLIAFLRAYVHKPQILILDEATSSVD-SHSEKLIQEATDKMTE-GRTSIIIAHRLTTV 541
Cdd:PRK10261 453 LPEhAWRYPHE-----FSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLLDLQRDfGIAYLFISHDMAVV 527

                        250
                 ....*....|....*....
gi 496950271 542 KK-ADRIIVLDKGKIVEIG 559
Cdd:PRK10261 528 ERiSHRVAVMYLGQIVEIG 546

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

361-564

4.21e-13

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 4.21e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 361 GISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG---VNIEEYTLCSLREHIATVLQDVFLfadSIynni 437
Cdd:PRK15079  39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDPLA---SL---- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 438 tlkNPAITEEEVIAaaKSIGVHNFLMSLPEgyhynVKER-GAML-----------------SAGQRQLIAFLRAYVHKPQ 499
Cdd:PRK15079 112 ---NPRMTIGEIIA--EPLRTYHPKLSRQE-----VKDRvKAMMlkvgllpnlinryphefSGGQCQRIGIARALILEPK 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 500 ILILDEATSSVD----SHSEKLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK15079 182 LIICDEPVSALDvsiqAQVVNLLQQLQREM--GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249

PRK10261

glutathione transporter ATP-binding protein; Provisional

342-566

4.85e-13

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 4.85e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 342 NIKFEDVRFEYVAgeeiLHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG----------VNIEEYT 411
Cdd:PRK10261  19 NIAFMQEQQKIAA----VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 412 LCSLRE----HIATVLQD-------VFLFADSIYNNITLKNPAITEEEVIAAAKSIGvhnfLMSLPEGyHYNVKERGAML 480
Cdd:PRK10261  95 AAQMRHvrgaDMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMLD----QVRIPEA-QTILSRYPHQL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 481 SAGQRQLIAFLRAYVHKPQILILDEATSSVD----SHSEKLIQEATDKMTEGrtSIIIAHRLTTVKK-ADRIIVLDKGKI 555
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGEA 247

                        250
                 ....*....|.
gi 496950271 556 VEIGNHEELLQ 566
Cdd:PRK10261 248 VETGSVEQIFH 258

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

343-566

4.89e-13

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 4.89e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEyvAGEEILHGISFEVKEGETIAIVGATGAGKT-TITNLLnrfyDL-------TSGAIYIDGvniEEYTLCS 414
Cdd:PRK10418   5 IELRNIALQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GIlpagvrqTAGRVLLDG---KPVAPCA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 415 LR-EHIATVLQDvflfADSIYNNI-TLKNPAI----------TEEEVIAAAKSIGV---------HNFLMSlpegyhynv 473
Cdd:PRK10418  76 LRgRKIATIMQN----PRSAFNPLhTMHTHARetclalgkpaDDATLTAALEAVGLenaarvlklYPFEMS--------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 474 kerGAMLsagQRQLIAFlrAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEGRTS--IIIAHRLTTVKK-ADRIIVL 550
Cdd:PRK10418 143 ---GGML---QRMMIAL--ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVM 214

                        250
                 ....*....|....*.
gi 496950271 551 DKGKIVEIGNHEELLQ 566
Cdd:PRK10418 215 SHGRIVEQGDVETLFN 230

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

358-576

5.50e-13

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: 68.72 E-value: 5.50e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCS-LREHIATVLQDVflfadSIYNN 436
Cdd:cd03218   15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEA-----SIFRK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 437 ITLknpaitEEEVIAAAKSIGV-----HNFLMSLPEGYH--YNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSS 509
Cdd:cd03218   90 LTV------EENILAVLEIRGLskkerEEKLEELLEEFHitHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 510 VDSHSEKLIQEATDKMTEGRTSIIIA-HRL-TTVKKADRIIVLDKGKIVEIGNHEELlqIENGYYRNLY 576
Cdd:cd03218  164 VDPIAVQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEI--AANELVRKVY 230

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

357-564

8.94e-13

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 8.94e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIeeyTLCSLRE-HIATVLQDVFLFAD-SIY 434
Cdd:PRK10851  16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDrKVGFVFQHYALFRHmTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 435 NNITL----------KNPAITEEEVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:PRK10851  93 DNIAFgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLD 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 505 EATSSVDSHSEKLIQEATDKMTE--GRTSIIIAH-RLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224

ABC_6TM_PrtD_LapB_HlyB_like

cd18783

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

23-302

9.27e-13

Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 69.08 E-value: 9.27e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVirDVR-- 100
Cdd:cd18783    1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRI--DARla 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 101 EKLFAHLLRFKMRYFDKSSIGVLvTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALI----SYATMPL 176
Cdd:cd18783   79 LRTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVvlafSALIALI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 177 ILYFTRWFQRSMNAAFV-EVRHQvanlnAFVQERISGI---KVLQLFAQEREELEN--FKKINEKHKQAWLkTIWYNSIF 250
Cdd:cd18783  158 ILAFLPPFRRRLQALYRaEGERQ-----AFLVETVHGIrtvKSLALEPRQRREWDErvARAIRARFAVGRL-SNWPQTLT 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496950271 251 FPIGDLcvsITIAlIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIA 302
Cdd:cd18783  232 GPLEKL---MTVG-VIWVGAYLVF-AGSLTVGALIAFNMLAGRVAGPLVQLA 278

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

362-564

1.03e-12

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 1.03e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytLCSLREHIATVLQDVFLFAD-SIYNNIT-- 438
Cdd:PRK11000  22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVFQSYALYPHlSVAENMSfg 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 439 LKNPAITEEE----VIAAAKSIGVHNFLMSLPEGyhynvkergamLSAGQRQLIAFLRAYVHKPQILILDEATSSVDS-- 512
Cdd:PRK11000 100 LKLAGAKKEEinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAal 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496950271 513 HSEKLIQEATDKMTEGRTSIIIAH-RLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

368-555

1.05e-12

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.58 E-value: 1.05e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   368 EGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEyTLCSLREHIATVLQDVFLF-----ADSIYNNITLKNP 442
Cdd:TIGR01257  955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFhhltvAEHILFYAQLKGR 1033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   443 AITEEEVIAAAksigvhnflMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEAT 522
Cdd:TIGR01257 1034 SWEEAQLEMEA---------MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104

                          170       180       190
                   ....*....|....*....|....*....|....
gi 496950271   523 DKMTEGRTSIIIAHRLTTVK-KADRIIVLDKGKI 555
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138

3a01204

TIGR00955

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...

357-566

1.16e-12

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 1.16e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  357 EILHGISFEVKEGETIAIVGATGAGKTTITNLLNrFYDLT----SGAIYIDGVNIEeytLCSLREHIATVLQDVFLFads 432
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFI--- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  433 iynnitlknPAITEEE-------------VIAAAKSIGVHNFL--MSLPEGYHYNVKERGAM--LSAGQRQLIAFLRAYV 495
Cdd:TIGR00955 112 ---------PTLTVREhlmfqahlrmprrVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELL 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271  496 HKPQILILDEATSSVDSHS-EKLIQEATDKMTEGRTSIIIAHRLTT--VKKADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256

cbiO

PRK13645

energy-coupling factor transporter ATPase;

350-568

1.26e-12

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 1.26e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 350 FEYVAgeeiLHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAI----YIDGVNIEEYT-LCSLREHIATVLQ 424
Cdd:PRK13645  22 FEFKA----LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKeVKRLRKEIGLVFQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 425 --DVFLFADSIYNNITLkNPAITEEEVIAAAKSIGVHNFLMSLPEGYhynVKERGAMLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:PRK13645  98 fpEYQLFQETIEKDIAF-GPVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLV 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 503 LDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTV-KKADRIIVLDKGKIVEIG-------NHEELLQIE 568
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifsNQELLTKIE 249

COG4586

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

359-566

1.29e-12

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 1.29e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTT----ITNLLNRfydlTSGAIYIDGVNI----EEYtlcslREHIATV-------- 422
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILVP----TSGEVRVLGYVPfkrrKEF-----ARRIGVVfgqrsqlw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 ----LQDVFLFADSIYNnitlknpaITEEEviaAAKSIGVHNFLMSLPEGYHYNVKErgamLSAGQR---QLIAflrAYV 495
Cdd:COG4586  109 wdlpAIDSFRLLKAIYR--------IPDAE---YKKRLDELVELLDLGELLDTPVRQ----LSLGQRmrcELAA---ALL 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIiahrLTT-----VKK-ADRIIVLDKGKIVEIGNHEELLQ 566
Cdd:COG4586  171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTIL----LTShdmddIEAlCDRVIVIDHGRIIYDGSLEELKE 244

GguA

NF040905

sugar ABC transporter ATP-binding protein;

359-557

2.02e-12

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 2.02e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTS--GAIYIDGvniEEYTLCSLR--EH--IATVLQDVFLFAD- 431
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRdsEAlgIVIIHQELALIPYl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 SIYNNITLKNP-----AITEEEVIAAAKSigvhnfLMS---LPEGYHYNVKERGAmlsaGQRQLIAFLRAYVHKPQILIL 503
Cdd:NF040905  94 SIAENIFLGNErakrgVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 504 DEATSSV-DSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:NF040905 164 DEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

359-555

2.17e-12

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: 65.92 E-value: 2.17e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREH-IATVLQDVF---LFAD-SI 433
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITLknpaiteeeviaaaksigvhnflmslpegyhynvkerGAMLSAG--QRQLIAflRAYVHKPQILILDEATSSVD 511
Cdd:cd03215   96 AENIAL-------------------------------------SSLLSGGnqQKVVLA--RWLARDPRVLILDEPTRGVD 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 496950271 512 SHSEKLIQEATDKMTEGRTSIIIahrLTT-----VKKADRIIVLDKGKI 555
Cdd:cd03215  137 VGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

347-565

3.46e-12

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 3.46e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 347 DVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDG--VNIEEYTLCSLREHIATVLQ 424
Cdd:PRK13638   6 DLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 425 D--VFLFADSIYNNI--TLKNPAITEEEViaaAKSIgvhNFLMSLPEGYHYNvKERGAMLSAGQRQLIAFLRAYVHKPQI 500
Cdd:PRK13638  85 DpeQQIFYTDIDSDIafSLRNLGVPEAEI---TRRV---DEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARY 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 501 LILDEATSSVDSHSE-KLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELL 565
Cdd:PRK13638 158 LLLDEPTAGLDPAGRtQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224

ycf16

CHL00131

sulfate ABC transporter protein; Validated

357-571

4.16e-12

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 4.16e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTITNLL--NRFYDLTSGAIYIDGVNIEEYTlCSLREH------------IATV 422
Cdd:CHL00131  21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLE-PEERAHlgiflafqypieIPGV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLFAdsIYNNiTLKNPAITEEEVIAAAKSIGVHNFLMSLPEGY-HYNVKERgamLSAGQRQLIAFLRAYVHKPQIL 501
Cdd:CHL00131 100 SNADFLRL--AYNS-KRKFQGLPELDPLEFLEIINEKLKLVGMDPSFlSRNVNEG---FSGGEKKRNEILQMALLDSELA 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 502 ILDEATSSVDSHSEKLIQEATDK-MTEGRTSIIIAH--RLTTVKKADRIIVLDKGKIVEIGNHEELLQIE-NGY 571
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEkKGY 247

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

346-555

5.91e-12

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 5.91e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 346 EDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVnieeyTLCSLREHIATVLQD 425
Cdd:PRK11247  16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 VFLFA-DSIYNNITLKNPAITEEEVIAAAKSIGVHNflmslpegyhyNVKERGAMLSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:PRK11247  90 ARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLLD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 505 EATSSVDSHS--------EKLIQEatdkmtEGRTSIIIAHRLT-TVKKADRIIVLDKGKI 555
Cdd:PRK11247 159 EPLGALDALTriemqdliESLWQQ------HGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

355-564

6.62e-12

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: 66.42 E-value: 6.62e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieEYTLCSlrehiatvlQDVFLFADSIY 434
Cdd:cd03291   49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----RISFSS---------QFSWIMPGTIK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 435 NNItLKNPAITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHS 514
Cdd:cd03291  116 ENI-IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 515 EKLIQEA-TDKMTEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:cd03291  195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245

ABC_6TM_ABCC_D2

cd18580

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...

26-318

8.51e-12

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.

Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 66.37 E-value: 8.51e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA 105
Cdd:cd18580    1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALIsyatMPLILYFTRWFQ 185
Cdd:cd18580   81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 186 RSMNAAFVEVRHQVAN----LNAFVQERISGIKVLQLF-AQEREELENFKKINEKHK--------QAWLkTIWYnsiffp 252
Cdd:cd18580  157 RYYLRTSRQLRRLESEsrspLYSHFSETLSGLSTIRAFgWQERFIEENLRLLDASQRafylllavQRWL-GLRL------ 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 253 igDLCVSITIALIVWFGgrqIIGDNVYDLGNIFL----FIQLSQQLFRPIRHIADkfntLQMGIIASDRV 318
Cdd:cd18580  230 --DLLGALLALVVALLA---VLLRSSISAGLVGLaltyALSLTGSLQWLVRQWTE----LETSMVSVERI 290

PRK13549

xylose transporter ATP-binding subunit; Provisional

359-554

1.39e-11

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.39e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTS--GAIYIDGVNIEEYTLC-SLREHIATVLQDVFLFAD-SIY 434
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 435 NNITLKNpAITEEEVIA-AAKSIGVHNFLMSLpeGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSV-DS 512
Cdd:PRK13549 101 ENIFLGN-EITPGGIMDyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtES 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 496950271 513 HSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGK 554
Cdd:PRK13549 178 ETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

347-545

1.95e-11

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 1.95e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 347 DVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEyTLCSLREHIATVLQdv 426
Cdd:PRK13540   6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 flfADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPegyHYnVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEA 506
Cdd:PRK13540  82 ---RSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLE---HL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 496950271 507 TSSVDSHS-EKLIQEATDKMTEGRTSIIIAHRLTTVKKAD 545
Cdd:PRK13540 155 LVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194

PRK14243

phosphate transporter ATP-binding protein; Provisional

359-538

1.95e-11

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 1.95e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGA-----IYIDGVNI--EEYTLCSLREHIATVLQDVFLFAD 431
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 SIYNNITLkNPAIT------EEEVIAAAKSigvhnflMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDE 505
Cdd:PRK14243 106 SIYDNIAY-GARINgykgdmDELVERSLRQ-------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177

                        170       180       190
                 ....*....|....*....|....*....|...
gi 496950271 506 ATSSVDSHSEKLIQEATDKMTEGRTSIIIAHRL 538
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

358-568

2.08e-11

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 2.08e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIYNNI 437
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 438 TLK-----NPAIT------EEEVIAAAKSIGVHNFlmslpegyhynVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEA 506
Cdd:PRK10253 102 VARgryphQPLFTrwrkedEEAVTKAMQATGITHL-----------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 507 TSSVD-SHSEKLIQEATD-KMTEGRTSIIIAHRLT-TVKKADRIIVLDKGKIVEIGNHEELLQIE 568
Cdd:PRK10253 171 TTWLDiSHQIDLLELLSElNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

22-564

3.86e-11

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.47 E-value: 3.86e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271    22 YRGVFIAVALFavLSSIFSTAQPYLIKVAIDNYITPKDYEGlvRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVRE 101
Cdd:TIGR01271   80 WRFVFYGILLY--FGEATKAVQPLLLGRIIASYDPFNAPER--EIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRI 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   102 KLFA----HLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMasdILKMFVITIVMFVidWKL----ALISYAT 173
Cdd:TIGR01271  156 ALFSliykKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVW---IAPLQVILLMGLI--WELlevnGFCGLGF 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   174 MPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEreelENFKKINEKHKQAWLKTI--------W 245
Cdd:TIGR01271  231 LILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDELKLTrkiaylryF 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   246 YNSIFFPIGDLCVSITI---ALIVWFGGRQIIGDNVYdlgNIFLFIQLSQQL----------FRPIRHIAD-----KFNT 307
Cdd:TIGR01271  307 YSSAFFFSGFFVVFLSVvpyALIKGIILRRIFTTISY---CIVLRMTVTRQFpgaiqtwydsLGAITKIQDflckeEYKT 383

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   308 LQMGIIASDRVFAILDTETDTETG--------GEKELKEVKGNIKFEDVRFEyVAGEEILHGISFEVKEGETIAIVGATG 379
Cdd:TIGR01271  384 LEYNLTTTEVEMVNVTASWDEGIGelfekikqNNKARKQPNGDDGLFFSNFS-LYVTPVLKNISFKLEKGQLLAVAGSTG 462

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   380 AGKTTITNLLNRFYDLTSGAIYIDGvnieeytlcslreHIATVLQDVFLFADSIYNNItLKNPAITEEEVIAAAKSIGVH 459
Cdd:TIGR01271  463 SGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI-IFGLSYDEYRYTSVIKACQLE 528

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   460 NFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEA-TDKMTEGRTSIIIAHRL 538
Cdd:TIGR01271  529 EDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKL 608

                          570       580
                   ....*....|....*....|....*.
gi 496950271   539 TTVKKADRIIVLDKGKIVEIGNHEEL 564
Cdd:TIGR01271  609 EHLKKADKILLLHEGVCYFYGTFSEL 634

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

359-557

4.50e-11

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 4.50e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCSLREH----IATVLQDVFLFAD-SI 433
Cdd:PRK11288  20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAAlaagVAIIYQELHLVPEmTV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITL-----KNPAITEEEVIAAA----KSIGVhNFLMSLPEGYhynvkergamLSAGQRQLIAFLRAYVHKPQILILD 504
Cdd:PRK11288  97 AENLYLgqlphKGGIVNRRLLNYEAreqlEHLGV-DIDPDTPLKY----------LSIGQRQMVEIAKALARNARVIAFD 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 505 EATSSVdSHSE-----KLIQEATDkmtEGRTSIIIAHRLTTV-KKADRIIVLDKGKIVE 557
Cdd:PRK11288 166 EPTSSL-SAREieqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220

PRK15056

manganese/iron ABC transporter ATP-binding protein;

343-569

5.08e-11

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 5.08e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytlcSLREH-IAT 421
Cdd:PRK15056   7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQ-------------DVFLFADsiYNNIT-LKNPAITEEEVIAAAKSigvhnfLMSLPEGYHYNVKErgamLSAGQRQL 487
Cdd:PRK15056  83 VPQseevdwsfpvlveDVVMMGR--YGHMGwLRRAKKRDRQIVTAALA------RVDMVEFRHRQIGE----LSGGQKKR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 488 IAFLRAYVHKPQILILDEATSSVDSHSE----KLIQEATDkmtEGRTSIIIAHRLTTVKKADRIIVLDKGKIVEIGNHEE 563
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEariiSLLRELRD---EGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227


                 ....*.
gi 496950271 564 LLQIEN 569
Cdd:PRK15056 228 TFTAEN 233

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

336-556

8.53e-11

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 8.53e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  336 LKEVKGNIK-FEDVRfeyvageeILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTS--GAIYIDGvniEEYTL 412
Cdd:TIGR02633   1 LLEMKGIVKtFGGVK--------ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSG---SPLKA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  413 CSLREH----IATVLQDVFLFAD-SIYNNITLKNpAITEEEVIA--AAKSIGVHNFL--MSLPEgyhYNVKERGAMLSAG 483
Cdd:TIGR02633  70 SNIRDTeragIVIIHQELTLVPElSVAENIFLGN-EITLPGGRMayNAMYLRAKNLLreLQLDA---DNVTRPVGDYGGG 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271  484 QRQLIAFLRAYVHKPQILILDEATSSV-DSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

345-555

1.04e-10

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 1.04e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 345 FEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieeytlcslREHIATVLQ 424
Cdd:COG0488    1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 425 DVFLFAD-SIYNNI----------------TLKNPAITEEEVIAAAKsigVHNFLMSLpEGYHYNVKERGAM-------- 479
Cdd:COG0488   69 EPPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAE---LQEEFEAL-GGWEAEARAEEILsglgfpee 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 480 --------LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHS----EKLIQEatdkmTEGrTSIIIAH-R--LTTVkkA 544
Cdd:COG0488  145 dldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN-----YPG-TVLVVSHdRyfLDRV--A 216

                        250
                 ....*....|.
gi 496950271 545 DRIIVLDKGKI 555
Cdd:COG0488  217 TRILELDRGKL 227

ABC_6TM_Pgp_ABCB1

cd18558

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...

61-288

1.18e-10

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.

Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 63.06 E-value: 1.18e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  61 EGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSS 140
Cdd:cd18558   56 EEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 141 GLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFA 220
Cdd:cd18558  136 KIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFG 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 221 QEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDLCVSITIALIVWFGGRQIIgDNVYDLGNIFLFI 288
Cdd:cd18558  216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVT-QQEYSIGEVLTVF 282

MglA

COG1129

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];

359-564

1.51e-10

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 1.51e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvniEEYTLCS----LREHIATVLQD-----VFLf 429
Cdd:COG1129  268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSprdaIRAGIAYVPEDrkgegLVL- 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 430 ADSIYNNITL-------KNPAITEEEVIAAAKSIgVHNFlmslpegyhyNVKERGAM-----LSAG--QRQLIAflRAYV 495
Cdd:COG1129  344 DLSIRENITLasldrlsRGGLLDRRRERALAEEY-IKRL----------RIKTPSPEqpvgnLSGGnqQKVVLA--KWLA 410

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 496 HKPQILILDEATSSVD--SHSE--KLIQEATDkmtEGRTSIII------AHRLttvkkADRIIVLDKGKIVEIGNHEEL 564
Cdd:COG1129  411 TDPKVLILDEPTRGIDvgAKAEiyRLIRELAA---EGKAVIVIsselpeLLGL-----SDRILVMREGRIVGELDREEA 481

fecE

PRK11231

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;

358-568

2.27e-10

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 2.27e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQdvflfadsiynnI 437
Cdd:PRK11231  17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ------------H 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 438 TLKNPAITEEEVIAAAKSIGVhNFLMSLPEGYHYNVKErgAM---------------LSAGQRQLiAFLrAYV--HKPQI 500
Cdd:PRK11231  85 HLTPEGITVRELVAYGRSPWL-SLWGRLSAEDNARVNQ--AMeqtrinhladrrltdLSGGQRQR-AFL-AMVlaQDTPV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 501 LILDEATSSVD-SHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQIE 568
Cdd:PRK11231 160 VLLDEPTTYLDiNHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

353-579

3.57e-10

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 3.57e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 353 VAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLL--NRFYDLTSGAIYIDGVNIEEY-------------------- 410
Cdd:PRK09580  11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELspedragegifmafqypvei 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 411 -----------TLCSLREHIATVLQDVFLFADSIYNNITLKNpaiTEEEVIAAAKSIGvhnflmslpegyhynvkergam 479
Cdd:PRK09580  91 pgvsnqfflqtALNAVRSYRGQEPLDRFDFQDLMEEKIALLK---MPEDLLTRSVNVG---------------------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTEG-RTSIIIAH--RLTTVKKADRIIVLDKGKIV 556
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIV 225

                        250       260
                 ....*....|....*....|...
gi 496950271 557 EIGNHEELLQIENGYYRNLYEVQ 579
Cdd:PRK09580 226 KSGDFTLVKQLEEQGYGWLTEQQ 248

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

343-570

4.65e-10

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.97 E-value: 4.65e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvaGEE-ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSlREHIAT 421
Cdd:PRK13537   8 IDFRNVEKRY--GDKlVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVFLFAD-SIYNNITLKNPAITEEEVIAAAKSIGVHNFlMSLPEGYHYNVKErgamLSAGQRQLIAFLRAYVHKPQI 500
Cdd:PRK13537  85 VPQFDNLDPDfTVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDPDV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 501 LILDEATSSVDSHSEKLIQEATDK-MTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQIENG 570
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESEIG 231

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

354-550

5.94e-10

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.78 E-value: 5.94e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieEYTLCSLREHIA-------TVLQDV 426
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEvpdslplTVRDLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FL--FAD-SIYNNITLKNPAIteeeVIAAAKSIGVHNFLmslpegyhynvKERGAMLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:NF040873  79 AMgrWARrGLWRRLTRDDRAA----VDDALERVGLADLA-----------GRQLGELSGGQRQRALLAQGLAQEADLLLL 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 504 DEATSSVDSHSE----KLIQEATDkmtEGRTSIIIAHRLTTVKKADRIIVL 550
Cdd:NF040873 144 DEPTTGLDAESReriiALLAEEHA---RGATVVVVTHDLELVRRADPCVLL 191

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

343-553

6.36e-10

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 6.36e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFeYVAGE----EILHGISFEVKEGETIAIVGATGAGKTTITNLL-NRFYD-LTSGAIYIDGVNIEEytlcSLR 416
Cdd:cd03232    4 LTWKNLNY-TVPVKggkrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDK----NFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 417 EHIATVLQ-DVFlfadsiynnitlkNPAITEEEVIaaaksigvhnflmslpegyHYNVKERGamLSAGQRQLIAFLRAYV 495
Cdd:cd03232   79 RSTGYVEQqDVH-------------SPNLTVREAL-------------------RFSALLRG--LSVEQRKRLTIGVELA 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 496 HKPQILILDEATSSVDSHSEKLIQEATDKMTE-GRTSIIIAHR--LTTVKKADRIIVLDKG 553
Cdd:cd03232  125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADsGQAILCTIHQpsASIFEKFDRLLLLKRG 185

ABC_6TM_ABCC_D1

cd18579

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...

29-318

1.07e-09

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.

Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 59.81 E-value: 1.07e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  29 VALFAVLSSIFSTAQPYLIKVAIdNYITPKDYEGLVRIvYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVR----EKLF 104
Cdd:cd18579    2 AGLLKLLEDLLSLAQPLLLGLLI-SYLSSYPDEPLSEG-YLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRsalsSLIY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 105 AHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSgLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWF 184
Cdd:cd18579   80 RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 185 QRSMNAAFvevrhqvANLNAFVQER-------ISGIKVLQLFAqereeLENF--KKINEKHKQ--AWLKTIWY-----NS 248
Cdd:cd18579  159 AKLISKLR-------KKLMKATDERvkltneiLSGIKVIKLYA-----WEKPflKRIEELRKKelKALRKFGYlralnSF 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 249 IFFPIGDLCVSITIALIVWFGgrqiigdNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18579  227 LFFSTPVLVSLATFATYVLLG-------NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289

ABC_6TM_ABCB9_like

cd18784

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...

31-318

1.20e-09

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.

Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 59.63 E-value: 1.20e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFStaqPYLIKVAIDNYITPKDYEGLVRIVYILIAL-----LCAEVTMQfLFSYysnwlgqTVIR---DVREK 102
Cdd:cd18784    6 LAAAVGEIFI---PYYTGQVIDGIVIEKSQDKFSRAIIIMGLLaiassVAAGIRGG-LFTL-------AMARlniRIRNL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 103 LFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTR 182
Cdd:cd18784   75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 183 WFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINE-----KHKQAWLKT--IWYNSIFFpigd 255
Cdd:cd18784  155 VYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKdtyklKIKEALAYGgyVWSNELTE---- 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 256 lcvSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18784  231 ---LALTVSTLYYGGHLVI-TGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

359-556

1.29e-09

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.29e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT-LCSLREHIATVLQDVflfadSIYNNI 437
Cdd:PRK09700  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQEL-----SVIDEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 438 T-LKNPAITEEEV-------IAAAKSIGVHNFLMSLPEGYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSS 509
Cdd:PRK09700  96 TvLENLYIGRHLTkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 496950271 510 V-DSHSEKLIQEATDKMTEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:PRK09700 176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

358-561

1.35e-09

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.35e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQdvflFADSIynni 437
Cdd:COG2401   45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD----FKDAV---- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 438 tlknpaiteeEVIAAAKSIGVHNFLMSLPEgyhynvkergamLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKL 517
Cdd:COG2401  117 ----------ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 518 ----IQEATDKMteGRTSIIIAHRlTTVKKA---DRIIVLDKGKIVEIGNH 561
Cdd:COG2401  175 varnLQKLARRA--GITLVVATHH-YDVIDDlqpDLLIFVGYGGVPEEKRR 222

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

355-535

1.44e-09

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: 57.89 E-value: 1.44e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQDVFLFADSIY 434
Cdd:cd03231   12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 435 NNITLKNPAITEEEVIAAAKSIGVHNFlMSLPEGYhynvkergamLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHS 514
Cdd:cd03231   92 ENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160

                        170       180
                 ....*....|....*....|.
gi 496950271 515 EKLIQEATDKMTEGRTSIIIA 535
Cdd:cd03231  161 VARFAEAMAGHCARGGMVVLT 181

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

362-555

1.51e-09

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.51e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  362 ISFEVKEGETIAIVGATGAGKT-TITNLLNRFYDLTSGAIYIDG--VNIEEyTLCSLREHIATVLQD------------- 425
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIRN-PAQAIRAGIAMVPEDrkrhgivpilgvg 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  426 --VFLFADSIYNNITLKNPAITEEEVIAAAKSIGVHNFLMSLPEGyhynvkergaMLSAGQRQLIAFLRAYVHKPQILIL 503
Cdd:TIGR02633 358 knITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 496950271  504 DEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTV-KKADRIIVLDKGKI 555
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVlGLSDRVLVIGEGKL 481

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

355-568

1.69e-09

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 1.69e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTL-CSLREHIATVLQDVFLFAD-S 432
Cdd:PRK10895  15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 IYNNITlknpAITE-EEVIAAAKSIGVHNFLMslpEGYHYN--VKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSS 509
Cdd:PRK10895  95 VYDNLM----AVLQiRDDLSAEQREDRANELM---EEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 510 VDSHS----EKLIQEATDKmteGRTSIIIAHRL-TTVKKADRIIVLDKGKIVEIGNHEELLQIE 568
Cdd:PRK10895 168 VDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

343-566

2.37e-09

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 2.37e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIdGVNIEeytlcslrehIATV 422
Cdd:COG0488  316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQDVFLF--ADSIYNNITLKNPAITEEEVIA-----------AAKSIGVhnflmslpegyhynvkergamLSAGQRQLIA 489
Cdd:COG0488  384 DQHQEELdpDKTVLDELRDGAPGGTEQEVRGylgrflfsgddAFKPVGV---------------------LSGGEKARLA 442

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 490 FLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMtEGrTSIIIAH-R--LTTVkkADRIIVLDKGKIVE-IGNHEELL 565
Cdd:COG0488  443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDDYL 518


                 .
gi 496950271 566 Q 566
Cdd:COG0488  519 E 519

ABC_6TM_ATM1_ABCB7_HMT1_ABCB6

cd18560

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...

31-313

2.73e-09

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.

Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 58.39 E-value: 2.73e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFSTAQPYLIKVAIDNYITPKdyEGLVRIVYILIALLCAEVTMQFLFSYYSNWL----GQTVIRDVREKLFAH 106
Cdd:cd18560    3 LLLILGKACNVLAPLFLGRAVNALTLAK--VKDLESAVTLILLYALLRFSSKLLKELRSLLyrrvQQNAYRELSLKTFAH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 107 LLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIV-MFVIDWKLALISYATMPLILYFTRW-- 183
Cdd:cd18560   81 LHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGAWLALIVFLSVLLYGVFTIKvt 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 184 -----FQRSMNAAFVEVrHQVAN--LNAFvqerisgiKVLQLFAQEREELENFKKINEKHKQAWLKTIWYNSIFFPIGDL 256
Cdd:cd18560  161 ewrtkFRRAANKKDNEA-HDIAVdsLLNF--------ETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQL 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 257 CVSITIALIVWFGGRQIIgDNVYDLGNIFLFIQLSQQLFRPIRHIADKFNTLQMGII 313
Cdd:cd18560  232 IIQLGLTLGLLLAGYRVV-DGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLT 287

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

369-552

3.29e-09

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 3.29e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   369 GETIAIVGATGAGKTTITNLLNRFYDLTS-GAIYIDGVNIEEYTLCSLREHIatvlqdvflfadsiynnitlknpaitee 447
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII---------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271   448 eviaaaksigvhnflmslpegyhynVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATD---- 523
Cdd:smart00382  54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108

                          170       180       190
                   ....*....|....*....|....*....|..
gi 496950271   524 ---KMTEGRTSIIIAHRLTTVKKADRIIVLDK 552
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRFDR 140

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

354-557

6.80e-09

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.02 E-value: 6.80e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEeytlcSLREHIATVLQDVFLFA--- 430
Cdd:PRK11248  12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-----GPGAERGVVFQNEGLLPwrn 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 431 --DSIYNNITLKNPAITEEEVIAAA--KSIGVhnflmslpEGYHynvKERGAMLSAGQRQLIAFLRAYVHKPQILILDEA 506
Cdd:PRK11248  87 vqDNVAFGLQLAGVEKMQRLEIAHQmlKKVGL--------EGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 507 TSSVDSHSEKLIQEATDKM--TEGRTSIIIAHRL-TTVKKADRIIVL--DKGKIVE 557
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwqETGKQVLLITHDIeEAVFMATELVLLspGPGRVVE 211

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

357-557

8.51e-09

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 8.51e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKT----TITNLLNrfydlTSGAIYIDG---------VNIEEYTLCSLR-EHIATV 422
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP-----SPPVVYPSGdirfhgeslLHASEQTLRGVRgNKIAMI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQD--VFL-----FADSIYNNITL-----KNPAITEeeVIAAAKSIGVHNFLMSLPEGYHynvkergaMLSAGQRQLIAF 490
Cdd:PRK15134  98 FQEpmVSLnplhtLEKQLYEVLSLhrgmrREAARGE--ILNCLDRVGIRQAAKRLTDYPH--------QLSGGERQRVMI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 491 LRAYVHKPQILILDEATSSVDSHSE----KLIQEATDKMTEGRtsIIIAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGL--LFITHNLSIVRKlADRVAVMQNGRCVE 237

ABC_6TM_TAP2

cd18590

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...

99-288

1.21e-08

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.

Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 56.58 E-value: 1.21e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  99 VREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLI- 177
Cdd:cd18590   71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTa 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 178 ----LYFTRwfqrsmNAAFV-EVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKK-INEKHKQAWLKTIWYnSIFF 251
Cdd:cd18590  151 iaqkVYNTY------HQKLSqAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEaLERTYNLKDRRDTVR-AVYL 223

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 496950271 252 PIGDLcVSITIALIVWFGGRQIIGDNVYDLGNIFLFI 288
Cdd:cd18590  224 LVRRV-LQLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259

ABC_6TM_LapB_like

cd18587

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...

20-223

1.24e-08

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: 56.68 E-value: 1.24e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  20 KPYRGVFIA---VALFAVLSSIFsTAQPYlikvaiDNYITPKDYEGL-VRIVYILIALlCAEVTMQFLFSYYSNWLGQTV 95
Cdd:cd18587    2 RIYRDVLLAallINLFALASPLF-VMNVY------DRVVPNNAIETLwVLAIGVLIAL-LFDFILKLLRAYFIDVAGKRA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  96 irDVR--EKLFAHLLRFKMRYfDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYAT 173
Cdd:cd18587   74 --DVIlsSRLFERVLGLRLEA-RPASVGSFANN-LREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVA 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 496950271 174 MPLILYFTRWFQRSMNAAFVEVRHQVANLNAFVQERISGIKVLQLFAQER 223
Cdd:cd18587  150 IPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEG 199

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

362-564

1.44e-08

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.44e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVKEGETIAIVGATGAGKT----TITNLLNRfYDLTSGAIYIDG---VNIEEYTLCSLR-EHIATVLQDvflfadsi 433
Cdd:PRK09473  35 LNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGreiLNLPEKELNKLRaEQISMIFQD-------- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 ynNITLKNP--AITEE--EVIAAAKSIGVHN-FLMS--------LPEGyhynvKERGAM----LSAGQRQLIAFLRAYVH 496
Cdd:PRK09473 106 --PMTSLNPymRVGEQlmEVLMLHKGMSKAEaFEESvrmldavkMPEA-----RKRMKMypheFSGGMRQRVMIAMALLC 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496950271 497 KPQILILDEATSSVDSHSEKLIQEATDKMT-EGRTSII-IAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

358-545

2.78e-08

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 2.78e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLN----RFY--DLT-------SGAiyidgvnieeyTLCSLREHIATV-- 422
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYsnDLTlfgrrrgSGE-----------TIWDIKKHIGYVss 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 -----------LQDVFL--FADSI--YNNITLKNPAITEE--EVIAAAKSIGVHNFlmslpegyHynvkergaMLSAGQR 485
Cdd:PRK10938 344 slhldyrvstsVRNVILsgFFDSIgiYQAVSDRQQKLAQQwlDILGIDKRTADAPF--------H--------SLSWGQQ 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 486 QLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKM-TEGRTSII------------IAHRLTTVKKAD 545
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLfvshhaedapacITHRLEFVPDGD 480

PRK10762

D-ribose transporter ATP binding protein; Provisional

359-555

3.25e-08

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 3.25e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLC-SLREHIATVLQDV----FLFADSI 433
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITLknPAITE-----------EEVIAAAKSIGVhnflmslpegyhYNVK-----ERGAMLSAGQRQLIAFLRAYVHK 497
Cdd:PRK10762 348 KENMSL--TALRYfsraggslkhaDEQQAVSDFIRL------------FNIKtpsmeQAIGLLSGGNQQKVAIARGLMTR 413

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 498 PQILILDEATSSVDSHSEKLIQEATDKM-TEGRTSIIIAHRLTTV-KKADRIIVLDKGKI 555
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFkAEGLSIILVSSEMPEVlGMSDRILVMHEGRI 473

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

343-554

3.30e-08

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: 52.84 E-value: 3.30e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 343 IKFEDVRFEYvAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGaIYIDGVNIEeytlcslrehIATV 422
Cdd:cd03221    1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK----------IGYF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 423 LQdvflfadsiynnitlknpaiteeeviaaaksigvhnflmslpegyhynvkergamLSAGQRQLIAFLRAYVHKPQILI 502
Cdd:cd03221   69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 503 LDEATSSVDSHSEKLIQEATdKMTEGrTSIIIAH-R--LTTVkkADRIIVLDKGK 554
Cdd:cd03221   94 LDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

358-564

6.39e-08

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 6.39e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT---LCSLREHIATVLQDVFLFAD-SI 433
Cdd:PRK11831  22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFTDmNV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNIT--LKNPAITEEEVIaaaksigvHNFLMSLPEGyhynVKERGAM------LSAGQRQLIAFLRAYVHKPQILILDE 505
Cdd:PRK11831 102 FDNVAypLREHTQLPAPLL--------HSTVMMKLEA----VGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDE 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 506 ATSSVDSHSE----KLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK11831 170 PFVGQDPITMgvlvKLISELNSAL--GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

355-520

6.83e-08

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.27 E-value: 6.83e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEIL-HGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEytlcsLREHIATVLqdvfLF---A 430
Cdd:PRK13538  12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYHQDL----LYlghQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 431 DSIYNNIT----------LKNPAiTEEEVIAAAKSIGVHNFlMSLPEGYhynvkergamLSAGQRQLIAFLRAYVHKPQI 500
Cdd:PRK13538  83 PGIKTELTalenlrfyqrLHGPG-DDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPL 150

                        170       180
                 ....*....|....*....|
gi 496950271 501 LILDEATSSVDSHSEKLIQE 520
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEA 170

ABC_6TM_VMR1_D2_like

cd18604

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...

26-270

2.08e-07

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.

Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 52.86 E-value: 2.08e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  26 FIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDY-EGLVRIVY---ILIALLCAEVTMQFLFSYYSNWLGQTVIRDVRE 101
Cdd:cd18604    1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALpPSEVSVLYylgIYALISLLSVLLGTLRYLLFFFGSLRASRKLHE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 102 KLFAHLLRFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISyatmPLILYFT 181
Cdd:cd18604   81 RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA----VVLAALY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 182 RWFQRSMNAAFVEVRHQVAN-----LNAFvQERISGIKVLQLF-AQEREELENFKKINEKHKQA--------WLkTIWYN 247
Cdd:cd18604  157 VYIGRLYLRASRELKRLESVarspiLSHF-GETLAGLVTIRAFgAEERFIEEMLRRIDRYSRAFrylwnlnrWL-SVRID 234

                        250       260
                 ....*....|....*....|...
gi 496950271 248 SiffpIGDLCVSITIALIVWFGG 270
Cdd:cd18604  235 L----LGALFSFATAALLVYGPG 253

PRK13549

xylose transporter ATP-binding subunit; Provisional

357-555

2.70e-07

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 2.70e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKT-TITNLLNRFYDLTSGAIYIDG--VNIEEyTLCSLREHIATVLQD------VF 427
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDrkrdgiVP 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 428 LFadSIYNNITLKN-PAITEEEVIAAAKSIGVHNFLMSlpegyHYNVKERGAM-----LSAGQRQLIAFLRAYVHKPQIL 501
Cdd:PRK13549 355 VM--GVGKNITLAAlDRFTGGSRIDDAAELKTILESIQ-----RLKVKTASPElaiarLSGGNQQKAVLAKCLLLNPKIL 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 502 ILDEATSSVDSHSE----KLIQEATDkmtEGRTSIIIAHRLTTV-KKADRIIVLDKGKI 555
Cdd:PRK13549 428 ILDEPTRGIDVGAKyeiyKLINQLVQ---QGVAIIVISSELPEVlGLSDRVLVMHEGKL 483

ABC_6TM_T1SS_like

cd18779

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...

23-169

3.90e-07

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: 52.16 E-value: 3.90e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQPYLIKVAIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLgQTVI-RDVRE 101
Cdd:cd18779    1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRL-RTRLdTQLTL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 102 KLFAHLLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALI 169
Cdd:cd18779   80 GFLEHLLRLPYRFFQQRSTGDLLMR-LSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLV 146

ABC_6TM_ABCB8_like

cd18574

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...

91-235

8.38e-07

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.

Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 51.01 E-value: 8.38e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  91 LGQTVIRDVREKLFAHLLRFKMRYFDKSSIGVLVTRAVNDmerIGEIFSSglFEMA-SDILKMFVIT----IVMFVIDWK 165
Cdd:cd18574   69 VGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSS--FKQCvSQGLRSVTQTvgcvVSLYLISPK 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 166 LALISYATMPlILYFTRW----FQRSMNAAfveVRHQVANLNAFVQERISGIKVLQLFAQEREELENFKKINEK 235
Cdd:cd18574  144 LTLLLLVIVP-VVVLVGTlygsFLRKLSRR---AQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEK 213

PRK10575

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

346-568

1.02e-06

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.56 E-value: 1.02e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 346 EDVRFEyVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREHIATVLQD 425
Cdd:PRK10575  15 RNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 426 VflfadsiynnitlknPA---ITEEEVIAaaksIGV---HNFLMSLPEGYHYNVKERGAM-------------LSAGQRQ 486
Cdd:PRK10575  94 L---------------PAaegMTVRELVA----IGRypwHGALGRFGAADREKVEEAISLvglkplahrlvdsLSGGERQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 487 --LIAFLRAyvHKPQILILDEATSSVD-SHSEK---LIQEATDKmtEGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:PRK10575 155 raWIAMLVA--QDSRCLLLDEPTSALDiAHQVDvlaLVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQG 230


                 ....*....
gi 496950271 560 NHEELLQIE 568
Cdd:PRK10575 231 TPAELMRGE 239

PLN03211

ABC transporter G-25; Provisional

358-559

1.54e-06

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.54e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLL------NRFydltSGAIYIDGVNIEEYTLcslrEHIATVLQDvflfaD 431
Cdd:PLN03211  83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqgNNF----TGTILANNRKPTKQIL----KRTGFVTQD-----D 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 432 SIYNNITLKNP-----------AITEEEVIAAAKSIGVHNFLMSLPEGYHYNVKERGamLSAGQRQLIAFLRAYVHKPQI 500
Cdd:PLN03211 150 ILYPHLTVRETlvfcsllrlpkSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSL 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 501 LILDEATSSVDSHSE-KLIQEATDKMTEGRTSIIIAHRLTT--VKKADRIIVLDKGKIVEIG 559
Cdd:PLN03211 228 LILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

357-556

2.06e-06

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: 48.80 E-value: 2.06e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTT----ITNLLNRFYDLtSGAIYIDGVNIEEytlcslrehIATVLQdvflfADS 432
Cdd:cd03233   21 PILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKE---------FAEKYP-----GEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 IYNNIT-LKNPAITEEEVIAAAKSIGVHNFLmslpegyhynvkeRGamLSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:cd03233   86 IYVSEEdVHFPTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 512 SHSE----KLIQEATDKMteGRTSIIIAHR--LTTVKKADRIIVLDKGKIV 556
Cdd:cd03233  151 SSTAleilKCIRTMADVL--KTTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

362-564

2.67e-06

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.74 E-value: 2.67e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVKEGETIAIVGATGAGKT----TITNLLNRFYDLTSGAIYIDGVNIEEYtlcSLREHIATVLQDV-FLFADSIynn 436
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRI---SEKERRNLVGAEVaMIFQDPM--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 437 iTLKNPAITEEEVIAAAksIGVHNflmslpEGYHYNVKERGA--------------------MLSAG--QRQLIAFlrAY 494
Cdd:PRK11022 100 -TSLNPCYTVGFQIMEA--IKVHQ------GGNKKTRRQRAIdllnqvgipdpasrldvyphQLSGGmsQRVMIAM--AI 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 495 VHKPQILILDEATSSVDSHSEKLIQEATDKMT--EGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEEL 564
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

355-556

2.67e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 2.67e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREH-IATVLQDVFLFAD-S 432
Cdd:PRK10982  10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQrS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 433 IYNNITL-----KNPAITEEEVIAAAKSIgvhnflmsLPE-GYHYNVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEA 506
Cdd:PRK10982  90 VMDNMWLgryptKGMFVDQDKMYRDTKAI--------FDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 507 TSSVD----SHSEKLIQEATDKmteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:PRK10982 162 TSSLTekevNHLFTIIRKLKER---GCGIVYISHKMEEIFQlCDEITILRDGQWI 213

ABC_6TM_HMT1

cd18583

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...

104-318

3.40e-06

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.

Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 49.06 E-value: 3.40e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 104 FAHLLRFKMRYFDKSSIGVLVtRAVNDMERIGEIFSSGLFE---MASDILKMFVITIVMFviDWKLALISYATMPLILY- 179
Cdd:cd18583   77 FNHVMNLSMDFHDSKKSGEVL-KAIEQGSSINDLLEQILFQivpMIIDLVIAIVYLYYLF--DPYMGLIVAVVMVLYVWs 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 180 ---FTRWFQ---RSMNAAFVEvRHQVANlnafvqERISGIKVLQLFAQEREELENFK-KINEKHKQAWLKTIWYNSIF-- 250
Cdd:cd18583  154 tikLTSWRTklrRDMIDADRE-ERSILT------ESLLNWETVKYFNREPYEKERYReAVKNYQKAERKYLFSLNLLNav 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496950271 251 ----FPIGDLCVSITIALIVWFGgRQIIGDNVydlgnifLFIQLSQQLFRPIRHIADKFNTLQMGIIASDRV 318
Cdd:cd18583  227 qsliLTLGLLAGCFLAAYQVSQG-QATVGDFV-------TLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

344-588

3.42e-06

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 3.42e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 344 KFEDVRFEYVAGE--EILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieEYTLCSLREHIAT 421
Cdd:PRK13545  23 KLKDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAALIAISSGLNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 422 VLQDVflfadsiyNNITLKN--PAITEEEV------IAAAKSIGvhNFLmslpegyHYNVKergaMLSAGQRQLIAFLRA 493
Cdd:PRK13545  99 QLTGI--------ENIELKGlmMGLTKEKIkeiipeIIEFADIG--KFI-------YQPVK----TYSSGMKSRLGFAIS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 494 YVHKPQILILDEATSSVDshsEKLIQEATDKMTE----GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQIE 568
Cdd:PRK13545 158 VHINPDILVIDEALSVGD---QTFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHY 234

                        250       260
                 ....*....|....*....|
gi 496950271 569 NGYYRNLYEVQFLEEVKYKE 588
Cdd:PRK13545 235 DEFLKKYNQMSVEERKDFRE 254

ABC_6TM_VMR1_D1_like

cd18596

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...

30-265

5.89e-06

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.

Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 48.26 E-value: 5.89e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  30 ALFAVLSSIFSTAQPYLIKvAIDNYITPKDYEGLVRIvYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKL----FA 105
Cdd:cd18596    3 ALLAVLSSVLSFAPPFFLN-RLLRYLEDPGEDATVRP-WVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILtqliFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 106 HLLRFKM---------------RYFDKSSIGVLVTRAVN----DMERIGEiFSSGLFEMASDILKMFVITIVMFVIDWKL 166
Cdd:cd18596   81 KALRRRDksgssksseskkkdkEEDEDEKSSASVGKINNlmsvDANRISE-FAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 167 ALISYATMPLILYFTRWFQRSMNAAFVEVRHQ----VANLNafvqERISGIKVLQLFAQEREELEnfkKINEKHKQ--AW 240
Cdd:cd18596  160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKArdarVQLVT----EVLQGIRMIKFFAWERKWEE---RILEAREEelKW 232

                        250       260
                 ....*....|....*....|....*
gi 496950271 241 LKTIWYNSIFFPIGDLCVSITIALI 265
Cdd:cd18596  233 LRKRFLLDLLLSLLWFLIPILVTVV 257

ABC_6TM_NHLM_bacteriocin

cd18569

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...

31-188

8.15e-06

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.

Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 47.86 E-value: 8.15e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFST----AQPYLIKVAIDNYITpkdyEGLVRIVYILIALLCAEVTMQFLFSyysnWLGQTVIRDVREKL--- 103
Cdd:cd18569    5 LFVVLAGLLLVipglVIPVFSRIFIDDILV----GGLPDWLRPLLLGMALTALLQGLLT----WLQQYYLLRLETKLals 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 104 -----FAHLLRFKMRYFDKSSIGVLVTR-AVNDmeRIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLI 177
Cdd:cd18569   77 sssrfFWHVLRLPVEFFSQRYAGDIASRvQSND--RVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLN 154

                        170
                 ....*....|.
gi 496950271 178 LYFTRWFQRSM 188
Cdd:cd18569  155 LLVLRLVSRKR 165

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

373-563

8.66e-06

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 8.66e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 373 AIVGATGAGKTTITNLLNRFYDLTSGAIYIDG---VNIEEYT-LCSLREHIATVLQDVFLFAD-SIYNNITLKNPAITEE 447
Cdd:PRK11144  28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGIcLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 448 EVIAAAKSIGVHNFLMSLPegyhynvkergAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVD--------SHSEKLIQ 519
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellPYLERLAR 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 496950271 520 EAtdkmtegRTSII-IAHRLTTVKK-ADRIIVLDKGKIVEIGNHEE 563
Cdd:PRK11144 177 EI-------NIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

358-511

8.74e-06

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 8.74e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 358 ILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieeytlcSLRehIATVLQDVFLFAD---SIY 434
Cdd:PRK09544  19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------KLR--IGYVPQKLYLDTTlplTVN 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 435 NNITLKnPAITEEEVIAAAKSIGVHNfLMSLPEgyhynvkergAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:PRK09544  88 RFLRLR-PGTKKEDILPALKRVQAGH-LIDAPM----------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152

ABC_6TM_peptidase_like

cd18571

Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ...

25-169

1.33e-05

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: 47.44 E-value: 1.33e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  25 VFIAVALFavLSSIFSTAQPYLIKVAIDNYITPKDYeGLvrIVYILIALLcaevtmqFLFsyysnwLGQTVIRDVREKLF 104
Cdd:cd18571    5 LQLLLGLL--LGSLLQLIFPFLTQSIVDKGINNKDL-NF--IYLILIAQL-------VLF------LGSTSIEFIRSWIL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 105 AH----------------LLRFKMRYFDKSSIGVLVTRaVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLAL 168
Cdd:cd18571   67 LHissrinisiisdflikLMRLPISFFDTKMTGDILQR-INDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFL 145


                 .
gi 496950271 169 I 169
Cdd:cd18571  146 I 146

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

357-407

2.97e-05

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 45.79 E-value: 2.97e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496950271 357 EILHGISFEVKEGETIAIVGATGAGKTTItnllnrFYDLT------SGAIYIDGVNI 407
Cdd:COG1137   17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIVglvkpdSGRIFLDGEDI 67

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

317-564

3.81e-05

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 3.81e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 317 RVFAILDT-ETDTET------GGEKELKEVKGNIKFEDVRFE----YVAGE---EILHGISFEVKEGETIAIVGATGAGK 382
Cdd:COG3845  218 KVVGTVDTaETSEEElaelmvGREVLLRVEKAPAEPGEVVLEvenlSVRDDrgvPALKDVSLEVRAGEILGIAGVAGNGQ 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 383 TTITNLLNRFYDLTSGAIYIDGVNIEEYTLCSLREH-IATVLQD---VFLFAD-SIYNNITLKN--------------PA 443
Cdd:COG3845  298 SELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgRGLVPDmSVAENLILGRyrrppfsrggfldrKA 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 444 ITE--EEVIAAaksigvhnflmslpegyhYNVKERG-----AMLSAG--QRQLIAflRAYVHKPQILILDEATSSVDSHS 514
Cdd:COG3845  378 IRAfaEELIEE------------------FDVRTPGpdtpaRSLSGGnqQKVILA--RELSRDPKLLIAAQPTRGLDVGA 437

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496950271 515 EKLIQEATDKMTEGRTSI---------IIAHrlttvkkADRIIVLDKGKIVEIGNHEEL 564
Cdd:COG3845  438 IEFIHQRLLELRDAGAAVllisedldeILAL-------SDRIAVMYEGRIVGEVPAAEA 489

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

359-587

7.59e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 7.59e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGvnieEYTLCSLREHIATVLQDVflfadsiyNNIT 438
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISAGLSGQLTGI--------ENIE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 439 LKNPAI--TEEEVIAAAKSIGVHNflmSLPEGYHYNVKErgamLSAGQRQLIAFLRAYVHKPQILILDEATSSVDshsEK 516
Cdd:PRK13546 108 FKMLCMgfKRKEIKAMTPKIIEFS---ELGEFIYQPVKK----YSSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 517 LIQEATDKMTE----GRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQiengyyrnLYEvQFLEEVKYK 587
Cdd:PRK13546 178 FAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLP--------KYE-AFLNDFKKK 244

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

359-559

9.79e-05

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.15 E-value: 9.79e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 359 LHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAI-YI--DGVNIEEYTLCS------LREHIATVLQdvflf 429
Cdd:PRK11701  22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRmrDGQLRDLYALSEaerrrlLRTEWGFVHQ----- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 430 adsiynnitlkNPAITEEEVIAAAKSIGVHnfLMSLPEgYHY-NVKERGA------------------MLSAGQRQLIAF 490
Cdd:PRK11701  97 -----------HPRDGLRMQVSAGGNIGER--LMAVGA-RHYgDIRATAGdwlerveidaariddlptTFSGGMQQRLQI 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496950271 491 LRAYVHKPQILILDEATS----SVDSHSEKLIQEATDKMteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIG 559
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGgldvSVQARLLDLLRGLVREL--GLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234

GguA

NF040905

sugar ABC transporter ATP-binding protein;

354-556

1.16e-04

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 1.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 354 AGEEILHGISFEVKEGETIAIVGATGAGKTTIT-NLLNRFYDL-TSGAIYIDGVNIEEYTLCSLREH-IATVLQDV---- 426
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAgLAYVTEDRkgyg 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 427 FLFADSIYNNITLKN-PAITEEEVIAAAKSIGVhnflmslPEGYHY-------NVKERGAMLSAGQRQLIAFLRAYVHKP 498
Cdd:NF040905 351 LNLIDDIKRNITLANlGKVSRRGVIDENEEIKV-------AEEYRKkmniktpSVFQKVGNLSGGNQQKVVLSKWLFTDP 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496950271 499 QILILDEATSSVDSHSE----KLIQEATDkmtEGRTSIIIAHRLTTV-KKADRIIVLDKGKIV 556
Cdd:NF040905 424 DVLILDEPTRGIDVGAKyeiyTIINELAA---EGKGVIVISSELPELlGMCDRIYVMNEGRIT 483

ABC_6TM_ABCB6

cd18581

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...

44-190

2.26e-04

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.

Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 43.39 E-value: 2.26e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  44 PYLIKVAIDNYiTPKDYEGLVRIVYILIALLCAEVTMQF-------LFSYYSNWL----GQTVIRDVREKLFAHLLRFKM 112
Cdd:cd18581   16 PILYKKIVDSL-TPDSADSPLAFPWALILLYVFLKFLQGggsgsvgLLSNLRSFLwipvQQFTTREISVKLFAHLHSLSL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 113 RYFDKSSIG-VL--VTRAVNDmerIGEIFSSGLFEMASDILKMfVITIVMFVI--DWKLALISYATM----PLILYFTRW 183
Cdd:cd18581   95 RWHLSRKTGeVLrvMDRGTSS---INSLLSYVLFNIGPTIADI-IIAIIYFAIafNPWFGLIVFVTMalylILTIIITEW 170

                        170
                 ....*....|
gi 496950271 184 ---FQRSMNA 190
Cdd:cd18581  171 rtkFRREMNK 180

ABC_6TM_AarD_CydDC_like

cd18781

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ...

29-317

2.51e-04

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.

Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 43.30 E-value: 2.51e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  29 VALFAVLSSIFSTAqpYLIKVAIDNYITPKDYeglVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFAHLL 108
Cdd:cd18781    7 ISLLANIAFVFSIA--NLLQKLLEGKLTTASL---LIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 109 RFKMRYFDKSSIGVLVTRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFTRWFQRSM 188
Cdd:cd18781   82 RLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 189 NAAFVEVRHQVANL-NAFVqERISGIKVLQLF-AQER------EELENFKKINEKhkqawLKTIWYNSI----FFPIGDL 256
Cdd:cd18781  162 KKLLSKYWGSYTDLgDSFL-ENLQGLTTLKIYqADERrheemnEEAEDFRKITMK-----VLTMQLNSItvmdLVAYGGA 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496950271 257 CVSITIALIVWFGGRqiigdnvYDLGNIFLFIQLSQQLFRPIR------HIAdkfntlqM-GIIASDR 317
Cdd:cd18781  236 ALGIILALLQFANGS-------ISLAGALFIILLSAEFFLPLRllgsffHIA-------MnGMAASDK 289

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

480-511

4.41e-04

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 4.41e-04

                         10        20        30
                 ....*....|....*....|....*....|..
gi 496950271 480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVD 511
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

PRK15093

peptide ABC transporter ATP-binding protein SapD;

480-565

4.56e-04

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 4.56e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMTE--GRTSIIIAHRLTTVKK-ADRIIVLDKGKIV 556
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTV 238


                 ....*....
gi 496950271 557 EIGNHEELL 565
Cdd:PRK15093 239 ETAPSKELV 247

PRK15064

ABC transporter ATP-binding protein; Provisional

355-566

7.96e-04

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 7.96e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 355 GEEILHGISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAI-YIDGVNIEEYTlcslREHIATVLQDVFLFaDSI 433
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYA----QDHAYDFENDLTLF-DWM 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 434 YNNITLKNpaitEEEVIAAAksIGvhNFLMSLPEgyhynVKERGAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSH 513
Cdd:PRK15064 406 SQWRQEGD----DEQAVRGT--LG--RLLFSQDD-----IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496950271 514 SEKLIQEATDKMtEGrTSIIIAHRLTTVKK-ADRIIVLDKGKIVEI-GNHEELLQ 566
Cdd:PRK15064 473 SIESLNMALEKY-EG-TLIFVSHDREFVSSlATRIIEITPDGVVDFsGTYEEYLR 525

PRK00635

excinuclease ABC subunit A; Provisional

480-550

8.90e-04

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 8.90e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496950271  480 LSAG--QRQLIAF-LRAYVHKPQILILDEATSSVDSHSEK-LIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVL 550
Cdd:PRK00635  810 LSGGeiQRLKLAYeLLAPSKKPTLYVLDEPTTGLHTHDIKaLIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

362-568

1.64e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 1.64e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 362 ISFEVKEGETIAIVGATGAGKTTITNLLNRFYDLTSGAIYIDGVNIEEYT-LCSLREHIATVLQDvfLFADSIYNNITlk 440
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEE--RRSTGIYAYLD-- 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 441 npaITEEEVIAAAKSIGVHNFLMS---LPEGYHY-----NVKERG-----AMLSAGQRQLIAFLRAYVHKPQILILDEAT 507
Cdd:PRK10982 343 ---IGFNSLISNIRNYKNKVGLLDnsrMKSDTQWvidsmRVKTPGhrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496950271 508 SSVDSHSE----KLIQEATDKmteGRTSIIIAHRLTTVKK-ADRIIVLDKGKIVEIGNHEELLQIE 568
Cdd:PRK10982 420 RGIDVGAKfeiyQLIAELAKK---DKGIIIISSEMPELLGiTDRILVMSNGLVAGIVDTKTTTQNE 482

PRK11147

ABC transporter ATPase component; Reviewed

341-389

1.98e-03

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 1.98e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496950271 341 GNIKF--EDVRFEyVAGEEILHGISFEVKEGETIAIVGATGAGKTTITNLL 389
Cdd:PRK11147 316 GKIVFemENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM 365

ABC_6TM_CFTR_D1

cd18594

Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ...

31-298

2.91e-03

Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.

Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 39.92 E-value: 2.91e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  31 LFAVLSSIFSTAQPYLIKVAIdNYITPkDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVREKLFA----H 106
Cdd:cd18594    4 ILLFLEESLKIVQPLLLGRLV-AYFVP-DSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSliykK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 107 LLRFKMRYFDKSSIGVLVTRAVNDMERigeifssglFEMASDILKMFVI----TIVMFVIDWKL----ALISYATMPLIL 178
Cdd:cd18594   82 TLKLSSSALSKITTGHIVNLLSNDVQK---------FDEVLVYLHFLWIaplqVIVLTGLLWREigpsSLAGLGVLLLLL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 179 YFTRWFQRsmnaAFVEVRHQVANLN----AFVQERISGIKVLQLFAQEreelENFKKINEKHKQAWLKTI--------WY 246
Cdd:cd18594  153 PLQAYLGK----LFAKYRRKTAGLTdervKIMNEIISGMRVIKMYTWE----ESFAKLIENIRKKELKLIrkaayiraFN 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496950271 247 NSIFFpigdlcVSITIALIVWFGGRQIIGdNVYDLGNIFLFIQLSQQLFRPI 298
Cdd:cd18594  225 MAFFF------FSPTLVSFATFVPYVLTG-NTLTARKVFTVISLLNALRMTI 269

ABC_6TM_PrtD_like

cd18586

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...

23-212

4.75e-03

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: 39.12 E-value: 4.75e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  23 RGVFIAVALFAVLSSIFSTAQP-YLIKVaIDNYITPKDYEGLVRIVYILIALLCAEVTMQFLFSYYSNWLGQTVIRDVRE 101
Cdd:cd18586    1 RRVFVEVGLFSFFINLLALAPPiFMLQV-YDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 102 KLFAHLLRFKMRYFDKSSIGvlvtRAVNDMERIGEIFSSGLFEMASDILKMFVITIVMFVIDWKLALISYATMPLILYFT 181
Cdd:cd18586   80 RVFRAVLELPLESRPSGYWQ----QLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLA 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 496950271 182 RWFQRSMNAAFVEVRHQVANLNAFVQERISG 212
Cdd:cd18586  156 WLNHRATRKPLGEANEAQAARDALAAETLRN 186

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

480-559

5.76e-03

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.07 E-value: 5.76e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 480 LSAGQRQ---LIAFLRAYVHkPQILILDEATSSVD-SHSEKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVLDK--- 552
Cdd:cd03238   88 LSGGELQrvkLASELFSEPP-GTLFILDEPSTGLHqQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPgsg 166

                         90
                 ....*....|
gi 496950271 553 ---GKIVEIG 559
Cdd:cd03238  167 ksgGKVVFSG 176

PRK11147

ABC transporter ATPase component; Reviewed

480-568

6.43e-03

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 6.43e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 480 LSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSeklIQEATDKMTEGRTSII-IAHRLTTVKK-ADRIIVLDKGKIVE 557
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfISHDRSFIRNmATRIVDLDRGKLVS 233

                         90
                 ....*....|....*....
gi 496950271 558 I-GNH-------EELLQIE 568
Cdd:PRK11147 234 YpGNYdqyllekEEALRVE 252

40850658_otr

NF000106

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;

477-564

7.05e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.95 E-value: 7.05e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271 477 GAMLSAGQRQLIAFLRAYVHKPQILILDEATSSVDSHSEKLIQEATDKMT-EGRTSIIIAHRLTTVKK-ADRIIVLDKGK 554
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGR 221

                         90
                 ....*....|
gi 496950271 555 IVEIGNHEEL 564
Cdd:NF000106 222 VIADGKVDEL 231

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

480-564

7.19e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 7.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496950271  480 LSAGQRQ---LIAFLRAYVHKPQILILDEATSSVDSHS-EKLIQEATDKMTEGRTSIIIAHRLTTVKKADRIIVL----- 550
Cdd:TIGR00630 830 LSGGEAQrikLAKELSKRSTGRTLYILDEPTTGLHFDDiKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpegg 909

                          90
                  ....*....|....*
gi 496950271  551 DK-GKIVEIGNHEEL 564
Cdd:TIGR00630 910 DGgGTVVASGTPEEV 924

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01