NCBI Conserved Domain Search

Conserved domains on [gi|15596057|ref|NP_249551|]

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ABC transporter ATP-binding protein/permease [Pseudomonas aeruginosa PAO1]

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];

1-596

9.70e-172

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 500.08 E-value: 9.70e-172

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   1 MSERGDRLsWAEIRRLALRHKKALLFANLVAVLATLCTVPIPLLLPllvdevllgkgdgalRFMDRLL-PADWQVAFGYI 79
Cdd:COG1132   1 MSKSPRKL-LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLG---------------RIIDALLaGGDLSALLLLL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  80 GLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLS 159
Cdd:COG1132  65 LLLLGLALL----RALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 160 RFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQG 239
Cdd:COG1132 141 QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 240 YFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLWFMIGPVEQLLGL 319
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANV 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 320 QYAYYAAGGALQRINELLARADEPRYPPLRDPFAgRTTVGIEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGK 398
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGK 379

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 399 STLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGR-ERSDQACWRALEIAQLADGV 477
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFI 459

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 478 RRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVK 557
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539

                       570       580       590
                ....*....|....*....|....*....|....*....
gi 15596057 558 QADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQM 596
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGGLYARLY-RLQFG 577

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

1-596

9.70e-172

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 500.08 E-value: 9.70e-172

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   1 MSERGDRLsWAEIRRLALRHKKALLFANLVAVLATLCTVPIPLLLPllvdevllgkgdgalRFMDRLL-PADWQVAFGYI 79
Cdd:COG1132   1 MSKSPRKL-LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLG---------------RIIDALLaGGDLSALLLLL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  80 GLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLS 159
Cdd:COG1132  65 LLLLGLALL----RALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 160 RFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQG 239
Cdd:COG1132 141 QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 240 YFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLWFMIGPVEQLLGL 319
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANV 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 320 QYAYYAAGGALQRINELLARADEPRYPPLRDPFAgRTTVGIEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGK 398
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGK 379

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 399 STLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGR-ERSDQACWRALEIAQLADGV 477
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFI 459

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 478 RRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVK 557
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539

                       570       580       590
                ....*....|....*....|....*....|....*....
gi 15596057 558 QADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQM 596
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGGLYARLY-RLQFG 577

MsbA_lipidA

TIGR02203

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

72-590

1.55e-96

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: 306.26 E-value: 1.55e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    72 WQVAFGYIGLMLaatllLRGAAlvfNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYEtlggGSISAHLVTDLDTLD 151
Cdd:TIGR02203  54 WWVPLVVIGLAV-----LRGIC---SFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFD----RQPTGTLLSRITFDS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   152 KFVGETLSRFLVAL----LTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLE 227
Cdd:TIGR02203 122 EQVASAATDAFIVLvretLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQ 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   228 AIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLW 307
Cdd:TIGR02203 202 GYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMI 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   308 FMIGPVEQLLGLQYAYYAAGGALQRINELLARADEP---RYPPlrdpfaGRTTVGIEVRGLDFAYGED--KVLEQLDLNI 382
Cdd:TIGR02203 282 ALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKdtgTRAI------ERARGDVEFRNVTFRYPGRdrPALDSISLVI 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   383 GAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER--S 460
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqaD 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   461 DQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF 540
Cdd:TIGR02203 436 RAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL 515

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15596057   541 LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:TIGR02203 516 MQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLH 565

ABCC_MsbA

cd03251

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

360-590

1.84e-83

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: 260.63 E-value: 1.84e-83

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03251   1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGRERSDQA-CWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVV 516
Cdd:cd03251  81 VSQDVFLFNDTVAENIAYGRPGATREeVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057 517 ILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234

PRK10790

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

75-595

7.17e-72

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 241.93 E-value: 7.17e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   75 AFGYIGLMLAATLLLRGAALVFNvlqaklfaRLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTL-DKF 153
Cdd:PRK10790  68 AAAYVGLQLLAAGLHYAQSLLFN--------RAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  154 VGETLSRFLVAllTLLGtaAILVWM---HWQLALLILLFNPLVI--------WSTvQLGKRVKHLKKLENDStarFTQAL 222
Cdd:PRK10790 140 VTVVATVLRSA--ALIG--AMLVAMfslDWRMALVAIMIFPAVLvvmviyqrYST-PIVRRVRAYLADINDG---FNEVI 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  223 TeTLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwksdaagRASGLLFQFGIDVFRAAAMLTVLL-------SDLS 295
Cdd:PRK10790 212 N-GMSVIQQFRQQARFGERMGEASRSHYMARMQTL----------RLDGFLLRPLLSLFSALILCGLLMlfgfsasGTIE 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  296 IGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRINELLARADEPRYPPLRDPFAGRttvgIEVRGLDFAYGEDK-V 374
Cdd:PRK10790 281 VGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGR----IDIDNVSFAYRDDNlV 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLT 454
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT 436

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  455 MGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALH 534
Cdd:PRK10790 437 LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057  535 QALGDFLEgRTTLIV-AHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQ 595
Cdd:PRK10790 517 QALAAVRE-HTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY-QLQL 576

ABC_tran

pfam00005

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

375-523

5.53e-34

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: 126.22 E-value: 5.53e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFND-SVRANL 453
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057   454 TMGR---ERSDQACWRalEIAQLADGVRRLPQgLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATS 523
Cdd:pfam00005  81 RLGLllkGLSKREKDA--RAEEALEKLGLGDL-ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

368-565

9.78e-24

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 9.78e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvREHVAVVLQH---PAL 444
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevPDS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 FNDSVRANLTMGRERsDQACWRALEI---AQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEA 521
Cdd:NF040873  70 LPLTVRDLVAMGRWA-RRGLWRRLTRddrAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15596057  522 TSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQADRVLVF 565
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191

GguA

NF040905

sugar ABC transporter ATP-binding protein;

373-570

7.18e-10

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 7.18e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSA--QRGSIRYGGvplEEIGLDCVR--EHVAVVLQH------P 442
Cdd:NF040905  15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDG---EVCRFKDIRdsEALGIVIIHqelaliP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  443 ALfndSVRANLTMGRERS-------DQACWRALEIaqLAD-GVRRLPqglDTVVGRSGVrlsgGQRQRLAIARMILAEPK 514
Cdd:NF040905  92 YL---SIAENIFLGNERAkrgvidwNETNRRAREL--LAKvGLDESP---DTLVTDIGV----GKQQLVEIAKALSKDVK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  515 VVILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVF-DGGHI 570
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRvADSITVLrDGRTI 218

40850658_otr

NF000106

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

359-584

3.45e-08

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 3.45e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGG--KSTLVQLLLGLySAQRGSIRYGGVPLEEIGLD-CVREHV 435
Cdd:NF000106  13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP-DAGRRPWRF*TWCANRRALRrTIG*HR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  436 AVVLQHPALFndSVRANLTM-GR----ERSDqACWRALEIaqladgVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:NF000106  92 PVR*GRRESF--SGRENLYMiGR*ldlSRKD-ARARADEL------LERF--SLTEAAGRAAAKYSGGMRRRLDLAASMI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  511 AEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEGG 584
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236

AAA

smart00382

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

385-560

1.51e-06

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

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 1.51e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIryggvpleeigldcvrehvavvlqhpalfndsVRANLTMGRERSDQac 464
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLD-- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    465 wraleiaqladgvrrlpQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL--- 541
Cdd:smart00382  48 -----------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110

                          170       180
                   ....*....|....*....|..
gi 15596057    542 ---EGRTTLIVAHRLSAVKQAD 560
Cdd:smart00382 111 lksEKNLTVILTTNDEKDLGPA 132

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

343-526

2.32e-06

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.32e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  343 PRYPPLRDPFAgrttvgIEVRGLDFAYGE----DKVleqlDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRY 418
Cdd:NF033858 256 PRPADDDDEPA------IEARGLTMRFGDftavDHV----SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  419 GGVPLEEIGLDcVREHVAVVLQHPALFND-SVRANLT-------MGRERSDQACWRALEIAQLADGVRRLPQgldtvvgr 490
Cdd:NF033858 326 FGQPVDAGDIA-TRRRVGYMSQAFSLYGElTVRQNLElharlfhLPAAEIAARVAEMLERFDLADVADALPD-------- 396

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15596057  491 sgvRLSGGQRQRLAIARMILAEPKVVILDEATSALD 526
Cdd:NF033858 397 ---SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

360-526

3.75e-05

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 3.75e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG-LDCVREHVAVV 438
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhRRAVCPRIAYM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQ------HPALfndSVRANLT-MGRERSDQACWRALEIAQLADGVrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILA 511
Cdd:NF033858  82 PQglgknlYPTL---SVFENLDfFGRLFGQDAAERRRRIDELLRAT-----GLAPFADRPAGKLSGGMKQKLGLCCALIH 153

                        170
                 ....*....|....*
gi 15596057  512 EPKVVILDEATSALD 526
Cdd:NF033858 154 DPDLLILDEPTTGVD 168

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

1-596

9.70e-172

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 500.08 E-value: 9.70e-172

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   1 MSERGDRLsWAEIRRLALRHKKALLFANLVAVLATLCTVPIPLLLPllvdevllgkgdgalRFMDRLL-PADWQVAFGYI 79
Cdd:COG1132   1 MSKSPRKL-LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLG---------------RIIDALLaGGDLSALLLLL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  80 GLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLS 159
Cdd:COG1132  65 LLLLGLALL----RALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 160 RFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQG 239
Cdd:COG1132 141 QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 240 YFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLWFMIGPVEQLLGL 319
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANV 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 320 QYAYYAAGGALQRINELLARADEPRYPPLRDPFAgRTTVGIEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGK 398
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGK 379

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 399 STLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGR-ERSDQACWRALEIAQLADGV 477
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFI 459

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 478 RRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVK 557
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539

                       570       580       590
                ....*....|....*....|....*....|....*....
gi 15596057 558 QADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQM 596
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGGLYARLY-RLQFG 577

SunT

COG2274

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

7-590

7.83e-136

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: 412.31 E-value: 7.83e-136

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   7 RLSWAEIRRLALRHKKALLFANLVAVLATLCtvpiplllpllvdevllgkgdgAL-------RFMDRLLPADwqvAFGYI 79
Cdd:COG2274 141 PFGLRWFLRLLRRYRRLLLQVLLASLLINLL----------------------ALatplftqVVIDRVLPNQ---DLSTL 195

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  80 GLMLAATLLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHlVTDLDTLDKFVGETLS 159
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR-FRDVESIREFLTGSLL 274

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 160 RFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQG 239
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAES 354

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 240 YFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFG-IDVFRAAAMLtVLLSDLSIGQMLAVFSYLWFMIGPVEQLLG 318
Cdd:COG2274 355 RFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYL-VIDGQLTLGQLIAFNILSGRFLAPVAQLIG 433

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 319 LQYAYYAAGGALQRINELLARADEP---RYPPLRDPFAGRttvgIEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGA 393
Cdd:COG2274 434 LLQRFQDAKIALERLDDILDLPPEReegRSKLSLPRLKGD----IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGR 509

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 394 SGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER-SDQACWRALEIAQ 472
Cdd:COG2274 510 SGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAG 589

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 473 LADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHR 552
Cdd:COG2274 590 LHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHR 669

                       570       580       590
                ....*....|....*....|....*....|....*...
gi 15596057 553 LSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707

CydC

COG4987

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

114-590

8.90e-100

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: 314.40 E-value: 8.90e-100

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 114 RIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLF---- 189
Cdd:COG4987  89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGllla 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 190 ----NPLVIWSTVQLGKRVKHLKklendstARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRdyavASQWKSDA 265
Cdd:COG4987 169 glllPLLAARLGRRAGRRLAAAR-------AALRARLTDLLQGAAELAAYGALDRALARLDAAEARLA----AAQRRLAR 237

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 266 AGRASGLLFQFGIDVFrAAAMLTVLLSDLSIGQ----MLAVFSylwFMIGPV-EQLLGLQYAYYAAGG---ALQRINELL 337
Cdd:COG4987 238 LSALAQALLQLAAGLA-VVAVLWLAAPLVAAGAlsgpLLALLV---LAALALfEALAPLPAAAQHLGRvraAARRLNELL 313

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 338 ARADEPRYPPlrDPFAGRTTVGIEVRGLDFAY--GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGS 415
Cdd:COG4987 314 DAPPAVTEPA--EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 416 IRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER-SDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVR 494
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 495 LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDG 574
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551

                       490
                ....*....|....*.
gi 15596057 575 DHQQLIAEGGLYARLY 590
Cdd:COG4987 552 THEELLAQNGRYRQLY 567

MsbA_lipidA

TIGR02203

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

72-590

1.55e-96

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 306.26 E-value: 1.55e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    72 WQVAFGYIGLMLaatllLRGAAlvfNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYEtlggGSISAHLVTDLDTLD 151
Cdd:TIGR02203  54 WWVPLVVIGLAV-----LRGIC---SFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFD----RQPTGTLLSRITFDS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   152 KFVGETLSRFLVAL----LTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLE 227
Cdd:TIGR02203 122 EQVASAATDAFIVLvretLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQ 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   228 AIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLW 307
Cdd:TIGR02203 202 GYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMI 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   308 FMIGPVEQLLGLQYAYYAAGGALQRINELLARADEP---RYPPlrdpfaGRTTVGIEVRGLDFAYGED--KVLEQLDLNI 382
Cdd:TIGR02203 282 ALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKdtgTRAI------ERARGDVEFRNVTFRYPGRdrPALDSISLVI 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   383 GAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER--S 460
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqaD 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   461 DQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF 540
Cdd:TIGR02203 436 RAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL 515

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15596057   541 LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:TIGR02203 516 MQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLH 565

CydD

COG4988

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

81-584

1.50e-94

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: 300.52 E-value: 1.50e-94

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  81 LMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSR 160
Cdd:COG4988  62 GLLLAVLLLRA---LLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQ 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 161 FLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKhlKKLEN--DSTARFTQALTETLEAIQEVRAgnrq 238
Cdd:COG4988 139 LFLAALVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAA--KASRRqwRALARLSGHFLDRLRGLTTLKL---- 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 239 gyfLGRLGHRAQEVRdyavasqwksdaagRASgllfqfgiDVFRAAAM--LTV---------LLSDLSIGqMLAVFSYLW 307
Cdd:COG4988 213 ---FGRAKAEAERIA--------------EAS--------EDFRKRTMkvLRVaflssavleFFASLSIA-LVAVYIGFR 266

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 308 FMIGPVE------------------QLLGLQY-AYYAAGGALQRINELLArADEPRYPPLRDPFAGRTTVGIEVRGLDFA 368
Cdd:COG4988 267 LLGGSLTlfaalfvlllapefflplRDLGSFYhARANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFS 345

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 369 YGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFND 447
Cdd:COG4988 346 YPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAG 425

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 448 SVRANLTMGR-ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALD 526
Cdd:COG4988 426 TIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057 527 AATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGG 584
Cdd:COG4988 506 AETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563

ABCC_MsbA

cd03251

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

360-590

1.84e-83

Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 260.63 E-value: 1.84e-83

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03251   1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGRERSDQA-CWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVV 516
Cdd:cd03251  81 VSQDVFLFNDTVAENIAYGRPGATREeVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057 517 ILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234

ABCC_ATM1_transporter

cd03253

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

360-590

7.24e-82

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: 256.77 E-value: 7.24e-82

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:cd03253   1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPALFNDSVRANLTMGRER-SDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03253  81 PQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233

ABC_MTABC3_MDL1_MDL2

cd03249

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

360-590

2.41e-80

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: 252.85 E-value: 2.41e-80

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY---GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVA 436
Cdd:cd03249   1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 437 VVLQHPALFNDSVRANLTMGR-ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:cd03249  81 LVSQEPVLFDGTIAENIRYGKpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 516 VILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235

ATM1

COG5265

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

4-595

2.99e-80

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: 264.37 E-value: 2.99e-80

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   4 RGDRLSWAEIRRLALRHKKALLFANLVAVLATLCTVPIPLLLPLLVDEVllgkgdgalrfMDRLLPADWQVAFGYIGLML 83
Cdd:COG5265  14 PRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDA-----------IDALLSGAAALLVVPVGLLL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  84 AATLLlRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALG---EYETlgGGsisahLVTDLDTLDKFVgETLSR 160
Cdd:COG5265  83 AYGLL-RLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRfhlERQT--GG-----LSRDIERGTKGI-EFLLR 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 161 FLV-----ALLTLLGTAAILVWM-HWQLALLILLFNPLVIWSTVQL-GKRVKHLKK---LENDSTARFTQAL--TETlea 228
Cdd:COG5265 154 FLLfnilpTLLEIALVAGILLVKyDWWFALITLVTVVLYIAFTVVVtEWRTKFRREmneADSEANTRAVDSLlnYET--- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 229 iqeVRagnrqgYFlgrlGHRAQEVRDYAVASQWKSDAAGRASGLLF--QFGIDVFRAAAMLTVLL--------SDLSIGQ 298
Cdd:COG5265 231 ---VK------YF----GNEAREARRYDEALARYERAAVKSQTSLAllNFGQALIIALGLTAMMLmaaqgvvaGTMTVGD 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 299 MLAVFSYlwfMIgpveQL------LGLQYAYYAAGGA-LQRINELLAR----ADEPRYPPLRdpfagRTTVGIEVRGLDF 367
Cdd:COG5265 298 FVLVNAY---LI----QLyiplnfLGFVYREIRQALAdMERMFDLLDQppevADAPDAPPLV-----VGGGEVRFENVSF 365

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 368 AYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFN 446
Cdd:COG5265 366 GYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 447 DSVRANLTMGR-ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSAL 525
Cdd:COG5265 446 DTIAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525

                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 526 DAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQ 595
Cdd:COG5265 526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW-ARQQ 594

ABCC_Glucan_exporter_like

cd03254

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

360-584

5.88e-80

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: 251.38 E-value: 5.88e-80

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:cd03254   3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPALFNDSVRANLTMGRERSDQACW-RALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03254  83 LQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGG 584
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229

3a01208

TIGR00958

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

111-589

6.85e-74

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 250.02 E-value: 6.85e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   111 IVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFN 190
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   191 PLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYavasqWKSDAAGRAS 270
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQL-----NKRKALAYAG 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   271 GL----LFQFGIDVfraaAMLT-----VLLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRINELLARad 341
Cdd:TIGR00958 387 YLwttsVLGMLIQV----LVLYyggqlVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDR-- 460

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   342 EPRYPP----LRDPFAGRttvgIEVRGLDFAY---GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRG 414
Cdd:TIGR00958 461 KPNIPLtgtlAPLNLEGL----IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   415 SIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLA-DGVRRLPQGLDTVVGRSGV 493
Cdd:TIGR00958 537 QVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAhDFIMEFPNGYDTEVGEKGS 616

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   494 RLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGdfLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAED 573
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694

                         490
                  ....*....|....*.
gi 15596057   574 GDHQQLIAEGGLYARL 589
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHL 710

ABCC_MRP_Like

cd03228

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

360-569

3.20e-72

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: 229.19 E-value: 3.20e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED--KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03228   1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLtmgrersdqacwraleiaqladgvrrlpqgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03228  81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGH 569
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

PRK10790

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

75-595

7.17e-72

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 241.93 E-value: 7.17e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   75 AFGYIGLMLAATLLLRGAALVFNvlqaklfaRLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTL-DKF 153
Cdd:PRK10790  68 AAAYVGLQLLAAGLHYAQSLLFN--------RAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  154 VGETLSRFLVAllTLLGtaAILVWM---HWQLALLILLFNPLVI--------WSTvQLGKRVKHLKKLENDStarFTQAL 222
Cdd:PRK10790 140 VTVVATVLRSA--ALIG--AMLVAMfslDWRMALVAIMIFPAVLvvmviyqrYST-PIVRRVRAYLADINDG---FNEVI 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  223 TeTLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwksdaagRASGLLFQFGIDVFRAAAMLTVLL-------SDLS 295
Cdd:PRK10790 212 N-GMSVIQQFRQQARFGERMGEASRSHYMARMQTL----------RLDGFLLRPLLSLFSALILCGLLMlfgfsasGTIE 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  296 IGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRINELLARADEPRYPPLRDPFAGRttvgIEVRGLDFAYGEDK-V 374
Cdd:PRK10790 281 VGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGR----IDIDNVSFAYRDDNlV 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLT 454
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT 436

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  455 MGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALH 534
Cdd:PRK10790 437 LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057  535 QALGDFLEgRTTLIV-AHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQ 595
Cdd:PRK10790 517 QALAAVRE-HTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY-QLQL 576

PRK11176

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

168-590

2.01e-70

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 237.61 E-value: 2.01e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  168 LLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFLGRLGH 247
Cdd:PRK11176 153 IIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDK 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  248 RAQEVRDYAVasqwKSDAAGRASGLLFQFgIDVFRAAAMLTV-----LLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYA 322
Cdd:PRK11176 233 VSNRMRQQGM----KMVSASSISDPIIQL-IASLALAFVLYAasfpsVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  323 YYAAGGALQRINELL---ARADEPRYPplrdpfAGRTTVGIEVRGLDFAY-GEDK-VLEQLDLNIGAGEKVALVGASGGG 397
Cdd:PRK11176 308 FQRGMAACQTLFAILdleQEKDEGKRV------IERAKGDIEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSG 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  398 KSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER--SDQACWRALEIAQLAD 475
Cdd:PRK11176 382 KSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqySREQIEEAARMAYAMD 461

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  476 GVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSA 555
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 15596057  556 VKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:PRK11176 542 IEKADEILVVEDGEIVERGTHAELLAQNGVYAQLH 576

ABCC_Hemolysin

cd03252

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

360-590

3.72e-69

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: 223.52 E-value: 3.72e-69

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03252   1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGRERSDQAcwRALEIAQLADG---VRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:cd03252  81 VLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 515 VVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLY 590
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234

bacteriocin_ABC

TIGR01193

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

95-592

4.92e-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: 236.94 E-value: 4.92e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    95 VFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLvALLTLLGTAAI 174
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFL-DMWILVIVGLF 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   175 LVWMHWQLALLILLFNPL---VIWSTVQLGKRVKHlKKLENDSTarFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQE 251
Cdd:TIGR01193 290 LVRQNMLLFLLSLLSIPVyavIIILFKRTFNKLNH-DAMQANAV--LNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGD 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   252 VRDYAVASQwKSDAAGRASGLLFQFGIDVF--RAAAMLtVLLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGA 329
Cdd:TIGR01193 367 YLNKSFKYQ-KADQGQQAIKAVTKLILNVVilWTGAYL-VMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVA 444

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   330 LQRINELLARADEPRYPPLRDpfAGRTTVG-IEVRGLDFAYG-EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLG 407
Cdd:TIGR01193 445 NNRLNEVYLVDSEFINKKKRT--ELNNLNGdIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG 522

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   408 LYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER--SDQACWRALEIAQLADGVRRLPQGLD 485
Cdd:TIGR01193 523 FFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKEnvSQDEIWAACEIAEIKDDIENMPLGYQ 602

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   486 TVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGdFLEGRTTLIVAHRLSAVKQADRVLVF 565
Cdd:TIGR01193 603 TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVL 681

                         490       500
                  ....*....|....*....|....*..
gi 15596057   566 DGGHIAEDGDHQQLIAEGGLYARLYGH 592
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRNGFYASLIHN 708

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

162-589

1.69e-67

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 229.85 E-value: 1.69e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  162 LVALLTLLGTAailVWMHWQLA-LLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQAlTETLEAIQEVRAGNRqgy 240
Cdd:PRK13657 141 LVALVVLLPLA---LFMNWRLSlVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHV-SDAIGNVSVVQSYNR--- 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  241 flgrLGHRAQEVRDYA---------VASQWK-SDAAGRASGLLFQFGIdvFRAAAMLtVLLSDLSIGQMLAVFSYLWFMI 310
Cdd:PRK13657 214 ----IEAETQALRDIAdnllaaqmpVLSWWAlASVLNRAASTITMLAI--LVLGAAL-VQKGQLRVGEVVAFVGFATLLI 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  311 GPVEQLLGLQYAYYAAGGALQRINELL----ARADEPRYPPLRDpFAGRttvgIEVRGLDFAY-GEDKVLEQLDLNIGAG 385
Cdd:PRK13657 287 GRLDQVVAFINQVFMAAPKLEEFFEVEdavpDVRDPPGAIDLGR-VKGA----VEFDDVSFSYdNSRQGVEDVSFEAKPG 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  386 EKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRE-RSDQAC 464
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdATDEEM 441

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  465 WRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGR 544
Cdd:PRK13657 442 RAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR 521

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 15596057  545 TTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:PRK13657 522 TTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566

NHLM_micro_ABC1

TIGR03796

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

81-589

4.72e-67

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: 231.37 E-value: 4.72e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    81 LMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHlVTDLDTLDKFVGETLSR 160
Cdd:TIGR03796 198 LGMGLTALLQG---VLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASR-VQLNDQVAEFLSGQLAT 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   161 FLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWsTVQL--GKRVKHLKKLENDsTARFTQALTETLEAIQEVRA-GNR 237
Cdd:TIGR03796 274 TALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVL-ALQLvsRRRVDANRRLQQD-AGKLTGVAISGLQSIETLKAsGLE 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   238 QGYFLGRLGHRAQevrdyAVASQWKSDAAGRASGLLFQFgIDVFRAAAMLT-----VLLSDLSIGQMLAVFSYLWFMIGP 312
Cdd:TIGR03796 352 SDFFSRWAGYQAK-----LLNAQQELGVLTQILGVLPTL-LTSLNSALILVvgglrVMEGQLTIGMLVAFQSLMSSFLEP 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   313 VEQLLGLqyayyaaGGALQRINELLARADE----PRYPPLRDPFA--------GRTTVGIEVRGLDFAYG--EDKVLEQL 378
Cdd:TIGR03796 426 VNNLVGF-------GGTLQELEGDLNRLDDvlrnPVDPLLEEPEGsaatseppRRLSGYVELRNITFGYSplEPPLIENF 498

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   379 DLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTM-GR 457
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLwDP 578

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   458 ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQAL 537
Cdd:TIGR03796 579 TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL 658

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15596057   538 GDflEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:TIGR03796 659 RR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708

type_I_sec_HlyB

TIGR01846

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

99-592

1.76e-66

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]

Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 229.63 E-value: 1.76e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    99 LQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHlVTDLDTLDKFV-GETLSRFLVALLTLLGTAAILvW 177
Cdd:TIGR01846 198 LRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVAR-VRELEQIRNFLtGSALTVVLDLLFVVVFLAVMF-F 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   178 MHWQLALLILLFNP--LVIWSTVQ--LGKRVKhlKKLENDSTArfTQALTETLEAIQEVRAGNRQGYFlgrlGHRAQEVR 253
Cdd:TIGR01846 276 YSPTLTGVVIGSLVcyALLSVFVGpiLRKRVE--DKFERSAAA--TSFLVESVTGIETIKATATEPQF----QNRWDRQL 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   254 DYAVASQWKSDAAGRASGLLFQFgIDVFRAAAML-----TVLLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGG 328
Cdd:TIGR01846 348 AAYVAASFRVTNLGNIAGQAIEL-IQKLTFAILLwfgahLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGI 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   329 ALQRINELLARADEPRYpplrdpfAGRTTV-----GIEVRGLDFAYGED--KVLEQLDLNIGAGEKVALVGASGGGKSTL 401
Cdd:TIGR01846 427 ALERLGDILNSPTEPRS-------AGLAALpelrgAITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTL 499

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   402 VQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRERSDQAcwRALEIAQLA---DGVR 478
Cdd:TIGR01846 500 TKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFE--HVIHAAKLAgahDFIS 577

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   479 RLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQ 558
Cdd:TIGR01846 578 ELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRA 657

                         490       500       510
                  ....*....|....*....|....*....|....
gi 15596057   559 ADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYGH 592
Cdd:TIGR01846 658 CDRIIVLEKGQIAESGRHEELLALQGLYARLWQQ 691

ABCC_bacteriocin_exporters

cd03245

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

360-574

5.68e-64

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: 209.37 E-value: 5.68e-64

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03245   3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGR-ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVV 516
Cdd:cd03245  83 VPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057 517 ILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDG 574
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220

ABCC_MRP_domain2

cd03244

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

360-574

2.47e-63

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: 207.73 E-value: 2.47e-63

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY--GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03244   3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03244  83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDG 574
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219

CydD

TIGR02857

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

81-564

1.46e-60

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: 209.84 E-value: 1.46e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    81 LMLAATLLLRgAALVFnvLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFvgetLSR 160
Cdd:TIGR02857  48 GALALVLLLR-ALLGW--LQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGY----FAR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   161 FLVAL-LTLLGTAAILV---WMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGN 236
Cdd:TIGR02857 121 YLPQLvLAVIVPLAILAavfPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFG 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   237 RQGYFLGRLGHRAQEVRDyavasqwKSDAAGRASgLLFQFGIDVFRA--AAMLTVLLSDLSIGQMLAVFSYLWFMI---- 310
Cdd:TIGR02857 201 RAKAQAAAIRRSSEEYRE-------RTMRVLRIA-FLSSAVLELFATlsVALVAVYIGFRLLAGDLDLATGLFVLLlape 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   311 --GPVEQLLGLQYAYYAAGGALQRINELLARADEPrYPPLRDPFAGRTTVgIEVRGLDFAY-GEDKVLEQLDLNIGAGEK 387
Cdd:TIGR02857 273 fyLPLRQLGAQYHARADGVAAAEALFAVLDAAPRP-LAGKAPVTAAPASS-LEFSGVSVAYpGRRPALRPVSFTVPPGER 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   388 VALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGR-ERSDQACWR 466
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIRE 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   467 ALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTT 546
Cdd:TIGR02857 431 ALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV 510

                         490
                  ....*....|....*...
gi 15596057   547 LIVAHRLSAVKQADRVLV 564
Cdd:TIGR02857 511 LLVTHRLALAALADRIVV 528

NHLM_micro_ABC2

TIGR03797

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

162-589

1.74e-59

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: 210.20 E-value: 1.74e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   162 LVALLTLlgtaAILVWMHWQLALLILLFNPLVIWSTVQLG-KRVKHLKKLENDSTARFTQALtETLEAIQEVR---AGNR 237
Cdd:TIGR03797 261 IFALLNL----GLMFYYSWKLALVAVALALVAIAVTLVLGlLQVRKERRLLELSGKISGLTV-QLINGISKLRvagAENR 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   238 QGYFLGRLghRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFrAAAMLTVLLSDLSIGQMLAVFSYLWFMIGPVEQLL 317
Cdd:TIGR03797 336 AFARWAKL--FSRQRKLELSAQRIENLLTVFNAVLPVLTSAALF-AAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLS 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   318 GLQYAYYAAGGALQR---INELLARADEPRYPPlrdpfaGRTTVGIEVRGLDFAYGED--KVLEQLDLNIGAGEKVALVG 392
Cdd:TIGR03797 413 NTLISILAVIPLWERakpILEALPEVDEAKTDP------GKLSGAIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVG 486

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   393 ASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQ 472
Cdd:TIGR03797 487 PSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAG 566

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   473 LADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFleGRTTLIVAHR 552
Cdd:TIGR03797 567 LAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHR 644

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 15596057   553 LSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:TIGR03797 645 LSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681

PRK10789

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

289-596

3.52e-58

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 204.56 E-value: 3.52e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  289 VLLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRINELLARA----DEPRYPPlrdpfAGRTTVGIEVRG 364
Cdd:PRK10789 246 VVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEApvvkDGSEPVP-----EGRGELDVNIRQ 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  365 LDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPAL 444
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 FNDSVRANLTMGR-ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATS 523
Cdd:PRK10789 401 FSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057  524 ALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYgHLQQM 596
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMY-RYQQL 552

CydC

TIGR02868

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

107-553

1.34e-56

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: 199.12 E-value: 1.34e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   107 LSKDIVYRI----RLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQL 182
Cdd:TIGR02868  76 VGHDAALRSlgalRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   183 A-------LLILLFNPLV-IWSTVQLGKRVKHLKklendstARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRD 254
Cdd:TIGR02868 156 AlilaaglLLAGFVAPLVsLRAARAAEQALARLR-------GELAAQLTDALDGAAELVASGALPAALAQVEEADRELTR 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   255 yAVASQWKSDAAGRASGLLFQfGIDVFRAAAMLTVLLSDLSI-GQMLAVFSYLWF-MIGPVEQLLGLQYAYYAAGGALQR 332
Cdd:TIGR02868 229 -AERRAAAATALGAALTLLAA-GLAVLGALWAGGPAVADGRLaPVTLAVLVLLPLaAFEAFAALPAAAQQLTRVRAAAER 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   333 INELLARA---DEPRYPplRDPFAGRTTVGIEVRGLDFAY-GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL 408
Cdd:TIGR02868 307 IVEVLDAAgpvAEGSAP--AAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   409 YSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGR-ERSDQACWRALEIAQLADGVRRLPQGLDTV 487
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTV 464

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057   488 VGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRL 553
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530

PRK11174

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

317-595

2.53e-56

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 199.69 E-value: 2.53e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  317 LGLQY-AYYAAGGALQRINELLArADEPRYPPLRDPFAGRTTVGIEVRGLDFAYGEDKVLEQ-LDLNIGAGEKVALVGAS 394
Cdd:PRK11174 307 LGTFYhAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPS 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  395 GGGKSTLVQLLLGlYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRER-SDQACWRALEIAQL 473
Cdd:PRK11174 386 GAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDaSDEQLQQALENAWV 464

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  474 ADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRL 553
Cdd:PRK11174 465 SEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQL 544

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15596057  554 SAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYGHLQQ 595
Cdd:PRK11174 545 EDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586

PRK11160

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

143-593

1.33e-54

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 194.66 E-value: 1.33e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  143 LVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLI--LLFNPLVIWSTV--QLGKRV-KHLkkleNDSTAR 217
Cdd:PRK11160 123 LVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALTLggILLLLLLLLPLLfyRLGKKPgQDL----THLRAQ 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  218 FTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVrdyaVASQWK-SDAAGRASGLL-FQFGIdvfraAAMLTVLLSDLS 295
Cdd:PRK11160 199 YRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQW----LAAQRRqANLTGLSQALMiLANGL-----TVVLMLWLAAGG 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  296 IGQM--------LAVFSYL--WFMIGPVeqllglqyayyaaGGALQ----------RINELLARADEPRYPPLRDPFAGR 355
Cdd:PRK11160 270 VGGNaqpgaliaLFVFAALaaFEALMPV-------------AGAFQhlgqviasarRINEITEQKPEVTFPTTSTAAADQ 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  356 ttVGIEVRGLDFAY--GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVRE 433
Cdd:PRK11160 337 --VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  434 HVAVVLQHPALFNDSVRANLTMGRER-SDQACWRALE---IAQLADGvrrlPQGLDTVVGRSGVRLSGGQRQRLAIARMI 509
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAAPNaSDEALIEVLQqvgLEKLLED----DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  510 LAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570


                 ....
gi 15596057  590 YGHL 593
Cdd:PRK11160 571 KQRL 574

ArpD

COG4618

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

81-582

1.71e-52

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: 188.80 E-value: 1.71e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  81 LMLaaTLLLRGAALVFNVLQA---KLFARLSKDIVYRIRLRLIErlrhiALGEYETLGGGSISAHLVTDLDTLDKFV-GE 156
Cdd:COG4618  60 LML--TLLALGLYAVMGLLDAvrsRILVRVGARLDRRLGPRVFD-----AAFRAALRGGGGAAAQALRDLDTLRQFLtGP 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 157 TLSRFLVALLTLLGTAAILVwMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAgn 236
Cdd:COG4618 133 GLFALFDLPWAPIFLAVLFL-FHPLLGLLALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEA-- 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 237 rQGyFLGRLGHRAQEVRDYAVASQWK-SDAAGRASG------LLFQfgIDVFRAAAMLtVLLSDLSIGQMLAVfSylwFM 309
Cdd:COG4618 210 -MG-MLPALRRRWQRANARALALQARaSDRAGGFSAlskflrLLLQ--SAVLGLGAYL-VIQGEITPGAMIAA-S---IL 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 310 IG----PVEQLLGLQYAYYAAGGALQRINELLA-RADEPRYPPLRDPfAGRttvgIEVRGLDFAY-GEDK-VLEQLDLNI 382
Cdd:COG4618 281 MGralaPIEQAIGGWKQFVSARQAYRRLNELLAaVPAEPERMPLPRP-KGR----LSVENLTVVPpGSKRpILRGVSFSL 355

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 383 GAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL-----EEIGldcvrEHVAVVLQHPALFNDSVRANLTMGR 457
Cdd:COG4618 356 EPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdrEELG-----RHIGYLPQDVELFDGTIAENIARFG 430

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 458 ERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQAL 537
Cdd:COG4618 431 DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI 510

                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*.
gi 15596057 538 GDF-LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:COG4618 511 RALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556

ABCC_TAP

cd03248

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

360-570

3.11e-50

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.

Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 173.43 E-value: 3.11e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY---GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVA 436
Cdd:cd03248  12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 437 VVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADG-VRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:cd03248  92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 516 VILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHI 570
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

MRP_assoc_pro

TIGR00957

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

76-586

6.45e-50

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: 186.69 E-value: 6.45e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057     76 FGYIGLMLAATLLLRGAALVFNVLQAKlfARLSKDIVYRIrlrlierLRHiALGEYETLGGGSISAHLVTDLDTLDKFVG 155
Cdd:TIGR00957 1011 YGALGILQGFAVFGYSMAVSIGGIQAS--RVLHQDLLHNK-------LRS-PMSFFERTPSGNLVNRFSKELDTVDSMIP 1080

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    156 ETLSRFLVALLTLLGtAAILVWMHWQLALLILLfnPL-VIWSTVQ--LGKRVKHLKKLENDSTARFTQALTETLEAIQEV 232
Cdd:TIGR00957 1081 PVIKMFMGSLFNVIG-ALIVILLATPIAAVIIP--PLgLLYFFVQrfYVASSRQLKRLESVSRSPVYSHFNETLLGVSVI 1157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    233 RAGNRQGYFLgrlgHRAQEVRDYAVASQWKSDAAGRASGLLFQF-GIDVFRAAAMLTVL--------LSDLSIGQMLAVF 303
Cdd:TIGR00957 1158 RAFEEQERFI----HQSDLKVDENQKAYYPSIVANRWLAVRLECvGNCIVLFAALFAVIsrhslsagLVGLSVSYSLQVT 1233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    304 SYLWFMIGPVEQLlglqyayYAAGGALQRINELLARADEPRY------PPLRDPFAGRttvgIEVRGLDFAYGE--DKVL 375
Cdd:TIGR00957 1234 FYLNWLVRMSSEM-------ETNIVAVERLKEYSETEKEAPWqiqetaPPSGWPPRGR----VEFRNYCLRYREdlDLVL 1302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    376 EQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTM 455
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDP 1382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    456 GRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQ 535
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15596057    536 ALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLY 586
Cdd:TIGR00957 1463 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513

EcfA2

COG1122

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

360-582

9.28e-50

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: 172.13 E-value: 9.28e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY-GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:COG1122   1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPA--LFNDSVRANLTMG-----------RERSDQACwRALEIAQLADgvrRLPQgldtvvgrsgvRLSGGQRQRLAI 505
Cdd:COG1122  81 FQNPDdqLFAPTVEEDVAFGpenlglpreeiRERVEEAL-ELVGLEHLAD---RPPH-----------ELSGGQKQRVAI 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057 506 ARMILAEPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVFSD 224

type_I_sec_PrtD

TIGR01842

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

61-582

2.58e-49

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: 179.47 E-value: 2.58e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    61 LRFMDRLLPAdwqvafGYIGLMLAATLLLRGAALVFNVLQAklfarLSKDIVYRIRLRLIERLR---HIALGEYETLGGG 137
Cdd:TIGR01842  30 LQVYDRVLTS------GSVPTLLMLTVLALGLYLFLGLLDA-----LRSFVLVRIGEKLDGALNqpiFAASFSATLRRGS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   138 SISAHLVTDLDTLDKFvgetlsrflvalLTLLGTAAI--LVWMHWQLaLLILLFNP----LVIWSTVQLGKrvkhLKKLE 211
Cdd:TIGR01842  99 GDGLQALRDLDQLRQF------------LTGPGLFAFfdAPWMPIYL-LVCFLLHPwigiLALGGAVVLVG----LALLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   212 NDSTAR-FTQALTETLEAIQEVRAGNRQGY------FLGRLGHRAQEVRDYAVASQWK-SDAAGRASGLlfqfgIDVFRA 283
Cdd:TIGR01842 162 NRATKKpLKEATEASIRANNLADSALRNAEvieamgMMGNLTKRWGRFHSKYLSAQSAaSDRAGMLSNL-----SKYFRI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   284 A---AMLT-----VLLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRINELLArADEPRYPPLRDPfAGR 355
Cdd:TIGR01842 237 VlqsLVLGlgaylAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLA-NYPSRDPAMPLP-EPE 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   356 TTVGIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHV 435
Cdd:TIGR01842 315 GHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHI 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   436 AVVLQHPALFNDSVRANLT-MGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:TIGR01842 395 GYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057   515 VVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543

ABCC_cytochrome_bd

cd03247

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

360-574

8.19e-46

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: 159.79 E-value: 8.19e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED--KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGlDCVREHVAV 437
Cdd:cd03247   1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLtmgrersdqacwraleiaqladgvrrlpqgldtvvgrsGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03247  80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDG 574
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

FetA

COG4619

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];

360-570

2.04e-45

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.60 E-value: 2.04e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:COG4619   1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFNDSVRANLtmgrERSDQACWRALEIAQLADGVRRLpqGLDT-VVGRSGVRLSGGQRQRLAIARMILAEPKVVIL 518
Cdd:COG4619  81 QEPALWGGTVRDNL----PFPFQLRERKFDRERALELLERL--GLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLL 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 519 DEATSALDAATEYALHQALGDFL--EGRTTLIVAH-RLSAVKQADRVLVFDGGHI 570
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209

PvdE

COG4615

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

69-581

5.81e-45

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: 167.67 E-value: 5.81e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  69 PADWQVAFGYIGLmLAATLLLRGAALVfnvlqakLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLD 148
Cdd:COG4615  45 AALARLLLLFAGL-LVLLLLSRLASQL-------LLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVR 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 149 TLDKFVgETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEA 228
Cdd:COG4615 117 TISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEG 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 229 IQEVR--AGNRQGYFLGRLGHRAQEVRDYAVAsqwksdaAGRASGLLFQFGIDVFRAA-AMLTVLLSDLSIGQMLAVFSY 305
Cdd:COG4615 196 FKELKlnRRRRRAFFDEDLQPTAERYRDLRIR-------ADTIFALANNWGNLLFFALiGLILFLLPALGWADPAVLSGF 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 306 ---LWFMIGPVEQLLGLQYAYYAAGGALQRINELLAR--ADEPRYPPLRDPFAGRTTVGIEVRGLDFAYGEDK-----VL 375
Cdd:COG4615 269 vlvLLFLRGPLSQLVGALPTLSRANVALRKIEELELAlaAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTL 348

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 376 EQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDsvranlTM 455
Cdd:COG4615 349 GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LL 422

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 456 GRERSDQAcwraleiAQLADGVRRLpqGLDTVV----GR-SGVRLSGGQRQRLAiarMILA--EPK-VVILDEATSALDA 527
Cdd:COG4615 423 GLDGEADP-------ARARELLERL--ELDHKVsvedGRfSTTDLSQGQRKRLA---LLVAllEDRpILVFDEWAADQDP 490

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 528 A-TEYALHQALGDF-LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG4615 491 EfRRVFYTELLPELkARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAA 546

ABC_cobalt_CbiO_domain1

cd03225

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

361-569

2.13e-43

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.

Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 154.16 E-value: 2.13e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAY--GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:cd03225   1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPA--LFNDSVRA-------NLTMGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMI 509
Cdd:cd03225  81 FQNPDdqFFGPTVEEevafgleNLGLPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 510 LAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGH 569
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211

CcmA

COG1131

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

360-582

7.09e-43

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 7.09e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcVREHVAVVL 439
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRANLT-------MGRERSDQACWRALEIAQLADGVRRLPQGLdtvvgrsgvrlSGGQRQRLAIARMILA 511
Cdd:COG1131  80 QEPALYPDlTVRENLRffarlygLPRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALLH 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 512 EPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221

ABCC_NFT1

cd03369

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

360-572

4.68e-42

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: 150.64 E-value: 4.68e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED--KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03369   7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGRERSDQACWRALEIAQladgvrrlpqgldtvvgrSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03369  87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSE------------------GGLNLSQGQRQLLCLARALLKRPRVLV 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAE 572
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203

ABC_NrtD_SsuB_transporters

cd03293

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

360-573

1.04e-41

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: 149.93 E-value: 1.04e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED----KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEigldcVREHV 435
Cdd:cd03293   1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFN-DSVRANLTMG--------RERSDQACwRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIA 506
Cdd:cd03293  76 GYVFQQDALLPwLTVLDNVALGlelqgvpkAEARERAE-ELLELVGLSGFENAYPH-----------QLSGGMRQRVALA 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDG--GHIAED 573
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215

ZnuC

COG1121

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

360-592

1.18e-41

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.62 E-value: 1.18e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEigldcVREHVAVVL 439
Cdd:COG1121   7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND---SVRANLTMGR-----------ERSDQACWRALE---IAQLADgvRRLPQgldtvvgrsgvrLSGGQRQR 502
Cdd:COG1121  82 QRAEVDWDfpiTVRDVVLMGRygrrglfrrpsRADREAVDEALErvgLEDLAD--RPIGE------------LSGGQQQR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAeDGDHQQLI 580
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLVA-HGPPEEVL 226

                       250
                ....*....|..
gi 15596057 581 AEGGLyARLYGH 592
Cdd:COG1121 227 TPENL-SRAYGG 237

ABCC_Protease_Secretion

cd03246

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

360-570

1.59e-41

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: 147.75 E-value: 1.59e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03246   1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLtmgrersdqacwraleiaqladgvrrlpqgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03246  81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15596057 518 LDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAVKQADRVLVFDGGHI 570
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173

GsiA

COG1123

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

330-581

3.37e-41

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: 156.22 E-value: 3.37e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 330 LQRINELLARADEPRYPPLRDPFAGRTTVGIEVRGLDFAY-----GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQL 404
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 405 LLGLYSAQRGSIRYGGVPLEEIGLDCVRE---HVAVVLQHP-ALFN--DSVRANLTMG---RERSDQAcWRALEIAQLAD 475
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDPySSLNprMTVGDIIAEPlrlHGLLSRA-ERRERVAELLE 389

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 476 GVrrlpqGLDT-VVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATeyalhQA-LGDFLE------GRTTL 547
Cdd:COG1123 390 RV-----GLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAqILNLLRdlqrelGLTYL 459

                       250       260       270
                ....*....|....*....|....*....|....*
gi 15596057 548 IVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG1123 460 FISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494

ABCC_MRP_domain1

cd03250

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

360-568

3.40e-40

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 145.30 E-value: 3.40e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK-----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvreH 434
Cdd:cd03250   1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 435 VAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:cd03250  68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 515 VVILDEATSALDAATEYAL-HQALGDFL-EGRTTLIVAHRLSAVKQADRVLVFDGG 568
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIfENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNG 203

DppF

COG1124

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

360-581

3.66e-40

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: 146.49 E-value: 3.66e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED----KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHV 435
Cdd:COG1124   2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPAL-FND--SVRANLT-----MGRERSDQACWRALEIAQLADGVR-RLPQgldtvvgrsgvRLSGGQRQRLAIA 506
Cdd:COG1124  82 QMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIA 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057 507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

360-573

1.18e-39

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.62 E-value: 1.18e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcvrehV 435
Cdd:COG1116   8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFN-DSVRANLTMG--------RERSDQACwRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIA 506
Cdd:COG1116  83 GVVFQEPALLPwLTVLDNVALGlelrgvpkAERRERAR-ELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDG--GHIAED 573
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVEE 222

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

360-581

1.36e-39

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 144.75 E-value: 1.36e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL--EEIGLDCVREHVAV 437
Cdd:COG1126   2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFND-SVRANLTMG-----RERSDQACWRALEI-AQ--LADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARM 508
Cdd:COG1126  82 VFQQFNLFPHlTVLENVTLApikvkKMSKAEAEERAMELlERvgLADKADAYPA-----------QLSGGQQQRVAIARA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 509 ILAEPKVVILDEATSALD--------------AAteyalhqalgdflEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAED 573
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDpelvgevldvmrdlAK-------------EGMTMVVVTHEMGfAREVADRVVFMDGGRIVEE 217


                ....*...
gi 15596057 574 GDHQQLIA 581
Cdd:COG1126 218 GPPEEFFE 225

ABC_PstB_phosphate_transporter

cd03260

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

360-579

1.96e-39

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: 143.86 E-value: 1.96e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQR-----GSIRYGGVPLEEIGLDCV--R 432
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLelR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 433 EHVAVVLQHPALFNDSVRANLTMG--------RERSDQACWRALEIAQLADGV-RRLpqgldtvvgrSGVRLSGGQRQRL 503
Cdd:cd03260  81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEVkDRL----------HALGLSGGQQQRL 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 504 AIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 579
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227

ABCC_SUR2

cd03288

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

374-589

4.43e-39

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: 143.90 E-value: 4.43e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANL 453
Cdd:cd03288  36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 454 TMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYAL 533
Cdd:cd03288 116 DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL 195

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 534 HQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA-EGGLYARL 589
Cdd:cd03288 196 QKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASL 252

ABC_DR_subfamily_A

cd03230

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

360-570

2.47e-38

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: 139.07 E-value: 2.47e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcVREHVAVVL 439
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRANLtmgrersdqacwraleiaqladgvrrlpqgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVIL 518
Cdd:cd03230  80 EEPSLYENlTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15596057 519 DEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHI 570
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173

ABC_Org_Solvent_Resistant

cd03261

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

360-581

4.85e-38

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: 140.33 E-value: 4.85e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCVREHVA 436
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRRMG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 437 VVLQHPALFND-SVRANLTMG-RERSDQACWRALEIAQLAdgvrrlpqgLDTvVGRSGVR------LSGGQRQRLAIARM 508
Cdd:cd03261  81 MLFQSGALFDSlTVFENVAFPlREHTRLSEEEIREIVLEK---------LEA-VGLRGAEdlypaeLSGGMKKRVALARA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 509 ILAEPKVVILDEATSALD--AATEYA-----LHQALGDflegrTTLIVAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLI 580
Cdd:cd03261 151 LALDPELLLYDEPTAGLDpiASGVIDdlirsLKKELGL-----TSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELR 225


                .
gi 15596057 581 A 581
Cdd:cd03261 226 A 226

ABC_MJ0796_LolCDE_FtsE

cd03255

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

360-570

6.01e-38

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: 139.55 E-value: 6.01e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCVR 432
Cdd:cd03255   1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELAAFR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 433 -EHVAVVLQHPALFND-SVRANLTM--------GRERSDQACWrALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQR 502
Cdd:cd03255  81 rRHIGFVFQSFNLLPDlTALENVELplllagvpKKERRERAEE-LLERVGLGDRLNHYPS-----------ELSGGQQQR 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDF--LEGRTTLIVAHRLSAVKQADRVLVFDGGHI 570
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218

FepC

COG1120

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

360-591

6.11e-38

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: 140.56 E-value: 6.11e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:COG1120   2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 Q-HPALFNDSVRANLTMGR-----------ERSDQACWRALE---IAQLADgvRRLPQgldtvvgrsgvrLSGGQRQRLA 504
Cdd:COG1120  82 QePPAPFGLTVRELVALGRyphlglfgrpsAEDREAVEEALErtgLEHLAD--RPVDE------------LSGGERQRVL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 505 IARMILAEPKVVILDEATSALDAATEYALHQALGDF--LEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227

                       250
                ....*....|
gi 15596057 582 EGGLyARLYG 591
Cdd:COG1120 228 PELL-EEVYG 236

ABC_6TM_exporters

cd07346

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

65-333

1.10e-37

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: 141.15 E-value: 1.10e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  65 DRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLV 144
Cdd:cd07346  27 DDVIPAGDLSLLLWIALLLLLLALLRA---LLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLT 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 145 TDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTE 224
Cdd:cd07346 104 SDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQE 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 225 TLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFS 304
Cdd:cd07346 184 SLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLA 263

                       250       260
                ....*....|....*....|....*....
gi 15596057 305 YLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd07346 264 YLGMLFGPIQRLANLYNQLQQALASLERI 292

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

360-581

1.31e-37

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 139.34 E-value: 1.31e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCVREHVA 436
Cdd:COG1127   6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRRIG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 437 VVLQHPALFND-SVRANLTMG-RERSDQAcwRAlEIAQLADGVRRLpqgldtvVGRSGVR------LSGGQRQRLAIARM 508
Cdd:COG1127  86 MLFQGGALFDSlTVFENVAFPlREHTDLS--EA-EIRELVLEKLEL-------VGLPGAAdkmpseLSGGMRKRVALARA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 509 ILAEPKVVILDEATSALD--AATEYA-----LHQALgdfleGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLI 580
Cdd:COG1127 156 LALDPEILLYDEPTAGLDpiTSAVIDelireLRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230


                .
gi 15596057 581 A 581
Cdd:COG1127 231 A 231

ABC_HisP_GlnQ

cd03262

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

360-570

3.40e-37

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: 137.28 E-value: 3.40e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL--EEIGLDCVREHVAV 437
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALF-NDSVRANLTMG----RERSDQAcwrALEIA-QLADGVrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILA 511
Cdd:cd03262  81 VFQQFNLFpHLTVLENITLApikvKGMSKAE---AEERAlELLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAM 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057 512 EPKVVILDEATSALDAateyalhQALGDFL--------EGRTTLIVAHRLS-AVKQADRVLVFDGGHI 570
Cdd:cd03262 153 NPKVMLFDEPTSALDP-------ELVGEVLdvmkdlaeEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213

ABC_ATPase

cd00267

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

361-569

6.88e-37

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: 134.68 E-value: 6.88e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQ 440
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 441 hpalfndsvranltmgrersdqacwraleiaqladgvrrlpqgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVILDE 520
Cdd:cd00267  81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15596057 521 ATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQA-DRVLVFDGGH 569
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157

ABC_Carb_Solutes_like

cd03259

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

360-574

7.43e-37

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: 136.50 E-value: 7.43e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEeiGLDCVREHVAVVL 439
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALF-NDSVRAN----LTMGRERSDQACWRALEIAQLAdgvrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:cd03259  79 QDYALFpHLTVAENiafgLKLRGVPKAEIRARVRELLELV--------GLEGLLNRYPHELSGGQQQRVALARALAREPS 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 515 VVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213

PLN03130

ABC transporter C family member; Provisional

374-589

1.38e-36

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 146.42 E-value: 1.38e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANL 453
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   454 TMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYAL 533
Cdd:PLN03130 1334 DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057   534 HQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA-EGGLYARL 589
Cdd:PLN03130 1414 QKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKM 1470

PLN03232

ABC transporter C family member; Provisional

341-589

1.52e-36

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.27 E-value: 1.52e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   341 DEPRYPPLRDPFAGrtTVGIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG 420
Cdd:PLN03232 1220 IENNRPVSGWPSRG--SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD 1297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   421 VPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQR 500
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQR 1377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   501 QRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLI 580
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457

                         250
                  ....*....|
gi 15596057   581 A-EGGLYARL 589
Cdd:PLN03232 1458 SrDTSAFFRM 1467

ABC_NikE_OppD_transporters

cd03257

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

360-574

7.52e-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: 7.52e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED----KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVRE-- 433
Cdd:cd03257   2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 434 -HVAVVLQHP-----------ALFNDSVRANltmGRERSDQAcwRALEIAQLADGV-------RRLPQgldtvvgrsgvR 494
Cdd:cd03257  82 kEIQMVFQDPmsslnprmtigEQIAEPLRIH---GKLSKKEA--RKEAVLLLLVGVglpeevlNRYPH-----------E 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 495 LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIA 571
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225


                ...
gi 15596057 572 EDG 574
Cdd:cd03257 226 EEG 228

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

359-579

9.54e-36

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.20 E-value: 9.54e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEeIGLDcVRE-HVAV 437
Cdd:COG1118   2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLP-PRErRVGF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALF-NDSVRAN----LTMGRERSDQAcwRA-----LEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIAR 507
Cdd:COG1118  80 VFQHYALFpHMTVAENiafgLRVRPPSKAEI--RArveelLELVQLEGLADRYPS-----------QLSGGQRQRVALAR 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 508 MILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221

LolD

COG1136

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];

360-573

2.26e-35

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.86 E-value: 2.26e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE---EIGLDCVR 432
Cdd:COG1136   5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslsERELARLR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 433 -EHVAVVLQHPALFND-SVRANLTM--------GRERSDQAcWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQR 502
Cdd:COG1136  85 rRHIGFVFQFFNLLPElTALENVALplllagvsRKERRERA-RELLERVGLGDRLDHRPS-----------QLSGGQQQR 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDF--LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAED 573
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225

NatA

COG4555

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

360-584

2.75e-35

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: 133.06 E-value: 2.75e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcVREHVAVVL 439
Cdd:COG4555   2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALF-NDSVRANLTM----GRERSDQACWRALEIAQLADgvrrLPQGLDTVVGRsgvrLSGGQRQRLAIARMILAEPK 514
Cdd:COG4555  81 DERGLYdRLTVRENIRYfaelYGLFDEELKKRIEELIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDPK 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 515 VVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAEGG 584
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQeVEALCDRVVILHKGKVVAQGSLDELREEIG 224

GsiA

COG1123

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

360-581

5.25e-35

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: 138.50 E-value: 5.25e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY--GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQ---RGSIRYGGVPLEEIGLDCVREH 434
Cdd:COG1123   5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 435 VAVVLQHPALFNDSVR---------ANLTMGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAI 505
Cdd:COG1123  85 IGMVFQDPMTQLNPVTvgdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057 506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232

ABC_Class3

cd03229

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

360-569

8.98e-35

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: 129.61 E-value: 8.98e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCV--REHVAV 437
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplRRRIGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALF-NDSVRANLTMGrersdqacwraleiaqladgvrrlpqgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVV 516
Cdd:cd03229  81 VFQDFALFpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 517 ILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGH 569
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178

ABC_Iron-Siderophores_B12_Hemin

cd03214

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

361-574

4.97e-34

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: 127.55 E-value: 4.97e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQ 440
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 441 hpALfndsvranltmgrersdqacwRALEIAQLADgvrrlpQGLDTvvgrsgvrLSGGQRQRLAIARMILAEPKVVILDE 520
Cdd:cd03214  81 --AL---------------------ELLGLAHLAD------RPFNE--------LSGGERQRVLLARALAQEPPILLLDE 123

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 521 ATSALDAATEYALHQALGDF--LEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180

ABC_tran

pfam00005

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

375-523

5.53e-34

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.22 E-value: 5.53e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFND-SVRANL 453
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057   454 TMGR---ERSDQACWRalEIAQLADGVRRLPQgLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATS 523
Cdd:pfam00005  81 RLGLllkGLSKREKDA--RAEEALEKLGLGDL-ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

360-550

7.19e-34

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: 127.98 E-value: 7.19e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcVREHVAVVL 439
Cdd:COG4133   3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAYLG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRANLTM-----GRERSDQACWRALEIAQLAdGVRRLPQGldtvvgrsgvRLSGGQRQRLAIARMILAEP 513
Cdd:COG4133  82 HADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLA-GLADLPVR----------QLSAGQKRRVALARLLLSPA 150

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15596057 514 KVVILDEATSALDAATEYALHQALGDFLEGRTTLIVA 550
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187

ABC_Metallic_Cations

cd03235

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

361-571

6.74e-33

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.

Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 125.34 E-value: 6.74e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEigldcVREHVAVVLQ 440
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 441 HPAL---FNDSVRANLTMGRERSdqacWRALEIAQLADgVRRLPQGLDTvVGRSGVR------LSGGQRQRLAIARMILA 511
Cdd:cd03235  76 RRSIdrdFPISVRDVVLMGLYGH----KGLFRRLSKAD-KAKVDEALER-VGLSELAdrqigeLSGGQQQRVLLARALVQ 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 512 EPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAV-KQADRVLVFDGGHIA 571
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211

MalK

COG3839

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

360-570

1.49e-32

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 1.49e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLeeIGLDCVREHVAVVL 439
Cdd:COG3839   4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRNIAMVF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALF-NDSVRANLTMG-----------RERSDQACwRALEIAQLADgvrRLPQGldtvvgrsgvrLSGGQRQRLAIAR 507
Cdd:COG3839  82 QSYALYpHMTVYENIAFPlklrkvpkaeiDRRVREAA-ELLGLEDLLD---RKPKQ-----------LSGGQRQRVALGR 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057 508 MILAEPKVVILDEATSALDAA------TE-YALHQALgdfleGRTTLIVAHRLS-AVKQADRVLVFDGGHI 570
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHDQVeAMTLADRIAVMNDGRI 212

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

330-582

2.14e-32

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 131.85 E-value: 2.14e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 330 LQRINELLARADEPRYPPLRDPFAGRTTVG-IEVRGLDFAYGEDKVL-EQLDLNIGAGEKVALVGASGGGKSTLVQLLLG 407
Cdd:COG4178 332 VDRLAGFEEALEAADALPEAASRIETSEDGaLALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 408 LYSAQRGSIRYggvPleeigldcVREHVAVVLQHPALFNDSVRANLT---MGRERSDQACWRALEIAQLADgvrrLPQGL 484
Cdd:COG4178 412 LWPYGSGRIAR---P--------AGARVLFLPQRPYLPLGTLREALLypaTAEAFSDAELREALEAVGLGH----LAERL 476

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 485 DTVVgRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGrTTLI-VAHRLSAVKQADRVL 563
Cdd:COG4178 477 DEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVIsVGHRSTLAAFHDRVL 554

                       250
                ....*....|....*....
gi 15596057 564 vfdggHIAEDGDHQQLIAE 582
Cdd:COG4178 555 -----ELTGDGSWQLLPAE 568

PstB

COG1117

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...

360-579

3.91e-32

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 3.91e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLL---LGLYSAQR--GSIRYGGVPLEEIGLDCV--R 432
Cdd:COG1117  12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGARveGEILLDGEDIYDPDVDVVelR 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 433 EHVAVVLQHPALFNDSVRANLTMG--------RERSDQACWRALEIAQLADGVR-RLpqgldtvvGRSGVRLSGGQRQRL 503
Cdd:COG1117  92 RRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALWDEVKdRL--------KKSALGLSGGQQQRL 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 504 AIARMILAEPKVVILDEATSALD-AAT---EYALHQALGDFlegrTTLIVAHRLSavkQA----DRVLVFDGGHIAEDGD 575
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDpISTakiEELILELKKDY----TIVIVTHNMQ---QAarvsDYTAFFYLGELVEFGP 236


                ....
gi 15596057 576 HQQL 579
Cdd:COG1117 237 TEQI 240

ABC_TM1139_LivF_branched

cd03224

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

360-582

9.20e-32

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: 122.54 E-value: 9.20e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-----VPLEEIgldcVREH 434
Cdd:cd03224   1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditgLPPHER----ARAG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 435 VAVVLQHPALFND-SVRANLTMGRERSDqacwRALEIAQLADGVRRLPQgLDTVVGRSGVRLSGGQRQRLAIARMILAEP 513
Cdd:cd03224  77 IGYVPEGRRIFPElTVEENLLLGAYARR----RAKRKARLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRP 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057 514 KVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

356-575

1.16e-31

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.98 E-value: 1.16e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 356 TTVGIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-----VPLEeigldc 430
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtgLPPE------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 431 vREHVAVVLQHPALF-NDSVRANLT-------MGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQR 502
Cdd:COG3842  76 -KRNVGMVFQDYALFpHLTVAENVAfglrmrgVPKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQR 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGD 575
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEeALALADRIAVMNDGRIEQVGT 219

PLN03232

ABC transporter C family member; Provisional

61-596

1.85e-31

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 130.87 E-value: 1.85e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    61 LRFMDRLLPAdwqvafgYIGLMLAATLLLrgaALVFNVL-QAKLFARLSKdIVYRIRLRLIERLRHIAL----GEYETLG 135
Cdd:PLN03232  328 LQSMQEGDPA-------WVGYVYAFLIFF---GVTFGVLcESQYFQNVGR-VGFRLRSTLVAAIFHKSLrlthEARKNFA 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   136 GGSISAHLVTDLDTLDKfVGETLS-------RFLVALLTL---LGTAAILvwmhWQLALLILL-FNPLVIwstvqlgKRV 204
Cdd:PLN03232  397 SGKVTNMITTDANALQQ-IAEQLHglwsapfRIIVSMVLLyqqLGVASLF----GSLILFLLIpLQTLIV-------RKM 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   205 KHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFLGRLghraQEVRDYAVAsqWKsdaagRASGLLFQFGIDVFRAA 284
Cdd:PLN03232  465 RKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRI----QGIRNEELS--WF-----RKAQLLSAFNSFILNSI 533

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   285 AMLTVLLS---------DLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRINELLARADE--PRYPPLRDpfa 353
Cdd:PLN03232  534 PVVVTLVSfgvfvllggDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERilAQNPPLQP--- 610

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   354 grTTVGIEVRGLDFAYG---EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSaqrgsiryggvPLEEIGLDc 430
Cdd:PLN03232  611 --GAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAETSSVV- 676

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   431 VREHVAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:PLN03232  677 IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVY 756

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   511 AEPKVVILDEATSALDAateYALHQA----LGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLY 586
Cdd:PLN03232  757 SNSDIYIFDDPLSALDA---HVAHQVfdscMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF 833

                         570
                  ....*....|
gi 15596057   587 ARLYGHLQQM 596
Cdd:PLN03232  834 KKLMENAGKM 843

CFTR_protein

TIGR01271

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

78-596

2.02e-31

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: 130.80 E-value: 2.02e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057     78 YIGLMLAATLL----LRGAALVFNVLQaklfarLSKdivyrirlRLIERLRHIAL----GEYETLGGGSISAHLVTDLDT 149
Cdd:TIGR01271  929 YIYVGTADSVLalgfFRGLPLVHTLLT------VSK--------RLHEQMLHSVLqapmAVLNTMKAGRILNRFTKDMAI 994

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    150 LDKFVGETLSRFLVALLTLLGtaAILVWMHWQLALLILLFNPLVIWSTVQLG--KRVKHLKKLENDSTARFTQALTETLE 227
Cdd:TIGR01271  995 IDDMLPLTLFDFIQLTLIVLG--AIFVVSVLQPYIFIAAIPVAVIFIMLRAYflRTSQQLKQLESEARSPIFSHLITSLK 1072

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    228 AIQEVRAGNRQGYFlGRLGHRAQEVRD-----YAVASQWksdaagrasgllFQFGIDV-----FRAAAMLTVLLSDLSIG 297
Cdd:TIGR01271 1073 GLWTIRAFGRQSYF-ETLFHKALNLHTanwflYLSTLRW------------FQMRIDIifvffFIAVTFIAIGTNQDGEG 1139

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    298 QMLAVFSYLWFMIGPveqllgLQYAYYAA---GGALQRINELLARADEPRYPPL----RDPFAGRTTVGIE--------- 361
Cdd:TIGR01271 1140 EVGIILTLAMNILST------LQWAVNSSidvDGLMRSVSRVFKFIDLPQEEPRpsggGGKYQLSTVLVIEnphaqkcwp 1213

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    362 ------VRGLDFAYGED--KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQrGSIRYGGVPLEEIGLDCVRE 433
Cdd:TIGR01271 1214 sggqmdVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRK 1292

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    434 HVAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEP 513
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    514 KVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYGHL 593
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAA 1452


                   ...
gi 15596057    594 QQM 596
Cdd:TIGR01271 1453 DRL 1455

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

358-574

2.91e-31

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.86 E-value: 2.91e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 358 VGIEVRGLDFAYGEDKVLEqldlnigaGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEE----IGLDCVRE 433
Cdd:cd03297   4 VDIEKRLPDFTLKIDFDLN--------EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 434 HVAVVLQHPALF-NDSVRANLTMGRERSDQACWRALEIAQLAdgvrRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAE 512
Cdd:cd03297  76 KIGLVFQQYALFpHLNVRENLAFGLKRKRNREDRISVDELLD----LL--GLDHLLNRYPAQLSGGEKQRVALARALAAQ 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 513 PKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:cd03297 150 PELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

360-583

3.25e-31

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 3.25e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:PRK13635   6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VLQHP--ALFNDSVRANLTMGRErsDQACWRALEIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:PRK13635  86 VFQNPdnQFVGATVQDDVAFGLE--NIGVPREEMVERVDQALRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  516 VILDEATSALDA-------ATEYALHQalgdflEGRTTLI-VAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEG 583
Cdd:PRK13635 162 IILDEATSMLDPrgrrevlETVRQLKE------QKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

359-574

4.80e-31

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: 120.91 E-value: 4.80e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvplEEIGLDCVRE-HVAV 437
Cdd:cd03296   2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVGF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFND-SVRANLTMG-RERSDQACWRALEIAQLADGVRRLPQgLDTVVGRSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:cd03296  79 VFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKV 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 516 VILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219

ABC_MetN_methionine_transporter

cd03258

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

370-581

7.03e-31

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: 120.38 E-value: 7.03e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 370 GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCVREHVAVVLQHPALFN 446
Cdd:cd03258  16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKARRRIGMIFQHFNLLS 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 447 D-SVRANLT-------MGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVIL 518
Cdd:cd03258  96 SrTVFENVAlpleiagVPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLC 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 519 DEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

357-575

8.09e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.25 E-value: 8.09e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  357 TVGIEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREH 434
Cdd:PRK13632   5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  435 VAVVLQHP--ALFNDSVRANLTMGRE--RSDQACWRALeIAQLADGVrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:PRK13632  85 IGIIFQNPdnQFIGATVEDDIAFGLEnkKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIASVLA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  511 AEPKVVILDEATSALDAATEYALHQALGDFLEGRT-TLI-VAHRLSAVKQADRVLVFDGGHIAEDGD 575
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGK 225

PTZ00265

multidrug resistance protein (mdr1); Provisional

360-588

5.99e-30

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 126.30 E-value: 5.99e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   360 IEVRGLDFAYGEDK---VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQR----------------------- 413
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgd 1245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   414 -------------------------------GSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANLTMGRERSD- 461
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATr 1325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   462 QACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL 541
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15596057   542 E--GRTTLIVAHRLSAVKQADRVLVFD-----GGHIAEDGDHQQLI-AEGGLYAR 588
Cdd:PTZ00265 1406 DkaDKTIITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLsVQDGVYKK 1460

DppD

COG0444

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

360-582

1.56e-29

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: 119.00 E-value: 1.56e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY----GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQR---GSIRYGGVPLEEIGLDCVR 432
Cdd:COG0444   2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 433 E----HVAVVLQHP--AL---------FNDSVRANLTMGRERSDQACWRALEIAQLADGVRRL---P-Qgldtvvgrsgv 493
Cdd:COG0444  82 KirgrEIQMIFQDPmtSLnpvmtvgdqIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPhE----------- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 494 rLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEyalHQALGDFLE-----GRTTLIVAHRLSAVKQ-ADRVLVFDG 567
Cdd:COG0444 151 -LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQ---AQILNLLKDlqrelGLAILFITHDLGVVAEiADRVAVMYA 226

                       250
                ....*....|....*
gi 15596057 568 GHIAEDGDHQQLIAE 582
Cdd:COG0444 227 GRIVEEGPVEELFEN 241

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

364-579

3.67e-29

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.44 E-value: 3.67e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   364 GLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEI---GLDCVREHVAVVLQ 440
Cdd:TIGR02769  16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   441 H-PALFN--DSVRA-------NLTMGRERSDQAcwRALEIAQL----ADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIA 506
Cdd:TIGR02769  96 DsPSAVNprMTVRQiigeplrHLTSLDESEQKA--RIAELLDMvglrSEDADKLPR-----------QLSGGQLQRINIA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057   507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 579
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQL 238

ABC_PotA_N

cd03300

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

360-570

6.61e-29

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: 114.64 E-value: 6.61e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLeeIGLDCVREHVAVVL 439
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRAN----LTMGRERSD---QACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILA 511
Cdd:cd03300  79 QNYALFPHlTVFENiafgLRLKKLPKAeikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVN 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 512 EPKVVILDEATSALDAATEY-------ALHQALgdfleGRTTLIVAHRLS-AVKQADRVLVFDGGHI 570
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKdmqlelkRLQKEL-----GITFVFVTHDQEeALTMSDRIAVMNKGKI 209

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

360-579

1.15e-28

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.11 E-value: 1.15e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvplEEIGLDCVRE-HVAVV 438
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHPALFN-----DSVRANLTM--GRERSDQACWRA-----LEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIA 506
Cdd:PRK10851  80 FQHYALFRhmtvfDNIAFGLTVlpRRERPNAAAIKAkvtqlLEMVQLAHLADRYPA-----------QLSGGQKQRVALA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224

ABC_PhnC_transporter

cd03256

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

360-582

1.19e-28

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 114.20 E-value: 1.19e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCVREHV 435
Cdd:cd03256   1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFND-SVRANLTMGReRSDQACWRAL-------EIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIAR 507
Cdd:cd03256  81 GMIFQQFNLIERlSVLENVLSGR-LGRRSTWRSLfglfpkeEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIAR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 508 MILAEPKVVILDEATSALDAATEyalHQALGDFLE-----GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASS---RQVMDLLKRinreeGITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAELTD 234


                .
gi 15596057 582 E 582
Cdd:cd03256 235 E 235

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

360-574

1.79e-28

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 117.36 E-value: 1.79e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-----VPLEeigldcvREH 434
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithVPAE-------NRH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  435 VAVVLQHPALF-NDSVRAN----LTMGRERSDQACWR---ALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIA 506
Cdd:PRK09452  88 VNTVFQSYALFpHMTVFENvafgLRMQKTPAAEITPRvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057  507 RMILAEPKVVILDEATSALDaateYALHQALGDFLE------GRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDG 574
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALD----YKLRKQMQNELKalqrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227

FtsE

COG2884

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

360-574

1.86e-28

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.22 E-value: 1.86e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCV---REHV 435
Cdd:COG2884   2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQ-HPALFNDSVRANLTMgrersdqacwrALEIAQLADGV--RRLPQGLDTVvGRSG------VRLSGGQRQRLAIA 506
Cdd:COG2884  82 GVVFQdFRLLPDRTVYENVAL-----------PLRVTGKSRKEirRRVREVLDLV-GLSDkakalpHELSGGEQQRVAIA 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVA-HRLSAVKQAD-RVLVFDGGHIAEDG 574
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVRDE 219

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

360-580

1.98e-28

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.65 E-value: 1.98e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDC--VREHVAV 437
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VLQHPALFND-SVRANLTMGRERSdqacwRALEIAQLADGVRRL--PQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:PRK09493  82 VFQQFYLFPHlTALENVMFGPLRV-----RGASKEEAEKQARELlaKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057  515 VVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLI 580
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLI 224

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

360-574

2.08e-28

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: 112.73 E-value: 2.08e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-----VPLEEIGldcvreh 434
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdLPPKDRD------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 435 VAVVLQHPALF-NDSVRAN----LTMGRERSDQACWRALEIAQLAdgvrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMI 509
Cdd:cd03301  74 IAMVFQNYALYpHMTVYDNiafgLKLRKVPKDEIDERVREVAELL--------QIEHLLDRKPKQLSGGQRQRVALGRAI 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 510 LAEPKVVILDEATSALDAATEYA-------LHQALgdfleGRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDG 574
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQmraelkrLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213

PhnC

COG3638

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...

360-591

3.03e-28

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 113.23 E-value: 3.03e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY-GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG---LDCVREHV 435
Cdd:COG3638   3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFND-SVRANLTMGR-----------------ERsdQACWRALEIAQLADgvrRLPQgldtvvgRSGvRLSG 497
Cdd:COG3638  83 GMIFQQFNLVPRlSVLTNVLAGRlgrtstwrsllglfppeDR--ERALEALERVGLAD---KAYQ-------RAD-QLSG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 498 GQRQRLAIARMILAEPKVVILDEATSALDAATEyalHQALGDFLE-----GRTTLIVAHRLS-AVKQADRVLVFDGGHIA 571
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTA---RQVMDLLRRiaredGITVVVNLHQVDlARRYADRIIGLRDGRVV 226

                       250       260
                ....*....|....*....|
gi 15596057 572 EDGDHQQLIAEggLYARLYG 591
Cdd:COG3638 227 FDGPPAELTDA--VLREIYG 244

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

360-583

3.41e-28

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: 112.92 E-value: 3.41e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLeeIGLdcvREHVAVVL 439
Cdd:cd03219   1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI--TGL---PPHEIARL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 ------QHPALFND-SVRANLTMGRERSDQACWRAL----EIAQLADGVRRLPQ--GLDTVVGRSGVRLSGGQRQRLAIA 506
Cdd:cd03219  76 gigrtfQIPRLFPElTVLENVMVAAQARTGSGLLLArarrEEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 507 RMILAEPKVVILDEATSALDAateyALHQALGDFLE-----GRTTLIVAHRLSAVKQ-ADRVLVFDGGhiaedgdhqQLI 580
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNP----EETEELAELIRelrerGITVLLVEHDMDVVMSlADRVTVLDQG---------RVI 222


                ...
gi 15596057 581 AEG 583
Cdd:cd03219 223 AEG 225

PRK11264

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

360-582

8.78e-28

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.15 E-value: 8.78e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGgvpleEIGLDC--------- 430
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG-----DITIDTarslsqqkg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  431 ----VREHVAVVLQHPALF-NDSVRANLTMG-----RERSDQACWRALEIaqLADgvrrlpqgldtvVGRSGV------R 494
Cdd:PRK11264  79 lirqLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkGEPKEEATARAREL--LAK------------VGLAGKetsyprR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  495 LSGGQRQRLAIARMILAEPKVVILDEATSALDA-------ATEYALHQalgdflEGRTTLIVAHRLS-AVKQADRVLVFD 566
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPelvgevlNTIRQLAQ------EKRTMVIVTHEMSfARDVADRAIFMD 218

                        250
                 ....*....|....*.
gi 15596057  567 GGHIAEDGDHQQLIAE 582
Cdd:PRK11264 219 QGRIVEQGPAKALFAD 234

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

362-573

1.02e-27

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 112.08 E-value: 1.02e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  362 VRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIgldcvREHVAVVLQH 441
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  442 PALFN-DSVRANLTMG-RERSDQACWRALEIAQLADGVRRLPQGldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:PRK11247  90 ARLLPwKKVIDNVGLGlKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  520 EATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAED 573
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 215

cbiO

PRK13637

energy-coupling factor transporter ATPase;

360-574

1.27e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 1.27e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYG-----EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL--EEIGLDCVR 432
Cdd:PRK13637   3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQHP--ALFNDSVR-------ANLTMGRERSDQACWRALEIAQLAdgvrrlpqgLDTVVGRSGVRLSGGQRQRL 503
Cdd:PRK13637  83 KKVGLVFQYPeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRV 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057  504 AIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAV-KQADRVLVFDGGHIAEDG 574
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227

MRP_assoc_pro

TIGR00957

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

300-587

1.68e-27

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 118.51 E-value: 1.68e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    300 LAVFSYLWFmigPVEQLLGLQYAYYAAGGALQRINELLARAD-EPRYPPlRDPFAGRTTVGIEVRGLDF--AYGEDKVLE 376
Cdd:TIGR00957  580 LALFNILRF---PLNILPMVISSIVQASVSLKRLRIFLSHEElEPDSIE-RRTIKPGEGNSITVHNATFtwARDLPPTLN 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    377 QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvreHVAVVLQHPALFNDSVRANLTMG 456
Cdd:TIGR00957  656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFG 722

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    457 RERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDA-ATEYALHQ 535
Cdd:TIGR00957  723 KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEH 802

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15596057    536 ALG--DFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYA 587
Cdd:TIGR00957  803 VIGpeGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856

MglA

COG1129

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

360-581

2.64e-27

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.50 E-value: 2.64e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL--------EEIGldcv 431
Cdd:COG1129   5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprdaQAAG---- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 432 rehVAVVLQHPALFND-SVRANLTMGRERS-----DqacWRAL--EIAQLADGVrrlpqGLD----TVVGrsgvRLSGGQ 499
Cdd:COG1129  81 ---IAIIHQELNLVPNlSVAENIFLGREPRrggliD---WRAMrrRARELLARL-----GLDidpdTPVG----DLSVAQ 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 500 RQRLAIARMILAEPKVVILDEATSALDAA-TEyALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVF-DGGHIAE--- 572
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEReVE-RLFRIIRRLKaQGVAIIYISHRLDEVFEiADRVTVLrDGRLVGTgpv 224

                       250
                ....*....|
gi 15596057 573 -DGDHQQLIA 581
Cdd:COG1129 225 aELTEDELVR 234

ABC_cobalt_CbiO_domain2

cd03226

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

361-570

3.81e-27

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: 108.88 E-value: 3.81e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPleeIGLDCVREHVAVVL 439
Cdd:cd03226   1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVM 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHP--ALFNDSVRANLTMGRERSDQACWRA------LEIAQLADgvrRLPQGLdtvvgrsgvrlSGGQRQRLAIARMILA 511
Cdd:cd03226  78 QDVdyQLFTDSVREELLLGLKELDAGNEQAetvlkdLDLYALKE---RHPLSL-----------SGGQKQRLAIAAALLS 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057 512 EPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLS-AVKQADRVLVFDGGHI 570
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEfLAKVCDRVLLLANGAI 204

ABC_Carb_Monos_I

cd03216

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

360-571

3.92e-27

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: 107.51 E-value: 3.92e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEeigldcvrehvavvl 439
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 qhpalFNDSVRAnltmgrersdqacwraleiaqLADGVRRLPQgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:cd03216  66 -----FASPRDA---------------------RRAGIAMVYQ------------LSVGERQMVEIARALARNARLLILD 107

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15596057 520 EATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIA 571
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

361-581

4.14e-27

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: 109.69 E-value: 4.14e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL-----EEIgldcVREHV 435
Cdd:COG0410   5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglppHRI----ARLGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFND-SVRANLTMGrersdqacwraleiAQLADGVRRLPQGLDTVV----------GRSGVRLSGGQRQRLA 504
Cdd:COG0410  81 GYVPEGRRIFPSlTVEENLLLG--------------AYARRDRAEVRADLERVYelfprlkerrRQRAGTLSGGEQQMLA 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 505 IARMILAEPKVVILDEATSALdaateyA--LHQALGDFL-----EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDH 576
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL------AplIVEEIFEIIrrlnrEGVTILLVEQNARFALEiADRAYVLERGRIVLEGTA 220


                ....*
gi 15596057 577 QQLIA 581
Cdd:COG0410 221 AELLA 225

PLN03130

ABC transporter C family member; Provisional

300-589

4.53e-27

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 117.15 E-value: 4.53e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   300 LAVFSYLWFmigPVEQLLGLQYAYYAAGGALQRINELLA---RADEPRyPPLrDPfagrTTVGIEVRGLDFAY---GEDK 373
Cdd:PLN03130  561 LSLFAVLRF---PLFMLPNLITQAVNANVSLKRLEELLLaeeRVLLPN-PPL-EP----GLPAISIKNGYFSWdskAERP 631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGlysaqrgsirygGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANL 453
Cdd:PLN03130  632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG------------ELPPRSDASVVIRGTVAYVPQVSWIFNATVRDNI 699

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   454 TMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDA-ATEYA 532
Cdd:PLN03130  700 LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQV 779

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057   533 LHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:PLN03130  780 FDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

360-574

7.96e-27

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: 108.07 E-value: 7.96e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVplEEIGLDCVREHVAVVL 439
Cdd:cd03268   1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFNdsvraNLTmGRErsdqacwrALEIAQLADGVR--RLPQGLDTV----VGRSGVR-LSGGQRQRLAIARMILAE 512
Cdd:cd03268  79 EAPGFYP-----NLT-ARE--------NLRLLARLLGIRkkRIDEVLDVVglkdSAKKKVKgFSLGMKQRLGIALALLGN 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057 513 PKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208

PTZ00265

multidrug resistance protein (mdr1); Provisional

360-565

1.21e-26

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 115.90 E-value: 1.21e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   360 IEVRGLDFAYGEDKVLE---QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGV-PLEEIGLDCVREHV 435
Cdd:PTZ00265  383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKI 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   436 AVVLQHPALFNDSVRANLTMG---------------------------RERSDQACWRAL-------------------- 468
Cdd:PTZ00265  463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkRNSCRAKCAGDLndmsnttdsneliemrknyq 542

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   469 -----EIAQLA------DGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQAL 537
Cdd:PTZ00265  543 tikdsEVVDVSkkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622

                         250       260       270
                  ....*....|....*....|....*....|
gi 15596057   538 GDFL--EGRTTLIVAHRLSAVKQADRVLVF 565
Cdd:PTZ00265  623 NNLKgnENRITIIIAHRLSTIRYANTIFVL 652

AbcC

COG1135

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];

360-575

1.25e-26

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 1.25e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLD--FAYGEDKV--LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCVR 432
Cdd:COG1135   2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 433 EHVAVVLQHPALFND-SVRANLTMgrersdqacwrALEIA-----QLADGVRRLpqgLDtVVGRSG------VRLSGGQR 500
Cdd:COG1135  82 RKIGMIFQHFNLLSSrTVAENVAL-----------PLEIAgvpkaEIRKRVAEL---LE-LVGLSDkadaypSQLSGGQK 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 501 QRLAIARMILAEPKVVILDEATSALDAATEYA-------LHQALGdfLegrTTLIVAHRLSAVKQ-ADRVLVFDGGHIAE 572
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSildllkdINRELG--L---TIVLITHEMDVVRRiCDRVAVLENGRIVE 221


                ...
gi 15596057 573 DGD 575
Cdd:COG1135 222 QGP 224

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

368-574

1.33e-26

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.66 E-value: 1.33e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-----VPLEEIGldcvrehVAVVLQHP 442
Cdd:PRK11000  12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndVPPAERG-------VGMVFQSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  443 ALF-NDSVRANLTMG-------RERSDQACWRALEIAQLADGVRRLPQGLdtvvgrsgvrlSGGQRQRLAIARMILAEPK 514
Cdd:PRK11000  85 ALYpHLSVAENMSFGlklagakKEEINQRVNQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVAEPS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057  515 VVILDEATSALDAA------TEYA-LHQALgdfleGRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDG 574
Cdd:PRK11000 154 VFLLDEPLSNLDAAlrvqmrIEISrLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216

ABC_membrane

pfam00664

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

62-313

1.37e-26

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: 109.27 E-value: 1.37e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    62 RFMDRLLPaDWQVAFGYIGLMLAATLLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISA 141
Cdd:pfam00664  24 RILDVLLP-DGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   142 HLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQA 221
Cdd:pfam00664 103 RLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   222 LTETLEAIQEVRAGNRQGYFLgrlgHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAML----TVLLSDLSIG 297
Cdd:pfam00664 183 AEESLSGIRTVKAFGREEYEL----EKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWfgayLVISGELSVG 258

                         250
                  ....*....|....*.
gi 15596057   298 QMLAVFSYLWFMIGPV 313
Cdd:pfam00664 259 DLVAFLSLFAQLFGPL 274

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

329-575

2.43e-26

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 2.43e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 329 ALQRInELLARADEPRYPPLRDPFAGRT--TVgIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLL 406
Cdd:COG0488 285 ALEKL-EREEPPRRDKTVEIRFPPPERLgkKV-LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 407 GLYSAQRGSIRYG-GVpleeigldcvreHVAVVLQHPALFNDSvranltmgrersdqacWRALE-IAQLADGVRRL---- 480
Cdd:COG0488 363 GELEPDSGTVKLGeTV------------KIGYFDQHQEELDPD----------------KTVLDeLRDGAPGGTEQevrg 414

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 481 --------PQGLDTVVGrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFlEGrTTLIVAH- 551
Cdd:COG0488 415 ylgrflfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHd 488

                       250       260
                ....*....|....*....|....*..
gi 15596057 552 R--LSAVkqADRVLVFDGGHIAE-DGD 575
Cdd:COG0488 489 RyfLDRV--ATRILEFEDGGVREyPGG 513

ABC_6TM_LmrA_like

cd18551

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

81-333

2.57e-26

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: 109.06 E-value: 2.57e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  81 LMLAATLLLrgAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSR 160
Cdd:cd18551  39 LALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQ 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 161 FLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGY 240
Cdd:cd18551 117 LVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEER 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 241 FLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQfgidvfraAAMLTVLL--------SDLSIGQMLAVFSYLWFMIGP 312
Cdd:cd18551 197 ETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ--------LALLVVLGvggarvasGALTVGTLVAFLLYLFQLITP 268

                       250       260
                ....*....|....*....|.
gi 15596057 313 VEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18551 269 LSQLSSFFTQLQKALGALERI 289

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

360-577

2.73e-26

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.79 E-value: 2.73e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIR-------YGGVPLEEIGLDcVR 432
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRE-LR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQH----PALfndSVRANLTMGRER-----SDQACWRALEIA---QLADGVRRLPQgldtvvgrsgvRLSGGQR 500
Cdd:PRK11124  82 RNVGMVFQQynlwPHL---TVQQNLIEAPCRvlglsKDQALARAEKLLerlRLKPYADRFPL-----------HLSGGQQ 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  501 QRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQ 577
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEvARKTASRVVYMENGHIVEQGDAS 226

cbiO

PRK13650

energy-coupling factor transporter ATPase;

360-584

3.66e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 3.66e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDK---VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVA 436
Cdd:PRK13650   5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHP------ALFNDSVRANL--------TMgRERSDQAcwraLEIAQLADGVRRLPqgldtvvgrsgVRLSGGQRQR 502
Cdd:PRK13650  85 MVFQNPdnqfvgATVEDDVAFGLenkgipheEM-KERVNEA----LELVGMQDFKEREP-----------ARLSGGQKQR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLI 580
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228


                 ....
gi 15596057  581 AEGG 584
Cdd:PRK13650 229 SRGN 232

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

360-592

4.24e-26

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 4.24e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:PRK13548   3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPAL-FNDSVRANLTMGR-------ERSDQACWRALEIAqladgvrrlpqGLDTVVGRSGVRLSGGQRQRLAIARmILA 511
Cdd:PRK13548  83 QHSSLsFPFTVEEVVAMGRaphglsrAEDDALVAAALAQV-----------DLAHLAGRDYPQLSGGEQQRVQLAR-VLA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  512 -------EPKVVILDEATSALD---------AATEYALHQALGdflegrtTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:PRK13548 151 qlwepdgPPRWLLLDEPTSALDlahqhhvlrLARQLAHERGLA-------VIVVLHDLNlAARYADRIVLLHQGRLVADG 223

                        250
                 ....*....|....*...
gi 15596057  575 DHQQLIAEGGLyARLYGH 592
Cdd:PRK13548 224 TPAEVLTPETL-RRVYGA 240

ABCC_CFTR2

cd03289

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

360-596

4.29e-26

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.

Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 108.02 E-value: 4.29e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED--KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQrGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:cd03289   3 MTVKDLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03289  82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGLYARLYGHLQQM 596
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240

ThiQ

COG3840

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

360-581

7.37e-26

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 7.37e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVleQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcvREHVAVVL 439
Cdd:COG3840   2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSMLF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRANLTMGRE------RSDQAcwRALEIAQ---LADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMI 509
Cdd:COG3840  78 QENNLFPHlTVAQNIGLGLRpglkltAEQRA--QVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCL 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 510 LAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

360-567

7.76e-26

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: 104.16 E-value: 7.76e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVL-EQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYggvpleeigldCVREHVAVV 438
Cdd:cd03223   1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPALFNDSVRanltmgrersDQAC--WraleiaqladgvrrlpqglDTVvgrsgvrLSGGQRQRLAIARMILAEPKVV 516
Cdd:cd03223  70 PQRPYLPLGTLR----------EQLIypW-------------------DDV-------LSGGEQQRLAFARLLLHKPKFV 113

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15596057 517 ILDEATSALDAATEYALHQALGDFLegrTTLI-VAHRLSAVKQADRVLVFDG 567
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELG---ITVIsVGHRPSLWKFHDRVLDLDG 162

ABC_6TM_MsbA_like

cd18552

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

63-333

8.87e-26

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: 107.51 E-value: 8.87e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  63 FMDRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAH 142
Cdd:cd18552  25 LLDDIFVEKDLEALLLVPLAIIGLFLLRG---LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISR 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 143 LVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQAL 222
Cdd:cd18552 102 ITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVL 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 223 TETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAV 302
Cdd:cd18552 182 QETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISF 261

                       250       260       270
                ....*....|....*....|....*....|.
gi 15596057 303 FSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18552 262 ITALLLLYQPIKRLSNVNANLQRGLAAAERI 292

PTZ00243

ABC transporter; Provisional

374-580

1.28e-25

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.56 E-value: 1.28e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANL 453
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   454 TMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVIL-DEATSALDAATEYA 532
Cdd:PTZ00243 1405 DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQ 1484

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 15596057   533 LHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLI 580
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532

ABC_ModC_like

cd03299

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

360-580

2.01e-25

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: 105.11 E-value: 2.01e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKvLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEigLDCVREHVAVVL 439
Cdd:cd03299   1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALF-NDSVRANLTMG----RERSDQACWRALEIAQLAdgvrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:cd03299  78 QNYALFpHMTVYKNIAYGlkkrKVDKKEIERKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057 515 VVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLI 580
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218

ABC_OpuCA_Osmoprotection

cd03295

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

360-581

2.61e-25

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: 104.69 E-value: 2.61e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:cd03295   1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPALF-NDSVRANLTM-------GRERSDQacwRALEIAQLADgvrrLPQGldTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:cd03295  81 IQQIGLFpHMTVEENIALvpkllkwPKEKIRE---RADELLALVG----LDPA--EFADRYPHELSGGQQQRVGVARALA 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057 511 AEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225

AppF

COG4608

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...

379-582

3.28e-25

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 106.74 E-value: 3.28e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 379 DLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG---LDCVREHVAVVLQHP-ALFN------DS 448
Cdd:COG4608  38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyASLNprmtvgDI 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 449 VRA-----NLTMGRERSDqacwRALEIAQL----ADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:COG4608 118 IAEplrihGLASKAERRE----RVAELLELvglrPEHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVCD 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057 520 EATSALDAATeyalhQA-----LGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:COG4608 183 EPVSALDVSI-----QAqvlnlLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248

ArtP

COG4161

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];

359-576

3.50e-25

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 3.50e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-------VPLEEIGLDcV 431
Cdd:COG4161   2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqKPSEKAIRL-L 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 432 REHVAVVLQH----PALfndSVRANLT------MGRERSdQACWRALEIA---QLADGVRRLPQgldtvvgrsgvRLSGG 498
Cdd:COG4161  81 RQKVGMVFQQynlwPHL---TVMENLIeapckvLGLSKE-QAREKAMKLLarlRLTDKADRFPL-----------HLSGG 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 499 QRQRLAIARMILAEPKVVILDEATSALD---AATEYALHQALGDflEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQ--TGITQVIVTHEVEfARKVASQVVYMEKGRIIEQG 223


                ..
gi 15596057 575 DH 576
Cdd:COG4161 224 DA 225

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

360-574

5.20e-25

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: 103.04 E-value: 5.20e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGeKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGlDCVREHVAVVL 439
Cdd:cd03264   1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALF-NDSVRANL-TMGR------ERSDQACWRALEIAQLADGVRRLPQGLdtvvgrsgvrlSGGQRQRLAIARMILA 511
Cdd:cd03264  79 QEFGVYpNFTVREFLdYIAWlkgipsKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVG 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057 512 EPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

364-573

6.81e-25

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 104.38 E-value: 6.81e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  364 GLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEI---GLDCVREHVAVVLQ 440
Cdd:PRK10419  17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  441 H-PALFN--DSVRA-------NLT----MGRERSDQACWRALEIA-QLADgvrRLPQgldtvvgrsgvRLSGGQRQRLAI 505
Cdd:PRK10419  97 DsISAVNprKTVREiireplrHLLsldkAERLARASEMLRAVDLDdSVLD---KRPP-----------QLSGGQLQRVCL 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057  506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTT--LIVAHRLSAVKQ-ADRVLVFDGGHIAED 573
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVET 233

ABC_6TM_YknU_like

cd18542

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

78-316

1.20e-24

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: 104.05 E-value: 1.20e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  78 YIGLMLAATLLlRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGET 157
Cdd:cd18542  41 LALLILGVALL-RG---VFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFG 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 158 LSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNR 237
Cdd:cd18542 117 LVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAR 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 238 QGYFLGRLGHRAQEVRDyavasqwKSDAAGRASGLLFQFgIDVFRAAAMLTVLL--------SDLSIGQMLAVFSYLWFM 309
Cdd:cd18542 197 EDYEIEKFDKENEEYRD-------LNIKLAKLLAKYWPL-MDFLSGLQIVLVLWvggylvinGEITLGELVAFISYLWML 268


                ....*..
gi 15596057 310 IGPVEQL 316
Cdd:cd18542 269 IWPVRQL 275

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

360-563

1.85e-24

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 1.85e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:PRK10247   8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALFNDSVRANLTMGRERSDQacwrALEIAQLADGVRR--LPqglDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:PRK10247  88 QTPTLFGDTVYDNLIFPWQIRNQ----QPDPAIFLDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15596057  518 LDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQADRVL 563
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVI 208

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

377-581

3.09e-24

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 3.09e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  377 QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVpleeiglDCV-----REHVAVVLQHPALFND-SVR 450
Cdd:PRK10771  17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-------DHTttppsRRPVSMLFQENNLFSHlTVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  451 ANLTMG-----RERSDQACwraleiaQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSAL 525
Cdd:PRK10771  90 QNIGLGlnpglKLNAAQRE-------KLHAIARQM--GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  526 DAATEYALHQALGDFLEGR--TTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219

ABC_6TM_exporter_like

cd18563

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

78-316

4.19e-24

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

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 102.59 E-value: 4.19e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  78 YIGLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGET 157
Cdd:cd18563  45 LVLGLAGAYVL----SALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 158 LSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNR 237
Cdd:cd18563 121 LPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057 238 QGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLWFMIGPVEQL 316
Cdd:cd18563 201 EKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWL 279

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

361-583

4.88e-24

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];

Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 101.65 E-value: 4.88e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEeiGL---DCVREHVAV 437
Cdd:COG0411   6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT--GLpphRIARLGIAR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFND-SVRANLTMGRERSDQACWRAL------------EIAQLADGV-RRLpqGLDTVVGRSGVRLSGGQRQRL 503
Cdd:COG0411  84 TFQNPRLFPElTVLENVLVAAHARLGRGLLAAllrlprarreerEARERAEELlERV--GLADRADEPAGNLSYGQQRRL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 504 AIARMILAEPKVVILDEATSALDAateyALHQALGDFL------EGRTTLIVAHRLSAVKQ-ADRVLVFDGGhiaedgdh 576
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNP----EETEELAELIrrlrdeRGITILLIEHDMDLVMGlADRIVVLDFG-------- 229


                ....*..
gi 15596057 577 qQLIAEG 583
Cdd:COG0411 230 -RVIAEG 235

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

360-568

5.18e-24

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: 100.48 E-value: 5.18e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCV----REH 434
Cdd:cd03290   1 VQVTNGYFSWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 435 VAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:cd03290  81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 515 VVILDEATSALDA-ATEYALHQALGDFL--EGRTTLIVAHRLSAVKQADRVLVFDGG 568
Cdd:cd03290 161 IVFLDDPFSALDIhLSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217

PRK14243

phosphate transporter ATP-binding protein; Provisional

355-562

8.75e-24

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 8.75e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  355 RTTVGIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQL---LLGLYSAQR--GSIRYGGVPLEEIGLD 429
Cdd:PRK14243   6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRveGKVTFHGKNLYAPDVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  430 C--VREHVAVVLQHPALFNDSVRANLTMG------RERSDQACWRALEIAQLADGVR-RLPQgldtvvgrSGVRLSGGQR 500
Cdd:PRK14243  86 PveVRRRIGMVFQKPNPFPKSIYDNIAYGaringyKGDMDELVERSLRQAALWDEVKdKLKQ--------SGLSLSGGQQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057  501 QRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLsavKQADRV 562
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM---QQAARV 216

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

390-582

9.60e-24

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 102.19 E-value: 9.60e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   390 LVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcvREHVAVVLQHPALF-NDSVRANLTMG-------RERSD 461
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGlkmrkvpRAEIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   462 QACWRALEIAQLADGVRRLPqgldtvvgrsgVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL 541
Cdd:TIGR01187  79 PRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15596057   542 E--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:TIGR01187 148 EqlGITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

368-565

9.78e-24

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 9.78e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvREHVAVVLQH---PAL 444
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevPDS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 FNDSVRANLTMGRERsDQACWRALEI---AQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEA 521
Cdd:NF040873  70 LPLTVRDLVAMGRWA-RRGLWRRLTRddrAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15596057  522 TSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQADRVLVF 565
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191

PRK14239

phosphate transporter ATP-binding protein; Provisional

360-579

1.07e-23

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 1.07e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLL-----LGLYSAQRGSIRYGGVPLEEIGLDCV--R 432
Cdd:PRK14239   6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTVdlR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQHPALFNDSVRANLTMG--------RERSDQACWRALEIAQLADGVR-RLPQgldtvvgrSGVRLSGGQRQRL 503
Cdd:PRK14239  86 KEIGMVFQQPNPFPMSIYENVVYGlrlkgikdKQVLDEAVEKSLKGASIWDEVKdRLHD--------SALGLSGGQQQRV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  504 AIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRL-SAVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqQASRISDRTGFFLDGDLIEYNDTKQM 234

ABC_6TM_Rv0194_D2_like

cd18546

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

67-333

1.17e-23

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: 101.41 E-value: 1.17e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  67 LLPADWQVAFGYIGLMLAATLllrgAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTD 146
Cdd:cd18546  30 VRAGDLGVLLLAAAAYLAVVL----AGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSD 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 147 LDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETL 226
Cdd:cd18546 106 IDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETL 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 227 EAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQwksdaagRASGLLFQFgIDVFRAAAMLTVLL--------SDLSIGQ 298
Cdd:cd18546 186 AGIRVVQAFRRERRNAERFAELSDDYRDARLRAQ-------RLVAIYFPG-VELLGNLATAAVLLvgawrvaaGTLTVGV 257

                       250       260       270
                ....*....|....*....|....*....|....*
gi 15596057 299 MLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18546 258 LVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292

cbiO

PRK13644

energy-coupling factor transporter ATPase;

375-585

1.31e-23

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 1.31e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG-LDCVREHVAVVLQHP--ALFNDSVRA 451
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPetQFVGRTVEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  452 NLTMGRErsdQACWRALEIAQLADgvRRLPQ-GLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATE 530
Cdd:PRK13644  98 DLAFGPE---NLCLPPIEIRKRVD--RALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  531 YALHQALGDFLE-GRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAEGGL 585
Cdd:PRK13644 173 IAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228

ABC_6TM_exporter_like

cd18564

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

55-333

2.08e-23

Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 101.05 E-value: 2.08e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  55 GKGDGALRFMDRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETL 134
Cdd:cd18564  32 DKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRG---LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRR 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 135 GGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDS 214
Cdd:cd18564 109 RTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRR 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 215 TARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQE-VRDYAVASQWKSdAAGRASGLLFQFGIDVFRAAAMLTVLLSD 293
Cdd:cd18564 189 EGALASVAQESLSAIRVVQAFGREEHEERRFARENRKsLRAGLRAARLQA-LLSPVVDVLVAVGTALVLWFGAWLVLAGR 267

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15596057 294 LSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18564 268 LTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

360-585

2.24e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.20 E-value: 2.24e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:PRK13647   5 IEVEDLHFRYKDGtKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHP--ALFNDSV-------RANLTMGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMI 509
Cdd:PRK13647  85 FQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  510 LAEPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGD-----HQQLIAE 582
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDkslltDEDIVEQ 233


                 ...
gi 15596057  583 GGL 585
Cdd:PRK13647 234 AGL 236

ABC_6TM_exporter_like

cd18550

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

67-333

2.26e-23

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 100.63 E-value: 2.26e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  67 LLPADWQVAFGYIGLMLAATLllrgAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTD 146
Cdd:cd18550  30 LPQGDLGLLVLLALGMVAVAV----ASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNND 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 147 LDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETL 226
Cdd:cd18550 106 VGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETL 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 227 EA--IQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwKSDAAGRAS----GLLFQFGIDVFRAAAMLTVLLSDLSIGQML 300
Cdd:cd18550 186 SVsgALLVKLFGREDDEAARFARRSRELRDLGV----RQALAGRWFfaalGLFTAIGPALVYWVGGLLVIGGGLTIGTLV 261

                       250       260       270
                ....*....|....*....|....*....|...
gi 15596057 301 AVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18550 262 AFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294

cbiO

PRK13640

energy-coupling factor transporter ATPase;

360-574

2.72e-23

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.26 E-value: 2.72e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLY---SAQRGSIRYGGVPLEEIGLDCVREH 434
Cdd:PRK13640   6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  435 VAVVLQHP------ALFNDSVR---ANLTMGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAI 505
Cdd:PRK13640  86 VGIVFQNPdnqfvgATVGDDVAfglENRAVPRPEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057  506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQADRVLVFDGGHIAEDG 574
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

360-583

2.85e-23

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: 98.35 E-value: 2.85e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLD--FAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEiGLDCVREHVAV 437
Cdd:cd03263   1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFND-SVRANLTM-----GRERSDqacwRALEIAQLADGVRrLPQGLDTVVGRsgvrLSGGQRQRLAIARMILA 511
Cdd:cd03263  80 CPQFDALFDElTVREHLRFyarlkGLPKSE----IKEEVELLLRVLG-LTDKANKRART----LSGGMKRKLSLAIALIG 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 512 EPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQ-ADRVLVFDGGhiaedgdhqQLIAEG 583
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG---------KLRCIG 214

ABC_ThiQ_thiamine_transporter

cd03298

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

360-574

3.67e-23

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: 97.95 E-value: 3.67e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVleQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVplEEIGLDCVREHVAVVL 439
Cdd:cd03298   1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV--DVTAAPPADRPVSMLF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRANLTMGR-------ERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILA 511
Cdd:cd03298  77 QENNLFAHlTVEQNVGLGLspglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVR 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 512 EPKVVILDEATSALDAATEYALHQALGDFLEGR--TTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211

PTZ00243

ABC transporter; Provisional

355-594

4.08e-23

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.86 E-value: 4.08e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   355 RTTVGIEVRGLDFAYGEDKVL-EQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIryggvpleeigldCVRE 433
Cdd:PTZ00243  655 RSAKTPKMKTDDFFELEPKVLlRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAER 721

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   434 HVAVVLQHPALFNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEP 513
Cdd:PTZ00243  722 SIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANR 801

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   514 KVVILDEATSALDAAT-EYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLiAEGGLYARLYGH 592
Cdd:PTZ00243  802 DVYLLDDPLSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADF-MRTSLYATLAAE 880


                  ..
gi 15596057   593 LQ 594
Cdd:PTZ00243  881 LK 882

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

340-581

4.60e-23

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: 103.23 E-value: 4.60e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 340 ADEPRYPPlrDPFAGRTTVGIEVRGLDFAY-----------GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL 408
Cdd:COG4172 258 AAEPRGDP--RPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL 335

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 409 YSAQrGSIRYGGVPLEEIG---LDCVREHVAVVLQHP--ALfndSVRanLTMGR----------------ERSDQACwRA 467
Cdd:COG4172 336 IPSE-GEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPfgSL---SPR--MTVGQiiaeglrvhgpglsaaERRARVA-EA 408

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 468 LEIAQLADGVR-RLPQgldtvvgrsgvRLSGGQRQRLAIAR-MILaEPKVVILDEATSALDAATeyalhQA-----LGDf 540
Cdd:COG4172 409 LEEVGLDPAARhRYPH-----------EFSGGQRQRIAIARaLIL-EPKLLVLDEPTSALDVSV-----QAqildlLRD- 470

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15596057 541 LEGR---TTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG4172 471 LQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

360-585

4.87e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 4.87e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDK--VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAV 437
Cdd:PRK13648   8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VLQHP--ALFNDSVRANLTMGRERsdqacwralEIAQLADGVRRLPQGLDTV--VGRSGVR---LSGGQRQRLAIARMIL 510
Cdd:PRK13648  88 VFQNPdnQFVGSIVKYDVAFGLEN---------HAVPYDEMHRRVSEALKQVdmLERADYEpnaLSGGQKQRVAIAGVLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  511 AEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVA--HRLSAVKQADRVLVFDGGHIAEDG------DHQQLIAE 582
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGtpteifDHAEELTR 238


                 ...
gi 15596057  583 GGL 585
Cdd:PRK13648 239 IGL 241

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

360-574

6.92e-23

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 6.92e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPAL-FNDSVRANLTMGR-------ERSDQACWRALEIAQLADGVRRLpqgldtvVGRSGVRLSGGQRQRLAIARMILA 511
Cdd:PRK09536  84 QDTSLsFEFDVRQVVEMGRtphrsrfDTWTETDRAAVERAMERTGVAQF-------ADRPVTSLSGGERQRVLLARALAQ 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  512 EPKVVILDEATSALD---AATEYALHQALGDflEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDG 574
Cdd:PRK09536 157 ATPVLLLDEPTASLDinhQVRTLELVRRLVD--DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

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

62-333

7.71e-23

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: 98.71 E-value: 7.71e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  62 RFMDRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISA 141
Cdd:cd18576  21 QLIDAALGGGDTASLNQIALLLLGLFLLQA---VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 142 HLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQA 221
Cdd:cd18576  98 RLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTI 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 222 LTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwksdAAGRASGLLFQFGIDVFRAA-------AMLTVLLSDL 294
Cdd:cd18576 178 VEETLQGIRVVKAFTREDYEIERYRKALERVVKLAL-------KRARIRALFSSFIIFLLFGAivavlwyGGRLVLAGEL 250

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15596057 295 SIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18576 251 TAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

377-581

1.95e-22

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis

Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 99.02 E-value: 1.95e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 377 QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLeeigLDCVRE--------HVAVVLQHPALFND- 447
Cdd:COG4148  17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL----QDSARGiflpphrrRIGYVFQEARLFPHl 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 448 SVRANLTMGRERsdqaCWRALEIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDA 527
Cdd:COG4148  93 SVRGNLLYGRKR----APRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057 528 ATeyalHQALGDFLE------GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:COG4148 167 AR----KAEILPYLErlrdelDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

361-583

2.45e-22

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 96.05 E-value: 2.45e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEeiGL---DCVREHVAV 437
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT--KLpphERARAGIAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   438 VLQHPALFND-SVRANLTMGRERsdqacwraleiaqLADGVRRLPQG-------LDTVVGRSGVRLSGGQRQRLAIARMI 509
Cdd:TIGR03410  80 VPQGREIFPRlTVEENLLTGLAA-------------LPRRSRKIPDEiyelfpvLKEMLGRRGGDLSGGQQQQLAIARAL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057   510 LAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEG 583
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

331-582

2.75e-22

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.36 E-value: 2.75e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  331 QRINELLARADEPRYPPLRDPFAG-RTTVGIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLY 409
Cdd:PRK13536  12 RRLELSPIERKHQGISEAKASIPGsMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  410 SAQRGSIRYGGVPLEEIGlDCVREHVAVVLQHPALFND-SVRANLT-------MGRERSDQACWRALEIAqladgvrRLP 481
Cdd:PRK13536  92 SPDAGKITVLGVPVPARA-RLARARIGVVPQFDNLDLEfTVRENLLvfgryfgMSTREIEAVIPSLLEFA-------RLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  482 QGLDTVVGrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRL-SAVKQA 559
Cdd:PRK13536 164 SKADARVS----DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMeEAERLC 239

                        250       260
                 ....*....|....*....|...
gi 15596057  560 DRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:PRK13536 240 DRLCVLEAGRKIAEGRPHALIDE 262

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

378-585

7.87e-22

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]

Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.10 E-value: 7.87e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   378 LDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEE----IGLDCVREHVAVVLQHPALFND-SVRAN 452
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   453 LTMGRERSDQACWRALEiaqlaDGVRRLpQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEY- 531
Cdd:TIGR02142  96 LRYGMKRARPSERRISF-----ERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYe 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057   532 ------ALHQALgdfleGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEGGL 585
Cdd:TIGR02142 170 ilpyleRLHAEF-----GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225

TauB

COG4525

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];

360-529

9.67e-22

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 9.67e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcvRehv 435
Cdd:COG4525   4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFN-DSVRANLTMG--------RERSDqacwRALEIAQLAdgvrrlpqGLDTVVGRSGVRLSGGQRQRLAIA 506
Cdd:COG4525  79 GVVFQKDALLPwLNVLDNVAFGlrlrgvpkAERRA----RAEELLALV--------GLADFARRRIWQLSGGMRQRVGIA 146

                       170       180
                ....*....|....*....|...
gi 15596057 507 RMILAEPKVVILDEATSALDAAT 529
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALT 169

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

360-583

1.14e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 1.14e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYG-----EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE----EIGLDC 430
Cdd:PRK13634   3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  431 VREHVAVVLQHP--ALFNDSVRANLTMGRE----RSDQACWRALEIAQLAdgvrrlpqGLD-TVVGRSGVRLSGGQRQRL 503
Cdd:PRK13634  83 LRKKVGIVFQFPehQLFEETVEKDICFGPMnfgvSEEDAKQKAREMIELV--------GLPeELLARSPFELSGGQMRRV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  504 AIARMILAEPKVVILDEATSALDAATE-------YALHQAlgdflEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGD 575
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRkemmemfYKLHKE-----KGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGT 229


                 ....*...
gi 15596057  576 HQQLIAEG 583
Cdd:PRK13634 230 PREIFADP 237

ModF

COG1119

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

360-574

1.17e-21

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: 94.38 E-value: 1.17e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLG-LYSAQRGSI-----RYGGVPLEEIgldcvRE 433
Cdd:COG1119   4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVrlfgeRRGGEDVWEL-----RK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 434 HVAVV---LQHPALFNDSVR------ANLTMG---------RERSDQacW-RALEIAQLADgvRRLPQgldtvvgrsgvr 494
Cdd:COG1119  79 RIGLVspaLQLRFPRDETVLdvvlsgFFDSIGlyreptdeqRERARE--LlELLGLAHLAD--RPFGT------------ 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 495 LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLI-VAHRLSAVKQA-DRVLVFDGGHIA 571
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVV 222


                ...
gi 15596057 572 EDG 574
Cdd:COG1119 223 AAG 225

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

360-573

1.44e-21

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 93.65 E-value: 1.44e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAY----GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCV---- 431
Cdd:COG4181   9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 432 REHVAVVLQH----P---ALFNDSVRANLTMGRERSDQACwRALEIAQLADGVRRLPQGLdtvvgrsgvrlSGGQRQRLA 504
Cdd:COG4181  89 ARHVGFVFQSfqllPtltALENVMLPLELAGRRDARARAR-ALLERVGLGHRLDHYPAQL-----------SGGEQQRVA 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 505 IARMILAEPKVVILDEATSALDAATE-------YALHQALGdflegrTTLI-VAHRLSAVKQADRVLVFDGGHIAED 573
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGeqiidllFELNRERG------TTLVlVTHDPALAARCDRVLRLRAGRLVED 227

cbiO

PRK13643

energy-coupling factor transporter ATPase;

373-582

2.29e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 2.29e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG----LDCVREHVAVVLQHP--ALFN 446
Cdd:PRK13643  20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  447 DSVRANLTMG-------RERSDQACWRALEIAQLADGVRRlpqgldtvvgRSGVRLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:PRK13643 100 ETVLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWE----------KSPFELSGGQMRRVAIAGILAMEPEVLVLD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057  520 EATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234

cbiO

PRK13642

energy-coupling factor transporter ATPase;

360-581

2.57e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.39 E-value: 2.57e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLD---LNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVA 436
Cdd:PRK13642   5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHP--ALFNDSVRANLTMGRErsDQACWRALEIAQLADGVrrLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:PRK13642  85 MVFQNPdnQFVGATVEDDVAFGME--NQGIPREEMIKRVDEAL--LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  515 VVILDEATSALDAATEYALHQALGDFLEGR--TTLIVAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229

thiQ

TIGR01277

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...

377-575

2.77e-21

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]

Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 92.62 E-value: 2.77e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   377 QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVplEEIGLDCVREHVAVVLQHPALFND-SVRANLTM 455
Cdd:TIGR01277  16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHlTVRQNIGL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   456 GRERSDQAcwRALEIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATE---YA 532
Cdd:TIGR01277  94 GLHPGLKL--NAEQQEKVVDAAQQV--GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLReemLA 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15596057   533 LHQALGDfLEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGD 575
Cdd:TIGR01277 170 LVKQLCS-ERQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVSD 212

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

360-584

3.40e-21

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 3.40e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcVREHVAVVL 439
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGVVP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALFND-SVRANLTM-GRE--RSDQACWRA----LEIAqladgvrRLPQGLDTVVGrsgvRLSGGQRQRLAIARMILA 511
Cdd:PRK13537  87 QFDNLDPDfTVRENLLVfGRYfgLSAAAARALvpplLEFA-------KLENKADAKVG----ELSGGMKRRLTLARALVN 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  512 EPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRL-SAVKQADRVLVFDGGH-IAEDGDHQQLIAEGG 584
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMeEAERLCDRLCVIEEGRkIAEGAPHALIESEIG 231

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

360-582

3.66e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 3.66e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGE-DKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE--EIGLDCVREHVA 436
Cdd:PRK13636   6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHP--ALFNDSVRANLTMGrersdqacwrALEIAQLADGVRRLpqgLDTVVGRSGVR---------LSGGQRQRLAI 505
Cdd:PRK13636  86 MVFQDPdnQLFSASVYQDVSFG----------AVNLKLPEDEVRKR---VDNALKRTGIEhlkdkpthcLSFGQKKRVAI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVK-QADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

375-574

4.59e-21

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.87 E-value: 4.59e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGV---PLEEIGLDCVREHVAVVLQHpalFN----- 446
Cdd:PRK11153  21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKELRKARRQIGMIFQH---FNllssr 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  447 ---DSVRANLT---MGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVILDE 520
Cdd:PRK11153  98 tvfDNVALPLElagTPKAEIKARVTELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  521 ATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223

ABC_6TM_Tm288_like

cd18547

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

72-316

6.92e-21

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: 93.24 E-value: 6.92e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  72 WQVAFGYIGLMLAATLLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLD 151
Cdd:cd18547  37 GGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIS 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 152 KFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQE 231
Cdd:cd18547 117 QALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKV 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 232 VRAGNRQGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLWFMIG 311
Cdd:cd18547 197 VKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQ 276


                ....*
gi 15596057 312 PVEQL 316
Cdd:cd18547 277 PINQI 281

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

360-574

1.01e-20

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 1.01e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQL---LLGLYSAQR--GSIRYGGVPLEEIGLDCVREH 434
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARvsGEVYLDGQDIFKMDVIELRRR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  435 VAVVLQHP-ALFNDSVRANLTMG----------RERSDQACWrALEIAQLADGVRrlpQGLDTVVGRsgvrLSGGQRQRL 503
Cdd:PRK14247  84 VQMVFQIPnPIPNLSIFENVALGlklnrlvkskKELQERVRW-ALEKAQLWDEVK---DRLDAPAGK----LSGGQQQRL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057  504 AIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDG 574
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227

ABC_FtsE

cd03292

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

360-550

1.06e-20

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages

Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 90.93 E-value: 1.06e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEI---GLDCVREHV 435
Cdd:cd03292   1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALFND-SVRANLTMGRERSDQA--CWR-----ALEIAQLADGVRRLPQGLdtvvgrsgvrlSGGQRQRLAIAR 507
Cdd:cd03292  81 GVVFQDFRLLPDrNVYENVAFALEVTGVPprEIRkrvpaALELVGLSHKHRALPAEL-----------SGGEQQRVAIAR 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15596057 508 MILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVA 550
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192

fecE

PRK11231

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;

360-585

3.89e-20

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 3.89e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALFND-SVRANLTMGR---------------ERSDQACwRALEIAQLADgvRRLPQgldtvvgrsgvrLSGGQRQRL 503
Cdd:PRK11231  83 QHHLTPEGiTVRELVAYGRspwlslwgrlsaednARVNQAM-EQTRINHLAD--RRLTD------------LSGGQRQRA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  504 AIArMILAE-PKVVILDEATSALDAAteyalHQA-LGDFL-----EGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGD 575
Cdd:PRK11231 148 FLA-MVLAQdTPVVLLDEPTTYLDIN-----HQVeLMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGT 221

                        250
                 ....*....|
gi 15596057  576 HQQLIAEGGL 585
Cdd:PRK11231 222 PEEVMTPGLL 231

ugpC

PRK11650

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

374-570

4.11e-20

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.21 E-value: 4.11e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP---LEEIGLDCvrehvAVVLQHPALF-NDSV 449
Cdd:PRK11650  19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvneLEPADRDI-----AMVFQNYALYpHMSV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  450 RANLTMG-----------RERSDQACwRALEIAQLADgvrRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVIL 518
Cdd:PRK11650  94 RENMAYGlkirgmpkaeiEERVAEAA-RILELEPLLD---RKPR-----------ELSGGQRQRVAMGRAIVREPAVFLF 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  519 DEATSALDAATEYA-------LHQALgdfleGRTTLIVAH-RLSAVKQADRVLVFDGGHI 570
Cdd:PRK11650 159 DEPLSNLDAKLRVQmrleiqrLHRRL-----KTTSLYVTHdQVEAMTLADRVVVMNGGVA 213

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

360-569

4.31e-20

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: 86.73 E-value: 4.31e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGgvpleeigldcvrehvavvl 439
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 qhpalfndsvranltmgrersdqacwRALEIAQladgvrrLPQgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:cd03221  61 --------------------------STVKIGY-------FEQ------------LSGGEKMRLALAKLLLENPNLLLLD 95

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15596057 520 EATSALDAATEYALHQALGDFleGRTTLIVAH-R--LSAVkqADRVLVFDGGH 569
Cdd:cd03221  96 EPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

374-570

5.30e-20

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 5.30e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDC---VREH-VAVVLQHPALFND-- 447
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDft 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  448 ---SVRANLTMGRERSDQACWRALEIAQLAdgvrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSA 524
Cdd:PRK11629 104 aleNVAMPLLIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15596057  525 LDAATEYALHQALGDF--LEGRTTLIVAHRLSAVKQADRVLVFDGGHI 570
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223

ABCG_EPDR

cd03213

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

370-564

5.31e-20

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: 87.99 E-value: 5.31e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 370 GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQR--GSIRYGGVPLEeigLDCVREHVAVVLQHpalfnD 447
Cdd:cd03213  20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLD---KRSFRKIIGYVPQD-----D 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 448 SVRANLTMgrersdqacWRALEI-AQLadgvrrlpqgldtvvgRSgvrLSGGQRQRLAIARMILAEPKVVILDEATSALD 526
Cdd:cd03213  92 ILHPTLTV---------RETLMFaAKL----------------RG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15596057 527 AATEYALHQALGDF-LEGRTTLIVAHRLSA--VKQADRVLV 564
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLL 184

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

360-574

8.96e-20

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.75 E-value: 8.96e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGED-KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL--EEIGLDCVREHVA 436
Cdd:PRK13639   2 LETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHP--ALFNDSVRA-------NLTMGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIAR 507
Cdd:PRK13639  82 IVFQNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  508 MILAEPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAV-KQADRVLVFDGGHIAEDG 574
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEG 219

cbiO

PRK13641

energy-coupling factor transporter ATPase;

360-570

1.02e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.89 E-value: 1.02e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYG-----EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE----EIGLDC 430
Cdd:PRK13641   3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  431 VREHVAVVLQHP--ALFNDSVRANLTMGRER----SDQACWRALEiaqladGVRRLpqGLDT-VVGRSGVRLSGGQRQRL 503
Cdd:PRK13641  83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNfgfsEDEAKEKALK------WLKKV--GLSEdLISKSPFELSGGQMRRV 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  504 AIARMILAEPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAVKQ-ADRVLVFDGGHI 570
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223

PRK09984

phosphonate ABC transporter ATP-binding protein;

360-579

1.10e-19

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 1.10e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGS---IRYGGVPLEEIG-----LDCV 431
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGrlardIRKS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  432 REHVAVVLQHPALFND-SVRANLTMGRERSD---QACWRALEIAQLADGVRRLPQ-GLDTVVGRSGVRLSGGQRQRLAIA 506
Cdd:PRK09984  85 RANTGYIFQQFNLVNRlSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  507 RMILAEPKVVILDEATSALDAATEYALHQALGDF--LEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

360-564

1.47e-19

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.47e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLeEIG--LDCVREHVAV 437
Cdd:COG3845   6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRspRDAIALGIGM 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFND-SVRANLTMGRERSDqacWRALEIAQLADGVRRLPQ--GL----DTVVGrsgvRLSGGQRQRLAIARMIL 510
Cdd:COG3845  85 VHQHFMLVPNlTVAENIVLGLEPTK---GGRLDRKAARARIRELSEryGLdvdpDAKVE----DLSVGEQQRVEILKALY 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057 511 AEPKVVILDEATSAL-DAATEyalhqALGDFL-----EGRTTLIVAHRLSAVKQ-ADRVLV 564
Cdd:COG3845 158 RGARILILDEPTAVLtPQEAD-----ELFEILrrlaaEGKSIIFITHKLREVMAiADRVTV 213

ABC_6TM_TmrA_like

cd18544

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

62-316

1.53e-19

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: 89.37 E-value: 1.53e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  62 RFMDRLLPA---DWQVAFGYIGLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGS 138
Cdd:cd18544  24 RAIDDYIVPgqgDLQGLLLLALLYLGLLLL----SFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 139 ISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARF 218
Cdd:cd18544 100 LVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRL 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 219 TQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQWksdaagrASGLLFQFgIDVFRAAAMLTVLL------- 291
Cdd:cd18544 180 NAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIK-------LFALFRPL-VELLSSLALALVLWygggqvl 251

                       250       260
                ....*....|....*....|....*.
gi 15596057 292 -SDLSIGQMLAVFSYLWFMIGPVEQL 316
Cdd:cd18544 252 sGAVTLGVLYAFIQYIQRFFRPIRDL 277

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

360-579

2.52e-19

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.78 E-value: 2.52e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvplEEIGLDCVREH-VAVV 438
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHPALF-----NDSVRANLTM---GRERSDQACWRALEIAQLAD-GVRRLPQgldtvvgrsgvrLSGGQRQRLAIARMI 509
Cdd:PRK11432  84 FQSYALFphmslGENVGYGLKMlgvPKEERKQRVKEALELVDLAGfEDRYVDQ------------ISGGQQQRVALARAL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057  510 LAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

375-574

2.72e-19

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]

Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.14 E-value: 2.72e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVrehvaVVLQHPALFN-DSVRANL 453
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   454 TMGRERSdqacwraleIAQLADGVRR--LPQGLDTVVGRSGV-----RLSGGQRQRLAIARMILAEPKVVILDEATSALD 526
Cdd:TIGR01184  76 ALAVDRV---------LPDLSKSERRaiVEEHIALVGLTEAAdkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15596057   527 AATEYALHQALGDFLE--GRTTLIVAHRL-SAVKQADRVLVFDGGHIAEDG 574
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197

cbiO

PRK13649

energy-coupling factor transporter ATPase;

359-574

2.81e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 2.81e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  359 GIEVRGLDFAYG-----EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL----EEIGLD 429
Cdd:PRK13649   2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  430 CVREHVAVVLQHP--ALFNDSVRANLTMGRER---SDQacwralEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLA 504
Cdd:PRK13649  82 QIRKKVGLVFQFPesQLFEETVLKDVAFGPQNfgvSQE------EAEALAREKLALVGISESLFEKNPFELSGGQMRRVA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057  505 IARMILAEPKVVILDEATSALDAATEY-------ALHQAlgdfleGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKelmtlfkKLHQS------GMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

359-558

4.08e-19

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 4.08e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQ-----RGSIRYGGVPLEE--IGLDCV 431
Cdd:PRK14258   7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  432 REHVAVVLQHPALFNDSVRANLTMG--------RERSDQACWRALEIAQLADGVRRlpqgldtVVGRSGVRLSGGQRQRL 503
Cdd:PRK14258  87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEIDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQRL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  504 AIARMILAEPKVVILDEATSALDAATEYALHQALGDFL--EGRTTLIVAHRLSAVKQ 558
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSR 216

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

359-567

4.14e-19

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.00 E-value: 4.14e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQ---RGSIRYGGVPLEeiGLDCVREHV 435
Cdd:COG4136   1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT--ALPAEQRRI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 436 AVVLQHPALF-NDSVRANL------TMGRERSDQACWRALEIAQLADGVRRLPqglDTvvgrsgvrLSGGQRQRLAIARM 508
Cdd:COG4136  79 GILFQDDLLFpHLSVGENLafalppTIGRAQRRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALLRA 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 509 ILAEPKVVILDEATSALDAateyALHQALGDFLEGRT------TLIVAHRLSAVKQADRVLVFDG 567
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDA----ALRAQFREFVFEQIrqrgipALLVTHDEEDAPAAGRVLDLGN 208

ABC_6TM_TAP_ABCB8_10_like

cd18557

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

62-333

5.04e-19

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: 87.62 E-value: 5.04e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  62 RFMDRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISA 141
Cdd:cd18557  21 RLIDTIIKGGDLDVLNELALILLAIYLLQS---VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 142 HLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQA 221
Cdd:cd18557  98 RLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQV 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 222 LTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASqwksdaaGRASGlLFQFGIDVFRAAAMLTVLL--------SD 293
Cdd:cd18557 178 AEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKK-------ALANA-LFQGITSLLIYLSLLLVLWyggylvlsGQ 249

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15596057 294 LSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18557 250 LTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

112-581

8.74e-19

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.03 E-value: 8.74e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  112 VYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLD-KFVgeTLSRFLVALLTLLGTAAILVWMHWQLALLILLFN 190
Cdd:PRK10522  80 VYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiAFV--RLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWM 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  191 PLVIWSTVQLGKRV-KHLKKL-ENDstarftQALTETLEAIQEVR---AGNR---QGYFLGRLGHRAQEVRDYAV----- 257
Cdd:PRK10522 158 AVTIWGGFVLVARVyKHMATLrETE------DKLYNDYQTVLEGRkelTLNReraEYVFENEYEPDAQEYRHHIIradtf 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  258 ---ASQWKSDAAGRASGLLFQFGI-----DVFRAAAM-LTVLLSDLSIGQMLAVFSYLwfmigpveqllglqyayYAAGG 328
Cdd:PRK10522 232 hlsAVNWSNIMMLGAIGLVFYMANslgwaDTNVAATYsLTLLFLRTPLLSAVGALPTL-----------------LSAQV 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  329 ALQRINELLARADEPRYPplrDPFAGRTTVGIEVRGLDFAYGEDKV-LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLG 407
Cdd:PRK10522 295 AFNKLNKLALAPYKAEFP---RPQAFPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTG 371

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  408 LYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPALFNDSVRANltmGRERSDQACWRALEIAQLADGVRrlpqgldTV 487
Cdd:PRK10522 372 LYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE---GKPANPALVEKWLERLKMAHKLE-------LE 441

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  488 VGR-SGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL--EGRTTLIVAHRLSAVKQADRVLV 564
Cdd:PRK10522 442 DGRiSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLE 521

                        490
                 ....*....|....*...
gi 15596057  565 FDGGHIAE-DGDHQQLIA 581
Cdd:PRK10522 522 MRNGQLSElTGEERDAAS 539

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

360-588

8.82e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 8.82e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAY-GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVV 438
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHP--ALFNDSVRANLTMGrersdqACWRALEIAQLADGVRRLPQ--GLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:PRK13652  84 FQNPddQIFSPTVEQDIAFG------PINLGLDEETVAHRVSSALHmlGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  515 VVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEGGLYAR 588
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

360-573

1.12e-18

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.78 E-value: 1.12e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAY--GED--KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCV---- 431
Cdd:PRK10535   5 LELKDIRRSYpsGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  432 REHVAVVLQHPALFndsvrANLTMGRERSDQACWRALEIAQLADGVRRLPQ--GLDTVVGRSGVRLSGGQRQRLAIARMI 509
Cdd:PRK10535  85 REHFGFIFQRYHLL-----SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057  510 LAEPKVVILDEATSALDAATEYA----LHQaLGDflEGRTTLIVAHRLSAVKQADRVLVFDGGHIAED 573
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEvmaiLHQ-LRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224

ABC_Carb_Monos_II

cd03215

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

361-570

1.51e-18

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.

Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 83.64 E-value: 1.51e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAygedKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE--------EIGLDCV- 431
Cdd:cd03215   6 EVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdaiRAGIAYVp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 432 --REHVAVVLQHpalfndSVRANLTMGRersdqacwraleiaqladgvrrlpqgldtvvgrsgvRLSGGQRQRLAIARMI 509
Cdd:cd03215  82 edRKREGLVLDL------SVAENIALSS------------------------------------LLSGGNQQKVVLARWL 119

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 510 LAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHI 570
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

360-575

1.57e-18

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: 84.12 E-value: 1.57e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL--YSAQRGSIRYGGVPLEEIGLDcvrehvav 437
Cdd:cd03217   1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 vlqhpalfnDSVRANLTMGRERSdqacwraLEIA--QLADGVRRLPQGLdtvvgrsgvrlSGGQRQRLAIARMILAEPKV 515
Cdd:cd03217  73 ---------ERARLGIFLAFQYP-------PEIPgvKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDL 125

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 516 VILDEATSALDAATEYALHQALGDFL-EGRTTLIVAH--RLSAVKQADRVLVFDGGHIAEDGD 575
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188

ABC_6TM_exporter_like

cd18778

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

62-333

1.59e-18

Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 86.44 E-value: 1.59e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  62 RFMDRLL--PADWQVAFGYIGLMLAATLLLRgaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSI 139
Cdd:cd18778  24 ELVDLVTigSKSLGLLLGLALLLLGAYLLRA----LLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 140 SAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFT 219
Cdd:cd18778 100 MSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELN 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 220 QALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwksdAAGRASGlLFQFGIDVFRAAAMLTVLL-------- 291
Cdd:cd18778 180 ALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQL-------RAMKLWA-IFHPLMEFLTSLGTVLVLGfggrlvla 251

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15596057 292 SDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18778 252 GELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

373-571

1.68e-18

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: 84.63 E-value: 1.68e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLysAQRGSIRYGGVPL--EEIGLDCVREHVAVVLQ----HPALfn 446
Cdd:cd03234  21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFngQPRKPDQFQKCVAYVRQddilLPGL-- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 447 dSVR------ANLTMGRERSDqacwralEIAQLADGVRRLPQGLDTVVGRSGVR-LSGGQRQRLAIARMILAEPKVVILD 519
Cdd:cd03234  97 -TVRetltytAILRLPRKSSD-------AIRKKRVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILD 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 520 EATSALDAATEYALHQALGDFL-EGRTTLIVAH--RLSAVKQADRVLVFDGGHIA 571
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223

ABC_Pro_Gly_Betaine

cd03294

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

379-582

1.91e-18

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: 85.39 E-value: 1.91e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 379 DLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVRE----HVAVVLQHPALF-NDSVRANL 453
Cdd:cd03294  44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 454 TMG--------RERSDQACwRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSAL 525
Cdd:cd03294 124 AFGlevqgvprAEREERAA-EALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 526 DAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:cd03294 192 DPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251

PRK13651

cobalt transporter ATP-binding subunit; Provisional

360-575

2.02e-18

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.29 E-value: 2.02e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYG-----EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRY---------GGVPLEE 425
Cdd:PRK13651   3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  426 IGLDCV---------------REHVAVVLQHP--ALFNDSVRAN-----LTMGRERsDQACWRALEIAQLADgvrrLPQg 483
Cdd:PRK13651  83 VLEKLViqktrfkkikkikeiRRRVGVVFQFAeyQLFEQTIEKDiifgpVSMGVSK-EEAKKRAAKYIELVG----LDE- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  484 ldTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALD-AATE------YALHQalgdflEGRTTLIVAHRL-SA 555
Cdd:PRK13651 157 --SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKeileifDNLNK------QGKTIILVTHDLdNV 228

                        250       260
                 ....*....|....*....|
gi 15596057  556 VKQADRVLVFDGGHIAEDGD 575
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGD 248

ABCC_CFTR1

cd03291

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

374-568

2.17e-18

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: 85.68 E-value: 2.17e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvreHVAVVLQHPALFNDSVRANL 453
Cdd:cd03291  52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 454 TMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYAL 533
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15596057 534 HQA-LGDFLEGRTTLIVAHRLSAVKQADRVLVFDGG 568
Cdd:cd03291 199 FEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

342-581

2.23e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 2.23e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  342 EPRYPPLrdPFAGRTTVGIEVRGLDFAY-----------GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYS 410
Cdd:PRK15134 260 EPSGDPV--PLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  411 AQrGSIRYGGVPLEEIG---LDCVREHVAVVLQHPalfNDSVRANLTMGR--ERSDQACWRALEIAQLADGVRRLPQ--G 483
Cdd:PRK15134 338 SQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLNPRLNVLQiiEEGLRVHQPTLSAAQREQQVIAVMEevG 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  484 LDTVV-GRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDaATEYALHQALGDFLEGRTTL---IVAHRLSAVKQ- 558
Cdd:PRK15134 414 LDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALLKSLQQKHQLaylFISHDLHVVRAl 492

                        250       260
                 ....*....|....*....|...
gi 15596057  559 ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK15134 493 CHQVIVLRQGEVVEQGDCERVFA 515

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

362-570

2.55e-18

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 2.55e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 362 VRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvREHVAVVLQH 441
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 442 PALFND-SVRANLTMGRERSDQACWRALEI-AQLADG-------------------------VRRLPQGL-------DTV 487
Cdd:COG0488  70 PPLDDDlTVLDTVLDGDAELRALEAELEELeAKLAEPdedlerlaelqeefealggweaearAEEILSGLgfpeedlDRP 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 488 VGrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSALDA-ATEYalhqaLGDFLEGR--TTLIVAH-R--LSAVkqADR 561
Cdd:COG0488 150 VS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW-----LEEFLKNYpgTVLVVSHdRyfLDRV--ATR 218


                ....*....
gi 15596057 562 VLVFDGGHI 570
Cdd:COG0488 219 ILELDRGKL 227

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

360-579

2.68e-18

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.20 E-value: 2.68e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIglDCVREHVAVVL 439
Cdd:PRK11607  20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALF-NDSVRANLTMGRERSDQAcwRAlEIAQladgvrRLPQGLDTV-----VGRSGVRLSGGQRQRLAIARMILAEP 513
Cdd:PRK11607  98 QSYALFpHMTVEQNIAFGLKQDKLP--KA-EIAS------RVNEMLGLVhmqefAKRKPHQLSGGQRQRVALARSLAKRP 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  514 KVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAH-RLSAVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

360-528

2.76e-18

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]

Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.18 E-value: 2.76e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEiGLDCVREHVAVVL 439
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   440 QHPALFND-SVRANLTMGRE---RSDQACWRALEIAQLaDGVRRLPQGldtvvgrsgvRLSGGQRQRLAIARMILAEPKV 515
Cdd:TIGR01189  80 HLPGLKPElSALENLHFWAAihgGAQRTIEDALAAVGL-TGFEDLPAA----------QLSAGQQRRLALARLWLSRRPL 148

                         170
                  ....*....|...
gi 15596057   516 VILDEATSALDAA 528
Cdd:TIGR01189 149 WILDEPTTALDKA 161

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

364-588

2.95e-18

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 2.95e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  364 GLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE--EIGLDCVREHVAVVLQH 441
Cdd:PRK13638   6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  442 P--ALFNDSVRANLTMGrersdqacWRALEIAQlADGVRRLPQGLdTVVGRSGVR------LSGGQRQRLAIARMILAEP 513
Cdd:PRK13638  86 PeqQIFYTDIDSDIAFS--------LRNLGVPE-AEITRRVDEAL-TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  514 KVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEGGLYAR 588
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232

CeuD

COG4604

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...

360-591

5.55e-18

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 5.55e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:COG4604   2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALfndSVRanLTM------GR-----ERSDQACWRA-------LEIAQLADgvRRLpqglDTvvgrsgvrLSGGQRQ 501
Cdd:COG4604  82 QENHI---NSR--LTVrelvafGRfpyskGRLTAEDREIideaiayLDLEDLAD--RYL----DE--------LSGGQRQ 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 502 RLAIArMILA-EPKVVILDEATSALD----AATEYALHQALGDFleGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGD 575
Cdd:COG4604 143 RAFIA-MVLAqDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL--GKTVVIVLHDINfASCYADHIVAMKDGRVVAQGT 219

                       250
                ....*....|....*.
gi 15596057 576 HQQLIAEGGLyARLYG 591
Cdd:COG4604 220 PEEIITPEVL-SDIYD 234

CFTR_protein

TIGR01271

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

374-569

6.66e-18

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 88.04 E-value: 6.66e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvpleeigldcvreHVAVVLQHPALFNDSVRANL 453
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    454 TMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYAL 533
Cdd:TIGR01271  508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 15596057    534 HQA-LGDFLEGRTTLIVAHRLSAVKQADRVLVFDGGH 569
Cdd:TIGR01271  588 FEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

369-574

6.68e-18

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.

Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.15 E-value: 6.68e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 369 YGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-VPLEEigldcVREHVA---VVL-QHPA 443
Cdd:cd03267  31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKR-----RKKFLRrigVVFgQKTQ 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 444 LFND-SVRANLTMGRERSDqacwraLEIAQLADGVRRLPQGLD-TVVGRSGVR-LSGGQRQRLAIARMILAEPKVVILDE 520
Cdd:cd03267 106 LWWDlPVIDSFYLLAAIYD------LPPARFKKRLDELSELLDlEELLDTPVRqLSLGQRMRAEIAAALLHEPEILFLDE 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 521 ATSALDAATEYALHQALGDFLEGR--TTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236

cbiO

PRK13646

energy-coupling factor transporter ATPase;

371-583

8.26e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.06 E-value: 8.26e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  371 EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLD----CVREHVAVVLQHP--AL 444
Cdd:PRK13646  19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirPVRKRIGMVFQFPesQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 FNDSVR-------ANLTMGRERSDQACWRALeiaqLADGVRRlpqgldTVVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:PRK13646  99 FEDTVEreiifgpKNFKMNLDEVKNYAHRLL----MDLGFSR------DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  518 LDEATSALDAATEYALHQALGDFL--EGRTTLIVAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIAEG 583
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

360-566

8.49e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.

Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.16 E-value: 8.49e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGlDCVREHVAVVL 439
Cdd:cd03231   1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 440 QHPALFND-SVRANLT-MGRERSDQACWRALEIAQLAdGVRRLPQGldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:cd03231  80 HAPGIKTTlSVLENLRfWHADHSDEQVEEALARVGLN-GFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWI 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15596057 518 LDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLSAVKQADRVLVFD 566
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

360-575

9.11e-18

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 9.11e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGED-----KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIR----YGGVPLEEIGLDC 430
Cdd:PRK13631  22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELIT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  431 ------------VREHVAVVLQHP--ALFNDSVRANLTMGRERSDQACWRALEIAQLAdgVRRLpqGLD-TVVGRSGVRL 495
Cdd:PRK13631 102 npyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFY--LNKM--GLDdSYLERSPFGL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  496 SGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAED 573
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEvADEVIVMDKGKILKT 257


                 ..
gi 15596057  574 GD 575
Cdd:PRK13631 258 GT 259

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

360-529

9.92e-18

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 9.92e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDcvrehVAVVL 439
Cdd:PRK11248   2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-----RGVVF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALFN-DSVRANLTMG-------RERSDQACWRALEIAQLAD-GVRRLPQgldtvvgrsgvrLSGGQRQRLAIARMIL 510
Cdd:PRK11248  77 QNEGLLPwRNVQDNVAFGlqlagveKMQRLEIAHQMLKKVGLEGaEKRYIWQ------------LSGGQRQRVGIARALA 144

                        170
                 ....*....|....*....
gi 15596057  511 AEPKVVILDEATSALDAAT 529
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFT 163

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

360-579

1.16e-17

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: 82.03 E-value: 1.16e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG--VPLEEIGldcVREHVAV 437
Cdd:cd03265   1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdVVREPRE---VRRRIGI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQHPALFND-SVRANLTM-GRERSDQACWRALEIAQLADGVrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:cd03265  78 VFQDLSVDDElTGWENLYIhARLYGVPGAERRERIDELLDFV-----GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057 516 VILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRL-SAVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

373-579

1.22e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.37 E-value: 1.22e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL---EEIGLDCVREHVAVVLQHPALfndSV 449
Cdd:PRK15079  35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLA---SL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  450 RANLTMGRERSD--QACWRALEIAQLADGVRR-------LPQgldtVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDE 520
Cdd:PRK15079 112 NPRMTIGEIIAEplRTYHPKLSRQEVKDRVKAmmlkvglLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057  521 ATSALDA---ATEYALHQALGDFLeGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK15079 188 PVSALDVsiqAQVVNLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249

ABC_6TM_PCAT1_LagD_like

cd18570

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

64-333

1.30e-17

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: 83.65 E-value: 1.30e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  64 MDRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHL 143
Cdd:cd18570  29 IDDIIPSGDINLLNIISIGLILLYLFQS---LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 144 vTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALT 223
Cdd:cd18570 106 -NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLI 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 224 ETLEAIQEVRAGNRQGYFLGRLGHR----AQEVRDYAVASQWKSDAAGRASGLlfqFGIDVFRAAAMLtVLLSDLSIGQM 299
Cdd:cd18570 185 ESLKGIETIKSLNAEEQFLKKIEKKfsklLKKSFKLGKLSNLQSSIKGLISLI---GSLLILWIGSYL-VIKGQLSLGQL 260

                       250       260       270
                ....*....|....*....|....*....|....
gi 15596057 300 LAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18570 261 IAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294

livF

PRK11614

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

369-591

1.31e-17

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 1.31e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  369 YGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGL-DCVREHVAVVLQHPALFND 447
Cdd:PRK11614  15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  448 -SVRANLTMG-----RERSDQACWRALEIaqladgvrrLPQGLDTVVGRSGVrLSGGQRQRLAIARMILAEPKVVILDEA 521
Cdd:PRK11614  95 mTVEENLAMGgffaeRDQFQERIKWVYEL---------FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEP 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057  522 TSALDAATEYALHQALGDFL-EGRTTLIVAHRLS-AVKQADRVLVFDGGHIA-EDGDHQQLIAEGGLYARLYG 591
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANqALKLADRGYVLENGHVVlEDTGDALLANEAVRSAYLGG 237

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

362-574

1.58e-17

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.67 E-value: 1.58e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  362 VRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRY---GGVPLEEIGLD------CVR 432
Cdd:PRK11701   9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSeaerrrLLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQHPAlfnDSVRANLT---------M-------GRERSDQACW-RALEIAqlADGVRRLPQgldtvvgrsgvRL 495
Cdd:PRK11701  89 TEWGFVHQHPR---DGLRMQVSaggnigerlMavgarhyGDIRATAGDWlERVEID--AARIDDLPT-----------TF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  496 SGGQRQRLAIARMILAEPKVVILDEATSALDAATeyalhQA-LGDFLEGRTT------LIVAHRLSAVKQ-ADRVLVFDG 567
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QArLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQ 227


                 ....*..
gi 15596057  568 GHIAEDG 574
Cdd:PRK11701 228 GRVVESG 234

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

360-581

1.60e-17

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.89 E-value: 1.60e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKS----TLVQLLLGLYSAQRGSIRYGGVPL---EEIGL 428
Cdd:COG4172   7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSEREL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 429 DCVR-EHVAVVLQHP--ALfN----------DSVRANLTMGRERSDQACWRALEIAQLADGVRRL---PQgldtvvgrsg 492
Cdd:COG4172  87 RRIRgNRIAMIFQEPmtSL-NplhtigkqiaEVLRLHRGLSGAAARARALELLERVGIPDPERRLdayPH---------- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 493 vRLSGGQRQRLAIArMILA-EPKVVILDEATSALDAATeyalhQA-----LGDfL---EGRTTLIVAHRLSAVKQ-ADRV 562
Cdd:COG4172 156 -QLSGGQRQRVMIA-MALAnEPDLLIADEPTTALDVTV-----QAqildlLKD-LqreLGMALLLITHDLGVVRRfADRV 227

                       250
                ....*....|....*....
gi 15596057 563 LVFDGGHIAEDGDHQQLIA 581
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFA 246

PRK10619

histidine ABC transporter ATP-binding protein HisP;

369-581

3.32e-17

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.55 E-value: 3.32e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  369 YGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEI-------------GLDCVREHV 435
Cdd:PRK10619  15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  436 AVVLQHpalFNdsVRANLTMgRERSDQACWRALEIAQlADGVRRLPQGLDTV------VGRSGVRLSGGQRQRLAIARMI 509
Cdd:PRK10619  95 TMVFQH---FN--LWSHMTV-LENVMEAPIQVLGLSK-QEARERAVKYLAKVgideraQGKYPVHLSGGQQQRVSIARAL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  510 LAEPKVVILDEATSALD---AATEYALHQALGDflEGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

360-562

5.03e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 5.03e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQL---LLGLYSAQR--GSIRYGGVPLEEIGLDC--VR 432
Cdd:PRK14267   5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARveGEVRLFGRNIYSPDVDPieVR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQHPALFN-----DSVRA-----NLTMGRERSDQACWRALEIAQLADGVRrlpqglDTVVGRSGvRLSGGQRQR 502
Cdd:PRK14267  85 REVGMVFQYPNPFPhltiyDNVAIgvklnGLVKSKKELDERVEWALKKAALWDEVK------DRLNDYPS-NLSGGQRQR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHrlsAVKQADRV 562
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH---SPAQAARV 214

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

369-575

5.12e-17

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 5.12e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 369 YGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRyggvpleeigldcVREHVAVVLQ-----HPA 443
Cdd:COG1134  36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-------------VNGRVSALLElgagfHPE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 444 LfndSVRAN-----LTMGRERSdqacwralEIAQLADGVRR---LPQGLDTVVGRsgvrLSGGQRQRLAIARMILAEPKV 515
Cdd:COG1134 103 L---TGRENiylngRLLGLSRK--------EIDEKFDEIVEfaeLGDFIDQPVKT----YSSGMRARLAFAVATAVDPDI 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 516 VILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGD 575
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229

PhnK

COG1101

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

371-573

5.39e-17

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 5.39e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 371 EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEigldcVREH-----VAVVLQHPAL- 444
Cdd:COG1101  18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPEYkrakyIGRVFQDPMMg 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 445 --FNDSVRANLTM----GRERSDQACWRALEIAQLADGVRRLPQGL----DTVVGRsgvrLSGGQRQRLAIARMILAEPK 514
Cdd:COG1101  93 taPSMTIEENLALayrrGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVGL----LSGGQRQALSLLMATLTKPK 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 515 VVILDEATSALDAATEYALHQALGDFLEGR--TTLIVAHRLS-AVKQADRVLVFDGGHIAED 573
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRIILD 230

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

360-530

7.37e-17

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 7.37e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvplEEIGLDCVREhVAVVL 439
Cdd:PRK13539   3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAE-ACHYL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QH-----PALfndSVRANLTMgrersdqacWRAL---EIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILA 511
Cdd:PRK13539  79 GHrnamkPAL---TVAENLEF---------WAAFlggEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVS 144

                        170
                 ....*....|....*....
gi 15596057  512 EPKVVILDEATSALDAATE 530
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAV 163

3a01204

TIGR00955

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...

385-586

1.17e-16

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 1.17e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   385 GEKVALVGASGGGKSTLVQLLlglysAQR--------GSIRYGGVPleeIGLDCVREHVAVVLQH----PALfndSVR-- 450
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNAL-----AFRspkgvkgsGSVLLNGMP---IDAKEMRAISAYVQQDdlfiPTL---TVReh 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   451 ----ANLTMGRERSDQAcwRALEIAQLADGVRrLPQGLDTVVGRSGVR--LSGGQRQRLAIARMILAEPKVVILDEATSA 524
Cdd:TIGR00955 120 lmfqAHLRMPRRVTKKE--KRERVDEVLQALG-LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057   525 LDAATEYALHQALGDF-LEGRTTLIVAHRLSA--VKQADRVLVFDGGHIAEDGDHQQLI---AEGGLY 586
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVpffSDLGHP 264

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

369-574

1.20e-16

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: 79.11 E-value: 1.20e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 369 YGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG--VPLEEIGldcvrehVAVvlqHPALfn 446
Cdd:cd03220  32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLG-------GGF---NPEL-- 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 447 dSVRANLT-----MGRERsDQACWRALEIAQLADgvrrLPQGLDTVVGrsgvRLSGGQRQRLAIARMILAEPKVVILDEA 521
Cdd:cd03220 100 -TGRENIYlngrlLGLSR-KEIDEKIDEIIEFSE----LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEV 169

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596057 522 TSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

365-581

1.23e-16

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 1.23e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  365 LDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGsIRYGGVPLeeIGLDCV---------REHV 435
Cdd:PRK14271  27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVL--LGGRSIfnyrdvlefRRRV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  436 AVVLQHPALFNDSVRANLTMG---------RERSDQACWRALEIAqLADGVR-RLPQgldtvvgrSGVRLSGGQRQRLAI 505
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAGvrahklvprKEFRGVAQARLTEVG-LWDAVKdRLSD--------SPFRLSGGQQQLLCL 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

374-568

1.43e-16

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];

Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.02 E-value: 1.43e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRY----GGVPLEEIG----LDCVREHVAVVLQH---- 441
Cdd:COG4778  26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASpreiLALRRRTIGYVSQFlrvi 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 442 ---PALfnDSV-RANLTMGRERsDQACWRALEI-AQLadgvrRLPQGLDTVvgrSGVRLSGGQRQRLAIARMILAEPKVV 516
Cdd:COG4778 106 prvSAL--DVVaEPLLERGVDR-EEARARARELlARL-----NLPERLWDL---PPATFSGGEQQRVNIARGFIADPPLL 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15596057 517 ILDEATSALDAATEYALHQALGDFLEGRTTLI-VAHRLSAVKQ-ADRVLVFDGG 568
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

361-589

2.22e-16

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 2.22e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL--YSAQRGSIRYGGVPL-----EEIgldcVRE 433
Cdd:COG0396   2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIlelspDER----ARA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 434 HVAVVLQHPALF-----NDSVRANLT-MGRERSDQACWRAlEIAQLADGVrrlpqGLDT-VVGRS-GVRLSGGQRQRLAI 505
Cdd:COG0396  78 GIFLAFQYPVEIpgvsvSNFLRTALNaRRGEELSAREFLK-LLKEKMKEL-----GLDEdFLDRYvNEGFSGGEKKRNEI 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 506 ARMILAEPKVVILDEATSALDAAteyALhQALGDFL-----EGRTTLIVAH--RLSAVKQADRVLVFDGGHIAEDGDH-- 576
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDID---AL-RIVAEGVnklrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKel 227

                       250
                ....*....|....
gi 15596057 577 -QQLIAEGglYARL 589
Cdd:COG0396 228 aLELEEEG--YDWL 239

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

360-568

2.32e-16

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: 78.09 E-value: 2.32e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL------------EEIG 427
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdiaarnrigylpEERG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 428 LdCVREHVAVVLQHPALFNDsvrANLTMGRERSDQACWRaLEIAQLADgvRRLPQgldtvvgrsgvrLSGGQRQRLAIAR 507
Cdd:cd03269  81 L-YPKMKVIDQLVYLAQLKG---LKKEEARRRIDEWLER-LELSEYAN--KRVEE------------LSKGNQQKVQFIA 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 508 MILAEPKVVILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVFDGG 568
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKG 204

PRK10762

D-ribose transporter ATP binding protein; Provisional

360-580

2.84e-16

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 2.84e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL--------EEIGLDCV 431
Cdd:PRK10762   5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssQEAGIGII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  432 REHVAVVlqhPALfndSVRANLTMGRE------RSDqacWRalEIAQLADG-VRRL--PQGLDTVVGrsgvRLSGGQRQR 502
Cdd:PRK10762  85 HQELNLI---PQL---TIAENIFLGREfvnrfgRID---WK--KMYAEADKlLARLnlRFSSDKLVG----ELSIGEQQM 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  503 LAIARMILAEPKVVILDEATSAL-DAATEyALHQALGDF-LEGRTTLIVAHRLSAVKQ-ADRVLVF-DGGHIAE----DG 574
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELkSQGRGIVYISHRLKEIFEiCDDVTVFrDGQFIAErevaDL 228


                 ....*.
gi 15596057  575 DHQQLI 580
Cdd:PRK10762 229 TEDSLI 234

cbiO

PRK13645

energy-coupling factor transporter ATPase;

371-574

3.47e-16

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.28 E-value: 3.47e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  371 EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYG--GVP--LEEIG-LDCVREHVAVVLQHP--A 443
Cdd:PRK13645  23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPanLKKIKeVKRLRKEIGLVFQFPeyQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  444 LFNDSVRANLTMGR----ERSDQACWRALEIAQLAdgvrRLPQgldTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:PRK13645 103 LFQETIEKDIAFGPvnlgENKQEAYKKVPELLKLV----QLPE---DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057  520 EATSALDAATEYalhqalgDFL---------EGRTTLIVAHRLSAV-KQADRVLVFDGGHIAEDG 574
Cdd:PRK13645 176 EPTGGLDPKGEE-------DFInlferlnkeYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

360-581

3.83e-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: 81.39 E-value: 3.83e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL--YSAQRGSIRYG----------GVPlEEIG 427
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERP-SKVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   428 LDC------------------------VREHVAVVLQHP-ALF-NDSVRANLTMGRE----RSDQACWRALEIAQLADGV 477
Cdd:TIGR03269  80 EPCpvcggtlepeevdfwnlsdklrrrIRKRIAIMLQRTfALYgDDTVLDNVLEALEeigyEGKEAVGRAVDLIEMVQLS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   478 RRLpqgldTVVGRSgvrLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL--EGRTTLIVAHRLSA 555
Cdd:TIGR03269 160 HRI-----THIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEV 231

                         250       260
                  ....*....|....*....|....*..
gi 15596057   556 VKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGTPDEVVA 258

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

312-586

9.54e-16

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: 81.21 E-value: 9.54e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    312 PVEQLLGLQYAYYAAGG--------ALQRINELLARADEPRYPP-LRDPFAGRT----TVGIEVRGLD--FAYGEDKVLE 376
Cdd:TIGR01257  868 PLPWYFLLQESYWLGGEgcstreerALEKTEPLTEEMEDPEHPEgINDSFFERElpglVPGVCVKNLVkiFEPSGRPAVD 947

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    377 QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEeIGLDCVREHVAVVLQHPALFNDSVRANLTMG 456
Cdd:TIGR01257  948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    457 RERSDQACWralEIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQA 536
Cdd:TIGR01257 1027 YAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 15596057    537 LGDFLEGRTTLIVAHRLSavkQADRVlvfdgghiaedGDHQQLIAEGGLY 586
Cdd:TIGR01257 1104 LLKYRSGRTIIMSTHHMD---EADLL-----------GDRIAIISQGRLY 1139

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

345-581

1.27e-15

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 1.27e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  345 YPPLRDPFAGRTTVgievrgldfaygedKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL- 423
Cdd:PRK11308  15 YPVKRGLFKPERLV--------------KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  424 --EEIGLDCVREHVAVVLQHP-----------ALFNDSVRANLTMGR-ERSDqacwRALEIAQLAdGVR-----RLPQgl 484
Cdd:PRK11308  81 kaDPEAQKLLRQKIQIVFQNPygslnprkkvgQILEEPLLINTSLSAaERRE----KALAMMAKV-GLRpehydRYPH-- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  485 dtvvgrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEyalHQALGDFLE-----GRTTLIVAHRLSAVKQ- 558
Cdd:PRK11308 154 ---------MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ---AQVLNLMMDlqqelGLSYVFISHDLSVVEHi 221

                        250       260
                 ....*....|....*....|...
gi 15596057  559 ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK11308 222 ADEVMVMYLGRCVEKGTKEQIFN 244

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

362-591

1.99e-15

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.56 E-value: 1.99e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  362 VRG--LDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:PRK10253   8 LRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALFND-SVRANLTMGRERSDQ--ACWRALEIAQLADGVRrlPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVV 516
Cdd:PRK10253  88 QNATTPGDiTVQELVARGRYPHQPlfTRWRKEDEEAVTKAMQ--ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057  517 ILDEATSALDAATEYALHQALGDF--LEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAeGGLYARLYG 591
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-AELIERIYG 242

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

360-528

2.01e-15

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 2.01e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEigldcVREHVA--- 436
Cdd:PRK13538   2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYHqdl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHPALFND------SVRANLTMGRERSDQACWRALEIAQLAdGVRRLPQGldtvvgrsgvRLSGGQRQRLAIARMIL 510
Cdd:PRK13538  77 LYLGHQPGIKTeltaleNLRFYQRLHGPGDDEALWEALAQVGLA-GFEDVPVR----------QLSAGQQRRVALARLWL 145

                        170
                 ....*....|....*...
gi 15596057  511 AEPKVVILDEATSALDAA 528
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQ 163

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

377-570

2.02e-15

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 2.02e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  377 QLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL----EEIGLDCVREHVAVVLQHPALF-NDSVRA 451
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  452 NLTMGRERSDQAcwraleiaQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEy 531
Cdd:PRK11144  96 NLRYGMAKSMVA--------QFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK- 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15596057  532 alhQALGDFLEGRT------TLIVAHRLSAVKQ-ADRVLVFDGGHI 570
Cdd:PRK11144 165 ---RELLPYLERLAreinipILYVSHSLDEILRlADRVVVLEQGKV 207

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

360-574

3.13e-15

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: 75.10 E-value: 3.13e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGV-----PLEeigldc 430
Cdd:cd03266   2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkePAE------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 431 VREHVAVVLQHPALFND-SVRANLTM-----GRERsDQACWRALEIAQLADgvrrlpqgLDTVVGRSGVRLSGGQRQRLA 504
Cdd:cd03266  76 ARRRLGFVSDSTGLYDRlTARENLEYfaglyGLKG-DELTARLEELADRLG--------MEELLDRRVGGFSTGMRQKVA 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057 505 IARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVA-HRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218

ABC_6TM_Rv0194_D1_like

cd18543

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

77-333

4.08e-15

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: 75.98 E-value: 4.08e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  77 GYIGLMLAATLLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGe 156
Cdd:cd18543  36 SALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA- 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 157 TLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGN 236
Cdd:cd18543 115 FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFG 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 237 RQGYFLGRLGHRAQEVRDYAVasqwksdaagRASGLL--FQFGIDVFRAAAMLTVLL--------SDLSIGQMLAVFSYL 306
Cdd:cd18543 195 RERRELDRFEAAARRLRATRL----------RAARLRarFWPLLEALPELGLAAVLAlggwlvanGSLTLGTLVAFSAYL 264

                       250       260
                ....*....|....*....|....*..
gi 15596057 307 WFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18543 265 TMLVWPVRMLGWLLAMAQRARAAAERV 291

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

359-573

4.41e-15

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 4.41e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 359 GIEVRGLdfaygEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRyGGVPLEEIGLDC-VREHVAV 437
Cdd:COG2401  35 GVELRVV-----ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC-VDVPDNQFGREAsLIDAIGR 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 438 VLQhpalFNDSVRAnltmgrersdqacwraLEIAQLADGV--RRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKV 515
Cdd:COG2401 109 KGD----FKDAVEL----------------LNAVGLSDAVlwLRRFK-----------ELSTGQKFRFRLALLLAERPKL 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 516 VILDEATSALDAATEYALHQALGDFL-EGRTTLIVA-HRLSAVK--QADRVLVFD-GGHIAED 573
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVAtHHYDVIDdlQPDLLIFVGyGGVPEEK 220

MglA

COG1129

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

344-571

4.96e-15

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 4.96e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 344 RYPPLRDPFAgrtTVGIEVRGLdfayGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL 423
Cdd:COG1129 244 LFPKRAAAPG---EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 424 EE----------IGL---DcvREHVAVVLQHpalfndSVRANLTMGR-ERSDQACW--RALEIAQLADGVRRL---PQGL 484
Cdd:COG1129 317 RIrsprdairagIAYvpeD--RKGEGLVLDL------SIRENITLASlDRLSRGGLldRRRERALAEEYIKRLrikTPSP 388

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 485 DTVVGRsgvrLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIV------AHRLSavk 557
Cdd:COG1129 389 EQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAaEGKAVIVIsselpeLLGLS--- 461

                       250
                ....*....|....
gi 15596057 558 qaDRVLVFDGGHIA 571
Cdd:COG1129 462 --DRILVMREGRIV 473

ABC_6TM_YknV_like

cd18545

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

68-333

5.05e-15

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: 75.97 E-value: 5.05e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  68 LPADWQVAFGYIGLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDL 147
Cdd:cd18545  32 PNGDLSGLLIIALLFLALNLV----NWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 148 DTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLE 227
Cdd:cd18545 108 NSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESIS 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 228 AIQEVRAGNRQGYFLGRLGHRAQEVRDyavasQWKSdaAGRASGLLFQFgIDVFRAAAMLTVLL--------SDLSIGQM 299
Cdd:cd18545 188 GIRVIQSFAREDENEEIFDELNRENRK-----ANMR--AVRLNALFWPL-VELISALGTALVYWyggklvlgGAITVGVL 259

                       250       260       270
                ....*....|....*....|....*....|....*
gi 15596057 300 LAVFSYLWFMIGPVeQLLGLQY-AYYAAGGALQRI 333
Cdd:cd18545 260 VAFIGYVGRFWQPI-RNLSNFYnQLQSAMASAERI 293

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

359-575

5.14e-15

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.12 E-value: 5.14e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  359 GIEVRGLDFAygEDKVL-EQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSA----QRGSIRYGGVPLEEIGLDcvRE 433
Cdd:PRK10418   4 QIELRNIALQ--AAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  434 HVAVVLQHP-ALFN--DSVRAN-----LTMGRERSDQACWRALEIAQLADGVRrlpqgldtVVGRSGVRLSGGQRQRLAI 505
Cdd:PRK10418  80 KIATIMQNPrSAFNplHTMHTHaretcLALGKPADDATLTAALEAVGLENAAR--------VLKLYPFEMSGGMLQRMMI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057  506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRT--TLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGD 575
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGD 224

PRK03695

vitamin B12-transporter ATPase; Provisional

370-568

1.19e-14

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 1.19e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  370 GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQrGSIRYGGVPLEEIGLDCVREHVAVVLQH-PALFNDS 448
Cdd:PRK03695   7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  449 VRANLTMGRERSDQACWRALEIAQLADGVrrlpqGLDTVVGRSGVRLSGG--QRQRLA-----IARMILAEPKVVILDEA 521
Cdd:PRK03695  86 VFQYLTLHQPDKTRTEAVASALNEVAEAL-----GLDDKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15596057  522 TSALDAATEYALHQALGDFLE-GRTTLIVAHRLS-AVKQADRVLVFDGG 568
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQG 209

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

360-574

1.67e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 1.67e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLeeIGLDCVREH---VA 436
Cdd:PRK15439  12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC--ARLTPAKAHqlgIY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHPALF-NDSVRANLTMGRERsdqacwRALEIAQLADGVRRLPQGLDTVVgrSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:PRK15439  90 LVPQEPLLFpNLSVKENILFGLPK------RQASMQKMKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057  516 VILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

373-582

1.96e-14

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.99 E-value: 1.96e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGS--IRYGG--VPLEEIGLDC---VREHVAVVLQHPALF 445
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDGrgrAKRYIGILHQEYDLY 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   446 -NDSVRANLT--MGRERSDQ-ACWRALEIAQLAdgvrrlpqGLD-----TVVGRSGVRLSGGQRQRLAIARMILAEPKVV 516
Cdd:TIGR03269 378 pHRTVLDNLTeaIGLELPDElARMKAVITLKMV--------GFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIV 449

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057   517 ILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

360-571

2.10e-14

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.02 E-value: 2.10e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLY--SAQRGSIRYGGVPLEEIGL-DCVREHVA 436
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   437 VVLQHPALFND-SVRANLTMGRERSDQACWRAL-EIAQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPK 514
Cdd:TIGR02633  82 IIHQELTLVPElSVAENIFLGNEITLPGGRMAYnAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   515 VVILDEATSALDAATEYALHQALGDF-LEGRTTLIVAHRLSAVKQ-ADRVLVF-DGGHIA 571
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIrDGQHVA 221

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

358-586

2.69e-14

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 2.69e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 358 VGIEVRGLDFAyGEDKV--LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE--------EIG 427
Cdd:COG3845 256 VVLEVENLSVR-DDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglsprerrRLG 334

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 428 LDCV---REHVAVVLqhpalfNDSVRANLTMGRERSDQACWRAL----EIAQLAD------GVRrlPQGLDTVVGrsgvR 494
Cdd:COG3845 335 VAYIpedRLGRGLVP------DMSVAENLILGRYRRPPFSRGGFldrkAIRAFAEelieefDVR--TPGPDTPAR----S 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 495 LSGGQRQRLAIARMILAEPKVVILDEATSALD-AATEYaLHQALgdfLE----GRTTLIVAHRLSAVKQ-ADRVLVFDGG 568
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDvGAIEF-IHQRL---LElrdaGAAVLLISEDLDEILAlSDRIAVMYEG 478

                       250       260
                ....*....|....*....|...
gi 15596057 569 HI-----AEDGDHQQLiaegGLY 586
Cdd:COG3845 479 RIvgevpAAEATREEI----GLL 497

PRK13633

energy-coupling factor transporter ATPase;

360-574

3.53e-14

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 3.53e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDK------VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG-LDCVR 432
Cdd:PRK13633   5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQHP--ALFNDSVRANLTMG-----------RERSDQAcwraLEIAQLADGVRRLPQgldtvvgrsgvRLSGGQ 499
Cdd:PRK13633  85 NKAGMVFQNPdnQIVATIVEEDVAFGpenlgippeeiRERVDES----LKKVGMYEYRRHAPH-----------LLSGGQ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  500 RQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF--LEGRTTLIVAHRLSAVKQADRVLVFDGGHIAEDG 574
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

360-579

3.96e-14

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 3.96e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG--VP-LEEIGLDCVREHVA 436
Cdd:PRK11831   8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPaMSRSRLYTVRKRMS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHPALFNDsvranLTMgrerSDQACWRALEIAQLADGVRRlpqglDTV------VGRSGV------RLSGGQRQRLA 504
Cdd:PRK11831  88 MLFQSGALFTD-----MNV----FDNVAYPLREHTQLPAPLLH-----STVmmkleaVGLRGAaklmpsELSGGMARRAA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  505 IARMILAEPKVVILDEATSALDAATEYALHQaLGDFLE---GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVK-LISELNsalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231

PRK10261

glutathione transporter ATP-binding protein; Provisional

371-574

4.09e-14

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 4.09e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  371 EDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG---LDCVREHVAVVLQHPALFND 447
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYASLD 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  448 SVRA------------NLTMGRERSDQACWRALEIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKV 515
Cdd:PRK10261 416 PRQTvgdsimeplrvhGLLPGKAAAARVAWLLERVGLLPEHAWRYPH-----------EFSGGQRQRICIARALALNPKV 484

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057  516 VILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

360-571

4.38e-14

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 4.38e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG-LDCVREHVAVV 438
Cdd:PRK09700   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHPALFND-SVRANLTMGRERSDQAC------WRAL----EIAQLADGVRRlpqGLDTVVGrsgvRLSGGQRQRLAIAR 507
Cdd:PRK09700  86 YQELSVIDElTVLENLYIGRHLTKKVCgvniidWREMrvraAMMLLRVGLKV---DLDEKVA----NLSISHKQMLEIAK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  508 MILAEPKVVILDEATSAL-DAATEYALhqALGDFL--EGRTTLIVAHRLSAVKQ-ADRVLVF-DGGHIA 571
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLrkEGTAIVYISHKLAEIRRiCDRYTVMkDGSSVC 225

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

374-581

5.12e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 5.12e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQ-----RGSIRYGGVPL---EEIGLDCVR-EHVAVVLQHPAl 444
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQEPM- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 fndsVRANLTMGRERsdqacwRALEIAQLADGVRRLP------QGLDTVVGRSGVR--------LSGGQRQRLAIARMIL 510
Cdd:PRK15134 103 ----VSLNPLHTLEK------QLYEVLSLHRGMRREAargeilNCLDRVGIRQAAKrltdyphqLSGGERQRVMIAMALL 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057  511 AEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246

PRK13549

xylose transporter ATP-binding subunit; Provisional

360-573

6.77e-14

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 6.77e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLY--SAQRGSIRYGGVPLEEIGL-DCVREHVA 436
Cdd:PRK13549   6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIrDTERAGIA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHPALFND-SVRANLTMGRERS-------DQACWRALEI-AQLadgvrRLPQGLDTVVGrsgvRLSGGQRQRLAIAR 507
Cdd:PRK13549  86 IIHQELALVKElSVLENIFLGNEITpggimdyDAMYLRAQKLlAQL-----KLDINPATPVG----NLGLGQQQLVEIAK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  508 MILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLI-VAHRLSAVKQ-ADRVLVF-DGGHIAED 573
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIyISHKLNEVKAiSDTICVIrDGRHIGTR 225

PRK10070

proline/glycine betaine ABC transporter ATP-binding protein ProV;

380-580

9.55e-14

proline/glycine betaine ABC transporter ATP-binding protein ProV;

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 9.55e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  380 LNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVRE----HVAVVLQHPALF-NDSVRANLT 454
Cdd:PRK10070  49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNTA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  455 MGRERSDQACWRALEIAqlADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALH 534
Cdd:PRK10070 129 FGMELAGINAEERREKA--LDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15596057  535 QALGDFL--EGRTTLIVAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLI 580
Cdd:PRK10070 205 DELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

373-582

1.60e-13

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.60e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGL-DCVREHVAVVLQHPALFND-SVR 450
Cdd:PRK11288  18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLVPEmTVA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  451 ANLTMGR--------ERSDQACWRALEIAQLadGVRRLPqglDTVVGRsgvrLSGGQRQRLAIARMILAEPKVVILDEAT 522
Cdd:PRK11288  98 ENLYLGQlphkggivNRRLLNYEAREQLEHL--GVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  523 SALDA-ATE--YALHQALGDflEGRTTLIVAHRLSAVKQ-ADRVLVF-DGGHIA-----EDGDHQQLIAE 582
Cdd:PRK11288 169 SSLSArEIEqlFRVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFkDGRYVAtfddmAQVDRDQLVQA 236

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

367-579

1.80e-13

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.85 E-value: 1.80e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  367 FAYGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLL---LGLYSAQ---RGSIRYGGVPLEEIGLDCVREHVAVVL 439
Cdd:PRK14246  17 YLYINDKaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHPALF-NDSVRANLTMGRERSDQACWRalEIAQLADGVRR---LPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKV 515
Cdd:PRK14246  97 QQPNPFpHLSIYDNIAYPLKSHGIKEKR--EIKKIVEECLRkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057  516 VILDEATSALDAATEYALHQALGDFLEGRTTLIVAHR-LSAVKQADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239

ABC_6TM_exporter_like

cd18565

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

63-254

2.84e-13

Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 71.06 E-value: 2.84e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  63 FMDRLLPAD-WQVAFGYIGLMLAATLLLRgaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISA 141
Cdd:cd18565  40 VPASLGPADpRGQLWLLGGLTVAAFLLES----LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMS 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 142 HLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRV--KHLKKLEndSTARFT 219
Cdd:cd18565 116 VLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIepRYRAVRE--AVGDLN 193

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15596057 220 QALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRD 254
Cdd:cd18565 194 ARLENNLSGIAVIKAFTAEDFERERVADASEEYRD 228

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

373-570

2.99e-13

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: 68.83 E-value: 2.99e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLL---LGLYSAQRGSIRYGGVPLEEIGLDCVREhVAVVLQHpalfnDSV 449
Cdd:cd03233  21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGE-IIYVSEE-----DVH 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 450 RANLTmgrersdqacwraleIAQLADGVRRLpQGLDTVVGrsgvrLSGGQRQRLAIARMILAEPKVVILDEATSALDAAT 529
Cdd:cd03233  95 FPTLT---------------VRETLDFALRC-KGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15596057 530 eyALH-----QALGDFLEGrTTLIVAHRLS--AVKQADRVLVFDGGHI 570
Cdd:cd03233 154 --ALEilkciRTMADVLKT-TTFVSLYQASdeIYDLFDKVLVLYEGRQ 198

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

360-581

3.10e-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: 69.49 E-value: 3.10e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDC-VREHVAVV 438
Cdd:cd03218   1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 439 LQHPALFND-SVRANLTMgrersdqacwrALEIAQLADGVR--RLPQ-----GLDTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:cd03218  81 PQEASIFRKlTVEENILA-----------VLEIRGLSKKEReeKLEElleefHITHLRKSKASSLSGGERRRVEIARALA 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 511 AEPKVVILDEATSALD--AATEYalhQALGDFLEGRT--TLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:cd03218 150 TNPKFLLLDEPFAGVDpiAVQDI---QKIIKILKDRGigVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222

PRK10908

cell division ATP-binding protein FtsE;

370-570

3.10e-13

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 3.10e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  370 GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG---VPLEEIGLDCVREHVAVVLQ-HPALF 445
Cdd:PRK10908  13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQIGMIFQdHHLLM 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  446 NDSVRANLTMgrersdqacwrALEI--AQLADGVRRLPQGLDTV-----VGRSGVRLSGGQRQRLAIARMILAEPKVVIL 518
Cdd:PRK10908  93 DRTVYDNVAI-----------PLIIagASGDDIRRRVSAALDKVglldkAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15596057  519 DEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAV-KQADRVLVFDGGHI 570
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215

ABC_6TM_bac_exporter_ABCB8_10_like

cd18575

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

103-258

3.19e-13

Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 70.59 E-value: 3.19e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 103 LFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQL 182
Cdd:cd18575  59 LVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKL 138

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057 183 ALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVA 258
Cdd:cd18575 139 TLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR 214

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

372-567

4.71e-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: 72.09 E-value: 4.71e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   372 DKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL--------YSAQRGSIRYggVPLEE-IGLDCVREHVAvvlqHP 442
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY--VPQRPyMTLGTLRDQII----YP 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   443 ALFNDSVRanltmgRERSDQACWRALEIAQLADGVRRlPQGLDTVVGRSGVrLSGGQRQRLAIARMILAEPKVVILDEAT 522
Cdd:TIGR00954 539 DSSEDMKR------RGLSDKDLEQILDNVQLTHILER-EGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECT 610

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15596057   523 SALDAATEYALHQALGDFleGRTTLIVAHRLSAVKQADRVLVFDG 567
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMDG 653

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

360-540

6.82e-13

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.12 E-value: 6.82e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   360 IEVRGLDFAYGeDKVL-EQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGgvpleeiglDCVreHVAVV 438
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETV--KLAYV 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   439 LQhpalFNDSVRANLTMGRERSDqacwrALEIAQLadGVRRLPQglDTVVGRSGVR----------LSGGQRQRLAIARM 508
Cdd:TIGR03719 391 DQ----SRDALDPNKTVWEEISG-----GLDIIKL--GKREIPS--RAYVGRFNFKgsdqqkkvgqLSGGERNRVHLAKT 457

                         170       180       190
                  ....*....|....*....|....*....|..
gi 15596057   509 ILAEPKVVILDEATSALDAATEYALHQALGDF 540
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF 489

PRK10575

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

362-591

1.95e-12

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.95e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  362 VRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQH 441
Cdd:PRK10575  14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  442 -PALFNDSVRANLTMGRERSDQACWR--ALEIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVIL 518
Cdd:PRK10575  94 lPAAEGMTVRELVAIGRYPWHGALGRfgAADREKVEEAISLV--GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  519 DEATSALDAATE---YALHQALGDfLEGRTTLIVAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIaEGGLYARLYG 591
Cdd:PRK10575 172 DEPTSALDIAHQvdvLALVHRLSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM-RGETLEQIYG 246

livG

PRK11300

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional

360-568

2.66e-12

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.32 E-value: 2.66e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEI-GLDCVREHVAVV 438
Cdd:PRK11300   6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHPALFND-------------SVRANLTMG-------RERSDQACWRAleiAQLADGVrrlpqGLDTVVGRSGVRLSGG 498
Cdd:PRK11300  86 FQHVRLFREmtvienllvaqhqQLKTGLFSGllktpafRRAESEALDRA---ATWLERV-----GLLEHANRQAGNLAYG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057  499 QRQRLAIARMILAEPKVVILDEATSALDAATEYALhQALGDFLE---GRTTLIVAHRLSAVKQ-ADRVLVFDGG 568
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKEL-DELIAELRnehNVTVLLIEHDMKLVMGiSDRIYVVNQG 230

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

378-579

2.74e-12

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 2.74e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  378 LDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQ---RGSIRYGG---VPLEEIGLDCVR-EHVAVVLQHPAL-FNDSV 449
Cdd:PRK09473  35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreiLNLPEKELNKLRaEQISMIFQDPMTsLNPYM 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  450 RAnltmgrerSDQAcwraLEIAQLADG----------VRRLpqglDTVV---GRSGVRL-----SGGQRQRLAIARMILA 511
Cdd:PRK09473 115 RV--------GEQL----MEVLMLHKGmskaeafeesVRML----DAVKmpeARKRMKMyphefSGGMRQRVMIAMALLC 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596057  512 EPKVVILDEATSALDAATEYALHQALGDF-LEGRTTLI-VAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 579
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249

PRK10261

glutathione transporter ATP-binding protein; Provisional

362-579

3.87e-12

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.87e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  362 VRGLDFAYGEDK----VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL-----EEIGL---- 428
Cdd:PRK10261  15 VENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrQVIELseqs 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  429 DCVREHV-----AVVLQHPAL-----------FNDSVRANLTMGRERSDQACWRALEIAqladgvrRLPQGlDTVVGRSG 492
Cdd:PRK10261  95 AAQMRHVrgadmAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQV-------RIPEA-QTILSRYP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  493 VRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRT--TLIVAHRLSAVKQ-ADRVLVFDGGH 569
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGE 246

                        250
                 ....*....|
gi 15596057  570 IAEDGDHQQL 579
Cdd:PRK10261 247 AVETGSVEQI 256

ABC_6TM_Pgp_ABCB1_D2_like

cd18578

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

92-339

5.81e-12

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: 67.09 E-value: 5.81e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  92 AALVFNVLQAKLFARLSKDIVYRIRLRLIER-LRH-IALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLL 169
Cdd:cd18578  64 VAGIAYFLQGYLFGIAGERLTRRLRKLAFRAiLRQdIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLV 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 170 GTAAILVWMHWQLALLILLFNPLVIWSTVqlgKRVKHLKKLENDSTARFTQA---LTETLEAIQEVRAGNRQGYFLGRLG 246
Cdd:cd18578 144 AGLIIAFVYGWKLALVGLATVPLLLLAGY---LRMRLLSGFEEKNKKAYEESskiASEAVSNIRTVASLTLEDYFLEKYE 220

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 247 HRAQEVRDYAVASqwksdaaGRASGLLF---QFGIDVFRAAAML--TVLLSD--LSIGQMLAVFSYLWFMIGPVEQLLGL 319
Cdd:cd18578 221 EALEEPLKKGLRR-------ALISGLGFglsQSLTFFAYALAFWygGRLVANgeYTFEQFFIVFMALIFGAQSAGQAFSF 293

                       250       260
                ....*....|....*....|
gi 15596057 320 QYAYYAAGGALQRINELLAR 339
Cdd:cd18578 294 APDIAKAKAAAARIFRLLDR 313

PRK11147

ABC transporter ATPase component; Reviewed

361-578

6.85e-12

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 6.85e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  361 EVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYgGVPLEeigldcvrehVAVVLQ 440
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------VAYFDQ 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  441 HPALFN--DSVRANLTMGRErsdqacwralEIaqLADGVRRlpqgldTVVG------------RSGVR-LSGGQRQRLAI 505
Cdd:PRK11147 390 HRAELDpeKTVMDNLAEGKQ----------EV--MVNGRPR------HVLGylqdflfhpkraMTPVKaLSGGERNRLLL 451

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  506 ARMILAEPKVVILDEATSALDAATEYALHQALGDFlEGrTTLIVAHrlsavkqaDRVLV---------FDG-GHIAE--- 572
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSH--------DRQFVdntvtecwiFEGnGKIGRyvg 521


                 ....*....
gi 15596057  573 ---DGDHQQ 578
Cdd:PRK11147 522 gyhDARQQQ 530

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

360-583

7.50e-12

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.58 E-value: 7.50e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL--YSAQRGSIRYGGVPLEEIG-LDCVREHVA 436
Cdd:PRK09580   2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpEDRAGEGIF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  437 VVLQHPA---------LFNDSVRANltmgRERSDQACWRALEIAQLADGVRRLPQGLDTVVGRS-GVRLSGGQRQRLAIA 506
Cdd:PRK09580  82 MAFQYPVeipgvsnqfFLQTALNAV----RSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  507 RMILAEPKVVILDEATSALDAATEYALHQALGDFLEG-RTTLIVAH--RLSAVKQADRVLVFDGGHIAEDGDH---QQLI 580
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLE 237


                 ...
gi 15596057  581 AEG 583
Cdd:PRK09580 238 EQG 240

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

374-573

1.66e-11

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.42 E-value: 1.66e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPL----EEIGLDCVREHVAVVLQH-------P 442
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSfmliptlN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  443 ALFNDSVRANLTMGRERSDQACWRALeIAQLADGVR--RLPqgldtvvgrsgVRLSGGQRQRLAIARMILAEPKVVILDE 520
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKAL-LEQLGLGKRldHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  521 ATSALDAATeyalHQALGDFL-----EGRTTLI-VAHRLSAVKQADRVLVFDGGHIAED 573
Cdd:PRK10584 173 PTGNLDRQT----GDKIADLLfslnrEHGTTLIlVTHDLQLAARCDRRLRLVNGQLQEE 227

COG4586

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

373-589

1.91e-11

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 1.91e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG-VPLEEigldcvRE----HVAVVL-Q------ 440
Cdd:COG4586  36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKR------RKefarRIGVVFgQrsqlww 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 441 -HPALfnDSVRANltmgRE--RSDQACWRALeIAQLAD--GVRRLpqgLDTVVgRsgvRLSGGQRQRLAIARMILAEPKV 515
Cdd:COG4586 110 dLPAI--DSFRLL----KAiyRIPDAEYKKR-LDELVEllDLGEL---LDTPV-R---QLSLGQRMRCELAAALLHRPKI 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 516 VILDEATSALDAATEYALHqalgDFL-----EGRTTLIVA-HRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEGGLYAR 588
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIR----EFLkeynrERGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251


                .
gi 15596057 589 L 589
Cdd:COG4586 252 I 252

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

360-560

2.76e-11

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 2.76e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvplEEIGLD-CVREHVAVV 438
Cdd:PRK13540   2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER---QSIKKDlCTYQKQLCF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQHPALFND--SVRANLTMGRERSDQacwrALEIAQLADgVRRLPQGLDTVVGrsgvRLSGGQRQRLAIARMILAEPKVV 516
Cdd:PRK13540  79 VGHRSGINPylTLRENCLYDIHFSPG----AVGITELCR-LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLW 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15596057  517 ILDEATSALDA-ATEYALHQALGDFLEGRTTLIVAHRLSAVKQAD 560
Cdd:PRK13540 150 LLDEPLVALDElSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194

PRK15064

ABC transporter ATP-binding protein; Provisional

360-551

2.90e-11

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 2.90e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGgvplE--EIGLdCVREHVAV 437
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----EnaNIGY-YAQDHAYD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VLQHPALFNdsvranlTMGRERS----DQAcwraleiaqladgVR----RLPQGLDTvVGRSGVRLSGGQRQRLAIARMI 509
Cdd:PRK15064 395 FENDLTLFD-------WMSQWRQegddEQA-------------VRgtlgRLLFSQDD-IKKSVKVLSGGEKGRMLFGKLM 453

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15596057  510 LAEPKVVILDEATSALDAATEYALHQALGDFlEGrtTLI-VAH 551
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG--TLIfVSH 493

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

365-574

5.10e-11

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 5.10e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  365 LDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQ--------RGSIRYGGVPLEEIG---LDCVRe 433
Cdd:PRK13547   7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLR- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  434 hvAVVLQ--HPAlFNDSVRANLTMGR-----------ERSDQACWRALEIAqladgvrrlpqGLDTVVGRSGVRLSGGQR 500
Cdd:PRK13547  86 --AVLPQaaQPA-FAFSAREIVLLGRypharragaltHRDGEIAWQALALA-----------GATALVGRDVTTLSGGEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  501 QRLAIARMI---------LAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLS-AVKQADRVLVFDGG 568
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADG 231


                 ....*.
gi 15596057  569 HIAEDG 574
Cdd:PRK13547 232 AIVAHG 237

ABC_6TM_TmrB_like

cd18541

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

70-316

5.58e-11

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: 63.58 E-value: 5.58e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  70 ADWQVAFGYIGLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDT 149
Cdd:cd18541  34 LTASQLLRYALLILLLALL----IGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNA 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 150 LDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAI 229
Cdd:cd18541 110 VRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGI 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 230 QEVRAGNRQGYFLGRLGHRAQEVRDyavasqwKSDAAGRASGLLFQFgIDVFRAAAMLTVLL--------SDLSIGQMLA 301
Cdd:cd18541 190 RVIKAFVQEEAEIERFDKLNEEYVE-------KNLRLARVDALFFPL-IGLLIGLSFLIVLWyggrlvirGTITLGDLVA 261

                       250
                ....*....|....*
gi 15596057 302 VFSYLWFMIGPVEQL 316
Cdd:cd18541 262 FNSYLGMLIWPMMAL 276

PRK10636

putative ABC transporter ATP-binding protein; Provisional

369-582

6.58e-11

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 6.58e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  369 YGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYG-GVPLeeigldcvrehvAVVLQHPALFnd 447
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKL------------GYFAQHQLEF-- 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  448 svranltmgrERSDQACWRALeiAQLADgvRRLPQGLDTVVGRSGV----------RLSGGQRQRLAIARMILAEPKVVI 517
Cdd:PRK10636 388 ----------LRADESPLQHL--ARLAP--QELEQKLRDYLGGFGFqgdkvteetrRFSGGEKARLVLALIVWQRPNLLL 453

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  518 LDEATSALDAATEYALHQALGDFlEGrTTLIVAHRLSAVKQA--DRVLVFDGGHIAEDG---DHQQLIAE 582
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDF-EG-ALVVVSHDRHLLRSTtdDLYLVHDGKVEPFDGdleDYQQWLSD 521

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

381-567

1.05e-10

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.43 E-value: 1.05e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 381 NIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGsiryggvpleEIGLDcvREHVAVVLQH-PALFNDSVRANLtmgRER 459
Cdd:cd03237  21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG----------DIEIE--LDTVSYKPQYiKADYEGTVRDLL---SSI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 460 SDQACWRALEIAQLADgvrrlPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGD 539
Cdd:cd03237  86 TKDFYTHPYFKTEIAK-----PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 15596057 540 FLEG--RTTLIVAHR-LSAVKQADRVLVFDG 567
Cdd:cd03237 161 FAENneKTAFVVEHDiIMIDYLADRLIVFEG 191

ABC_6TM_YwjA_like

cd18549

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

62-327

1.07e-10

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: 62.85 E-value: 1.07e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  62 RFMDRLLPADwqvAFGYIGLMLAATLLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISA 141
Cdd:cd18549  27 YIIDDLLPSK---NLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 142 HLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQA 221
Cdd:cd18549 104 RITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQ 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 222 LTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDyAVASQWKSDAagrasglLFQFGIDVFRAAAMLTVLL--------SD 293
Cdd:cd18549 184 LEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLE-SKKKAYKAMA-------YFFSGMNFFTNLLNLVVLVaggyfiikGE 255

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15596057 294 LSIGQMLAVFSYLWFMIGPVEQLLGL--QYAYYAAG 327
Cdd:cd18549 256 ITLGDLVAFLLYVNVFIKPIRRLVNFteQYQKGMAG 291

PRK13543

heme ABC exporter ATP-binding protein CcmA;

364-526

1.09e-10

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 1.09e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  364 GLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIglDCVReHVAVVLQHPA 443
Cdd:PRK13543  16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSR-FMAYLGHLPG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  444 LFND-SVRANLTM-----GReRSDQACWRALEIAQLADGVrrlpqglDTVVGrsgvRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:PRK13543  93 LKADlSTLENLHFlcglhGR-RAKQMPGSALAIVGLAGYE-------DTLVR----QLSAGQKKRLALARLWLSPAPLWL 160


                 ....*....
gi 15596057  518 LDEATSALD 526
Cdd:PRK13543 161 LDEPYANLD 169

PLN03211

ABC transporter G-25; Provisional

385-568

1.13e-10

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.13e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  385 GEKVALVGASGGGKSTLVQLLLGLYSAQ--RGSIRY-GGVPLEEIgldcvREHVAVVLQHPALF-NDSVRANLT------ 454
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILAnNRKPTKQI-----LKRTGFVTQDDILYpHLTVRETLVfcsllr 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  455 MGRERSDQACWRALE--IAQLAdgvrrLPQGLDTVVGRSGVR-LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEY 531
Cdd:PLN03211 169 LPKSLTKQEKILVAEsvISELG-----LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15596057  532 ALHQALGDFLE-GRTTLIVAHRLSA-VKQA-DRVLVFDGG 568
Cdd:PLN03211 244 RLVLTLGSLAQkGKTIVTSMHQPSSrVYQMfDSVLVLSEG 283

ycf16

CHL00131

sulfate ABC transporter protein; Validated

360-575

1.33e-10

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.33e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLG--LYSAQRGSIRYGGVPLEEIGLDcVREHVAV 437
Cdd:CHL00131   8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE-ERAHLGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VL--QHPALFN-----DSVRANLTMGRERSDQACWRALEIAQLadgvrrLPQGLDtVVGRSGVRL--------SGGQRQR 502
Cdd:CHL00131  87 FLafQYPIEIPgvsnaDFLRLAYNSKRKFQGLPELDPLEFLEI------INEKLK-LVGMDPSFLsrnvnegfSGGEKKR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAH--RLSAVKQADRVLVFDGGHIAEDGD 575
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

373-551

1.52e-10

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.52e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRG------SIRYGGVPlEEIGLD---CVREHVAVVLQH-P 442
Cdd:TIGR03719  19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKVGYLP-QEPQLDptkTVRENVEEGVAEiK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   443 ALFN--DSVRANLT------------MGR--ERSDQA-CW---RALEIAQLAdgvRRLPQGlDTVVGRsgvrLSGGQRQR 502
Cdd:TIGR03719  98 DALDrfNEISAKYAepdadfdklaaeQAElqEIIDAAdAWdldSQLEIAMDA---LRCPPW-DADVTK----LSGGERRR 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15596057   503 LAIARMILAEPKVVILDEATSALDAATEYALHQALGDFlEGrTTLIVAH 551
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

359-520

1.57e-10

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.58 E-value: 1.57e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGV-----PLEE-----IGL 428
Cdd:COG1137   3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHKrarlgIGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 429 dcvrehvavvL-QHPALFND-SVRANLTMgrersdqacwrALEIAQLADGVR--RLPQ-----GLDTVVGRSGVRLSGGQ 499
Cdd:COG1137  83 ----------LpQEASIFRKlTVEDNILA-----------VLELRKLSKKEReeRLEElleefGITHLRKSKAYSLSGGE 141

                       170       180
                ....*....|....*....|.
gi 15596057 500 RQRLAIARMILAEPKVVILDE 520
Cdd:COG1137 142 RRRVEIARALATNPKFILLDE 162

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

385-589

2.30e-10

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 2.30e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   385 GEKVALVGASGGGKSTLVQLLLGLYSAQ-RGSIRYGGVPLE-EIGLDCVREHVAVVLQ----HPALFNDSVRANLTM--- 455
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEdrkrHGIVPILGVGKNITLsvl 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   456 ----GRERSDQACwralEIAQLADGVRRL---PQGLDTVVGRsgvrLSGGQRQRLAIARMILAEPKVVILDEATSALDAA 528
Cdd:TIGR02633 366 ksfcFKMRIDAAA----ELQIIGSAIQRLkvkTASPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057   529 TEYALHQALGDFL-EGRTTLIVAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:TIGR02633 438 AKYEIYKLINQLAqEGVAIIVVSSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500

ABC_6TM_Tm287_like

cd18548

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

71-313

2.64e-10

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: 61.65 E-value: 2.64e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  71 DWQVAFGYIGLMLAATLLlrgaALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTL 150
Cdd:cd18548  34 DLSYILRTGLLMLLLALL----GLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQV 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 151 DKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHL-----KKLEndstaRFTQALTET 225
Cdd:cd18548 110 QNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLfkkvqKKLD-----RLNRVVREN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 226 LEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwksdAAGRASGLL---FQFGIDVfraaAMLTVLL--------SDL 294
Cdd:cd18548 185 LTGIRVIRAFNREDYEEERFDKANDDLTDTSL-------KAGRLMALLnplMMLIMNL----AIVAILWfgghlinaGSL 253

                       250
                ....*....|....*....
gi 15596057 295 SIGQMLAVFSYLWFMIGPV 313
Cdd:cd18548 254 QVGDLVAFINYLMQILMSL 272

PRK15112

peptide ABC transporter ATP-binding protein SapF;

378-581

3.31e-10

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.96 E-value: 3.31e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  378 LDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIGLDCVREHVAVVLQHPA-----------LFN 446
Cdd:PRK15112  32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisqILD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  447 DSVRANLTMGRERSDQACWRAL-EIAQLADGVRRLPQgldtvvgrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSAL 525
Cdd:PRK15112 112 FPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALASL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  526 DAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 581
Cdd:PRK15112 181 DMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

368-582

4.68e-10

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 4.68e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRyggVPLEEIGL----DCVREHVAVVLQHPA 443
Cdd:PRK10895  12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---IDDEDISLlplhARARRGIGYLPQEAS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  444 LFND-SVRANLTMGRE-RSDqacwraLEIAQLADGVRRLPQGLDTVVGRS--GVRLSGGQRQRLAIARMILAEPKVVILD 519
Cdd:PRK10895  89 IFRRlSVYDNLMAVLQiRDD------LSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596057  520 EATSALDAATEYALHQALGDFLE-GRTTLIVAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLIAE 582
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

374-570

5.87e-10

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 5.87e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    374 VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLG-LYSAQR---GSIRYGGVPLEEIgldcVREHVAVVLQ------H-P 442
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIgveGVITYDGITPEEI----KKHYRGDVVYnaetdvHfP 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    443 AL-------FNDSVR--ANLTMGRERSDqacwRALEIAQLADGVRRLPQGLDTVVGRSGVR-LSGGQRQRLAIARMILAE 512
Cdd:TIGR00956  152 HLtvgetldFAARCKtpQNRPDGVSREE----YAKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGG 227

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057    513 PKVVILDEATSALDAATEYALHQAL---GDFLEGrTTLIVAHRLS--AVKQADRVLVFDGGHI 570
Cdd:TIGR00956  228 AKIQCWDNATRGLDSATALEFIRALktsANILDT-TPLVAIYQCSqdAYELFDKVIVLYEGYQ 289

ABC_6TM_Pgp_ABCB1_D1_like

cd18577

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

76-303

6.34e-10

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: 60.57 E-value: 6.34e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  76 FGYIGLmlaatlllrgAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVG 155
Cdd:cd18577  53 FVYLGI----------GSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIG 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 156 ETLSRFLVALLTLLgtAAILV--WMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVR 233
Cdd:cd18577 123 EKLGLLIQSLSTFI--AGFIIafIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVK 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596057 234 AGNRQGYFLGRLGHRAQEVRDYAVasqWKSDAAGRASGLLFqFGIDVFRAAAML--TVLLSD--LSIGQMLAVF 303
Cdd:cd18577 201 AFGGEEKEIKRYSKALEKARKAGI---KKGLVSGLGLGLLF-FIIFAMYALAFWygSRLVRDgeISPGDVLTVF 270

PRK15056

manganese/iron ABC transporter ATP-binding protein;

385-558

6.52e-10

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 6.52e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVP----LEEIGLDCVREHVAVVLQHPALFNDSVRANLT--MGRE 458
Cdd:PRK15056  33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqaLQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYghMGWL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  459 RSDQACWRALEIAQLAdgvrRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALG 538
Cdd:PRK15056 113 RRAKKRDRQIVTAALA----RV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR 186

                        170       180
                 ....*....|....*....|.
gi 15596057  539 DFL-EGRTTLIVAHRLSAVKQ 558
Cdd:PRK15056 187 ELRdEGKTMLVSTHNLGSVTE 207

GguA

NF040905

sugar ABC transporter ATP-binding protein;

373-570

7.18e-10

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 7.18e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSA--QRGSIRYGGvplEEIGLDCVR--EHVAVVLQH------P 442
Cdd:NF040905  15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDG---EVCRFKDIRdsEALGIVIIHqelaliP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  443 ALfndSVRANLTMGRERS-------DQACWRALEIaqLAD-GVRRLPqglDTVVGRSGVrlsgGQRQRLAIARMILAEPK 514
Cdd:NF040905  92 YL---SIAENIFLGNERAkrgvidwNETNRRAREL--LAKvGLDESP---DTLVTDIGV----GKQQLVEIAKALSKDVK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  515 VVILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVF-DGGHI 570
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRvADSITVLrDGRTI 218

ABC_6TM_TAP

cd18572

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

87-326

7.92e-10

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: 60.25 E-value: 7.92e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  87 LLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALL 166
Cdd:cd18572  43 LLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 167 TLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAgnrqgyflgrLG 246
Cdd:cd18572 123 QLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRS----------FA 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 247 HRAQEVRDYAVASQ------WKSDAAgrasGLLFQFGIDVFRAAAMLTVLL--------SDLSIGQMLAVFSYLWFMIGP 312
Cdd:cd18572 193 TEEREARRYERALDkalklsVRQALA----YAGYVAVNTLLQNGTQVLVLFygghlvlsGRMSAGQLVTFMLYQQQLGEA 268

                       250
                ....*....|....*...
gi 15596057 313 VEQLL----GLQYAYYAA 326
Cdd:cd18572 269 FQSLGdvfsSLMQAVGAA 286

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

385-575

8.33e-10

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 8.33e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    385 GEKVALVGASGGGKSTLVQLLlglysAQR--------GSIRYGGVPLEE---------------IGLDCVREHV--AVVL 439
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLLNVL-----AERvttgvitgGDRLVNGRPLDSsfqrsigyvqqqdlhLPTSTVRESLrfSAYL 863

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    440 QHPALFNDSvranltmgrERSD--QACWRALEIAQLADGVrrlpqgldtvVGRSGVRLSGGQRQRLAIARMILAEPKVVI 517
Cdd:TIGR00956  864 RQPKSVSKS---------EKMEyvEEVIKLLEMESYADAV----------VGVPGEGLNVEQRKRLTIGVELVAKPKLLL 924

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057    518 -LDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAV--KQADRVLVFD-GGHIAEDGD 575
Cdd:TIGR00956  925 fLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAIlfEEFDRLLLLQkGGQTVYFGD 987

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

368-570

1.64e-09

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 1.64e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSI------RYGGVPlEEIGLDcvrehvavvlqh 441
Cdd:PRK09544  13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrngklRIGYVP-QKLYLD------------ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  442 PALfndsvraNLTMGRersdqacwraleIAQLADGVRR---LPqGLDTV-----VGRSGVRLSGGQRQRLAIARMILAEP 513
Cdd:PRK09544  80 TTL-------PLTVNR------------FLRLRPGTKKediLP-ALKRVqaghlIDAPMQKLSGGETQRVLLARALLNRP 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  514 KVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAV-KQADRVLVFDgGHI 570
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLN-HHI 198

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

382-568

2.44e-09

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 2.44e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 382 IGAGEKVALVGASGGGKSTLVQLLlglysAQR-------GSIRYGGVPLEEigldCVREHVAVVLQHPALFndsvrANLT 454
Cdd:cd03232  30 VKPGTLTALMGESGAGKTTLLDVL-----AGRktagvitGEILINGRPLDK----NFQRSTGYVEQQDVHS-----PNLT 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 455 MgRErsdqacwrALEIAQLADGvrrlpqgldtvvgrsgvrLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALH 534
Cdd:cd03232  96 V-RE--------ALRFSALLRG------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15596057 535 QALGDF-LEGRTTLIVAHRLSAV--KQADRVLVFDGG 568
Cdd:cd03232 149 RFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185

ABC_6TM_ABCB10_like

cd18573

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

111-328

2.49e-09

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: 58.68 E-value: 2.49e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 111 IVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFN 190
Cdd:cd18573  72 IVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVV 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 191 PLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVasqwksdAAGRAS 270
Cdd:cd18573 152 PPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAK-------KEALAS 224

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057 271 GLLF---QFGIDVfraaAMLTVLL--------SDLSIGQMLAvfsylwFMIgpveqllglqYAYYAAGG 328
Cdd:cd18573 225 GLFFgstGFSGNL----SLLSVLYyggslvasGELTVGDLTS------FLM----------YAVYVGSS 273

PRK10762

D-ribose transporter ATP binding protein; Provisional

385-581

4.04e-09

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.04e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE----EIGLDCV-------REHVAVVLQHpalfndSVRAN- 452
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspQDGLANGivyisedRKRDGLVLGM------SVKENm 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  453 -LTMGRERSDQACW--RALEIAQLADGVR----RLPqGLDTVVGRsgvrLSGGQRQRLAIARMILAEPKVVILDEATSAL 525
Cdd:PRK10762 352 sLTALRYFSRAGGSlkHADEQQAVSDFIRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057  526 DAATEYALHQALGDF-LEGRTTLIVAHRLSAV-KQADRVLVFDGGHI-----AEDGDHQQLIA 581
Cdd:PRK10762 427 DVGAKKEIYQLINQFkAEGLSIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLMA 489

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

385-567

4.55e-09

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 4.55e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIryggvpleEIGLDcvrehVAVVLQHP-ALFNDSVRANLTMGRERSDQA 463
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK-----ISYKPQYIsPDYDGTVEEFLRSANTDDFGS 432

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 464 CWRALEIAQladgvrrlPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEG 543
Cdd:COG1245 433 SYYKTEIIK--------PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504

                       170       180
                ....*....|....*....|....*..
gi 15596057 544 R--TTLIVAHRLSAVKQ-ADRVLVFDG 567
Cdd:COG1245 505 RgkTAMVVDHDIYLIDYiSDRLMVFEG 531

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

385-572

5.45e-09

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 5.45e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG-LDCVREHVAVVLQH---PALF-NDSVRANLTMGRER 459
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITESrrdNGFFpNFSIAQNMAISRSL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  460 SDQACWRALEI------AQLADGVRRLPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATE--- 530
Cdd:PRK09700 369 KDGGYKGAMGLfhevdeQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKaei 448

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15596057  531 YALHQALGDflEGRTTLIVAHRLSAVKQA-DRVLVFDGGHIAE 572
Cdd:PRK09700 449 YKVMRQLAD--DGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

330-540

7.35e-09

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 7.35e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  330 LQRINELLARADEPR-------YPPlrDPFAGrtTVGIEVRGLDFAYGeDKVL-EQLDLNIGAGEKVALVGASGGGKSTL 401
Cdd:PRK11819 292 LARYEELLSEEYQKRnetneifIPP--GPRLG--DKVIEAENLSKSFG-DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTL 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  402 VQLLLGLYSAQRGSIRYGgvpleeiglDCVreHVAVVLQhpalFNDSVRANLTMGRERSDqacwrALEIAQLadGVRRLP 481
Cdd:PRK11819 367 FKMITGQEQPDSGTIKIG---------ETV--KLAYVDQ----SRDALDPNKTVWEEISG-----GLDIIKV--GNREIP 424

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  482 QglDTVVGRSGVR----------LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF 540
Cdd:PRK11819 425 S--RAYVGRFNFKggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF 491

PRK13549

xylose transporter ATP-binding subunit; Provisional

385-589

1.15e-08

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.15e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  385 GEKVALVGASGGGKSTLVQLLLGLY-SAQRGSIRYGGVPLE-EIGLDCVREHVAVV----LQHPALFNDSVRANLTM--- 455
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVpedrKRDGIVPVMGVGKNITLaal 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  456 ----GRERSDQacwrALEIAQLADGVRRLPQGLDTVVGRSGvRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEY 531
Cdd:PRK13549 368 drftGGSRIDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  532 ALHQALGDFL-EGRTTLIVAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIAEGGLYARL 589
Cdd:PRK13549 443 EIYKLINQLVqQGVAIIVISSELPEVlGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAAL 502

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

378-571

1.31e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 1.31e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  378 LDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGvplEEIGLDCVREHVAVVL-------QHPALFNDSVR 450
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALSTAQRLARGLvylpedrQSSGLYLDAPL 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  451 ANLTMGRERSDQACW--RALEIAQLADGVRRLpqGLDTVVGRSGVR-LSGGQRQRLAIARMILAEPKVVILDEATSALDA 527
Cdd:PRK15439 359 AWNVCALTHNRRGFWikPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15596057  528 ATEYALHQALGDFLE-GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIA 571
Cdd:PRK15439 437 SARNDIYQLIRSIAAqNVAVLFISSDLEEIEQmADRVLVMHQGEIS 482

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

373-525

1.42e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.42e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLE--------EIGLDCVREHVAVVLQHpal 444
Cdd:PRK10982  12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealENGISMVHQELNLVLQR--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 fndSVRANLTMGRE-------------RSDQACWRALEIaqladgvrrlpqglDTVVGRSGVRLSGGQRQRLAIARMILA 511
Cdd:PRK10982  89 ---SVMDNMWLGRYptkgmfvdqdkmyRDTKAIFDELDI--------------DIDPRAKVATLSVSQMQMIEIAKAFSY 151

                        170
                 ....*....|....
gi 15596057  512 EPKVVILDEATSAL 525
Cdd:PRK10982 152 NAKIVIMDEPTSSL 165

PLN03140

ABC transporter G family member; Provisional

389-554

3.31e-08

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.31e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   389 ALVGASGGGKSTLVQLLLGLYSAQ--RGSIRYGGVPLEE-----IGLDCVREHV---AVVLQHPALFNDSVRANLTMGRE 458
Cdd:PLN03140  910 ALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQetfarISGYCEQNDIhspQVTVRESLIYSAFLRLPKEVSKE 989

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   459 RSDQACWRALEIAQLaDGVRrlpqglDTVVGRSGVR-LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQAL 537
Cdd:PLN03140  990 EKMMFVDEVMELVEL-DNLK------DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062

                         170
                  ....*....|....*...
gi 15596057   538 GDFLE-GRTTLIVAHRLS 554
Cdd:PLN03140 1063 RNTVDtGRTVVCTIHQPS 1080

40850658_otr

NF000106

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

359-584

3.45e-08

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 3.45e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  359 GIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGG--KSTLVQLLLGLySAQRGSIRYGGVPLEEIGLD-CVREHV 435
Cdd:NF000106  13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP-DAGRRPWRF*TWCANRRALRrTIG*HR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  436 AVVLQHPALFndSVRANLTM-GR----ERSDqACWRALEIaqladgVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:NF000106  92 PVR*GRRESF--SGRENLYMiGR*ldlSRKD-ARARADEL------LERF--SLTEAAGRAAAKYSGGMRRRLDLAASMI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  511 AEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAEGG 584
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

382-567

3.54e-08

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 3.54e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  382 IGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIryggvpleEIGLDcvrehVAVVLQH-PALFNDSVRANLTMGRERS 460
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK-----ISYKPQYiKPDYDGTVEDLLRSITDDL 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  461 DQACWRAlEIAQladgvrrlPQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF 540
Cdd:PRK13409 429 GSSYYKS-EIIK--------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499

                        170       180       190
                 ....*....|....*....|....*....|
gi 15596057  541 LEGR--TTLIVAHRLSAVKQ-ADRVLVFDG 567
Cdd:PRK13409 500 AEEReaTALVVDHDIYMIDYiSDRLMVFEG 529

ABC_6TM_PrtD_LapB_HlyB_like

cd18782

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

76-333

3.59e-08

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: 55.29 E-value: 3.59e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  76 FGYIGLMLAATLLLRGAAL---VFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLvTDLDTLDK 152
Cdd:cd18782  35 QQDLATLYVIGVVMLVAALleaVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 153 F-VGETLSRFLVALLTLLgTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQE 231
Cdd:cd18782 114 FlTGTALTTLLDVLFSVI-YIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQT 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 232 VRAGNRQgyflgrLGHRAQEVRDYA--VASQWKSDAAGRASGLLFQFGIDVFRAAAMLT----VLLSDLSIGQMLAVFSY 305
Cdd:cd18782 193 VKAQNAE------LKARWRWQNRYArsLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVgaylVLRGELTLGQLIAFRIL 266

                       250       260
                ....*....|....*....|....*...
gi 15596057 306 LWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18782 267 SGYVTGPILRLSTLWQQFQELRVSLERL 294

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

375-574

6.99e-08

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 6.99e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLllGLYSAqrGSIRYGGVPleeigldcvrehvAVVLQHPALFNDSVRANLT 454
Cdd:cd03238  11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYAS--GKARLISFL-------------PKFSRNKLIFIDQLQFLID 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 455 MGRersdqacwraleiaqladGVRRLPQGLDTvvgrsgvrLSGGQRQRLAIARMILAEPK--VVILDEATSALDAATEYA 532
Cdd:cd03238  74 VGL------------------GYLTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15596057 533 LHQALGDFL-EGRTTLIVAHRLSAVKQADRVLVF------DGGHIAEDG 574
Cdd:cd03238 128 LLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176

ABC_6TM_AtABCB27_like

cd18780

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...

95-290

1.04e-07

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: 53.79 E-value: 1.04e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  95 VFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAI 174
Cdd:cd18780  57 IATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVF 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 175 LVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFLGRLGHRAQEVRD 254
Cdd:cd18780 137 MFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYL 216

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15596057 255 YAVASqwksdaaGRASGlLFQFGIDVFRAAAMLTVL 290
Cdd:cd18780 217 LGKKL-------ARASG-GFNGFMGAAAQLAIVLVL 244

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

368-551

1.86e-07

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 1.86e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDK-VLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL---YS----AQRGsIRYGGVPlEEIGLD-------CVR 432
Cdd:PRK11819  15 VVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkeFEgearPAPG-IKVGYLP-QEPQLDpektvreNVE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  433 EHVAVVLQHPALFNDsVRANLT------------MGR--ERSDQA-CW---RALEIAqlADGVRrLPQGlDTVVGRsgvr 494
Cdd:PRK11819  93 EGVAEVKAALDRFNE-IYAAYAepdadfdalaaeQGElqEIIDAAdAWdldSQLEIA--MDALR-CPPW-DAKVTK---- 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  495 LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFlEGrTTLIVAH 551
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY-PG-TVVAVTH 218

ABC_6TM_TAP1

cd18589

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...

114-278

2.79e-07

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: 52.47 E-value: 2.79e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 114 RIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLILLFNPLV 193
Cdd:cd18589  70 RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLL 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 194 IWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRA-GNRQG---YFLGRL--GHR--AQEVRDYAVaSQWKSDa 265
Cdd:cd18589 150 LLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSfANEEGeaqRYRQRLqkTYRlnKKEAAAYAV-SMWTSS- 227

                       170
                ....*....|...
gi 15596057 266 agrASGLLFQFGI 278
Cdd:cd18589 228 ---FSGLALKVGI 237

ABC_6TM_Sav1866_like

cd18554

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

106-333

3.49e-07

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: 52.04 E-value: 3.49e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 106 RLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALL 185
Cdd:cd18554  72 WIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFV 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 186 ILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRA-----------GNRQGYFLGR-LGHRAQEVR 253
Cdd:cd18554 152 SLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSfalekheqkqfDKRNGHFLTRaLKHTRWNAK 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 254 DYAVASqwksdaagrasgLLFQFGIDVFRAAAMLTVLLSDLSIGQMLAVFSYLWFMIGPVEQLLGLQYAYYAAGGALQRI 333
Cdd:cd18554 232 TFSAVN------------TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

373-574

6.56e-07

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 6.56e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  373 KVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL------YSAQRgsIRYGGVPLEEIG----LDCVREHVAVVLQHP 442
Cdd:PRK11022  21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAEK--LEFNGQDLQRISekerRNLVGAEVAMIFQDP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  443 AlfnDSVRANLTMGRErsdqaCWRALEIAQLADGVRRLPQGLD--TVVG------RSGV---RLSGGQRQRLAIARMILA 511
Cdd:PRK11022  99 M---TSLNPCYTVGFQ-----IMEAIKVHQGGNKKTRRQRAIDllNQVGipdpasRLDVyphQLSGGMSQRVMIAMAIAC 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  512 EPKVVILDEATSALDAATEYALHQALGDFL--EGRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAEDG 574
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETG 236

AAA

smart00382

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

385-560

1.51e-06

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 1.51e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIryggvpleeigldcvrehvavvlqhpalfndsVRANLTMGRERSDQac 464
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLD-- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057    465 wraleiaqladgvrrlpQGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL--- 541
Cdd:smart00382  48 -----------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110

                          170       180
                   ....*....|....*....|..
gi 15596057    542 ---EGRTTLIVAHRLSAVKQAD 560
Cdd:smart00382 111 lksEKNLTVILTTNDEKDLGPA 132

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

385-554

1.59e-06

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 1.59e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGsiRYGGVP--------------------LEEIGLDCVREhVAVVLQHPAL 444
Cdd:cd03236  26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeildefrgselqnyftkLLEGDVKVIVK-PQYVDLIPKA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 445 FNDSVRANLtmgrERSDqacwralEIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSA 524
Cdd:cd03236 103 VKGKVGELL----KKKD-------ERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169

                       170       180       190
                ....*....|....*....|....*....|.
gi 15596057 525 LDAATEYALHQALGDFLE-GRTTLIVAHRLS 554
Cdd:cd03236 170 LDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200

PRK11147

ABC transporter ATPase component; Reviewed

368-540

1.59e-06

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.59e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  368 AYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG----------VPLEEIGldCVREHVAV 437
Cdd:PRK11147  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdPPRNVEG--TVYDFVAE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VLQHPA------------LFNDSVRANLT-MGR--ERSD-QACWRaLEiAQLADGVRRLpqGLDTVVGRSgvRLSGGQRQ 501
Cdd:PRK11147  90 GIEEQAeylkryhdishlVETDPSEKNLNeLAKlqEQLDhHNLWQ-LE-NRINEVLAQL--GLDPDAALS--SLSGGWLR 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15596057  502 RLAIARMILAEPKVVILDEATSALDAATEYALHQALGDF 540
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF 202

ABC_6TM_Pgp_ABCB1

cd18558

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

87-303

2.09e-06

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: 49.97 E-value: 2.09e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  87 LLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALL 166
Cdd:cd18558  66 LIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIA 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 167 TLLGTAAILVWMHWQLALLILLFNPL-----VIWSTVQLGKRVKHLKKLENDStarftQALTETLEAIQEVRAGNRQGYF 241
Cdd:cd18558 146 TFGTGFIIGFIRGWKLTLVILAISPVlglsaVVWAKILSGFTDKEKKAYAKAG-----AVAEEVLEAFRTVIAFGGQQKE 220

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596057 242 LGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFGIDV-FRAAAMLtVLLSDLSIGQMLAVF 303
Cdd:cd18558 221 ETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALaFWYGTYL-VTQQEYSIGEVLTVF 282

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

343-526

2.32e-06

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.32e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  343 PRYPPLRDPFAgrttvgIEVRGLDFAYGE----DKVleqlDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRY 418
Cdd:NF033858 256 PRPADDDDEPA------IEARGLTMRFGDftavDHV----SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  419 GGVPLEEIGLDcVREHVAVVLQHPALFND-SVRANLT-------MGRERSDQACWRALEIAQLADGVRRLPQgldtvvgr 490
Cdd:NF033858 326 FGQPVDAGDIA-TRRRVGYMSQAFSLYGElTVRQNLElharlfhLPAAEIAARVAEMLERFDLADVADALPD-------- 396

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15596057  491 sgvRLSGGQRQRLAIARMILAEPKVVILDEATSALD 526
Cdd:NF033858 397 ---SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

367-589

5.45e-06

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 5.45e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  367 FAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLL---LGLYSAQRgsiryggvpleeiglDCVREHVAVV----L 439
Cdd:PRK10938  11 FRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALageLPLLSGER---------------QSQFSHITRLsfeqL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHpaLFNDS-VRANLTMGRERSDQACWRALEIAQlaDGVR------RLPQ--GLDTVVGRSGVRLSGGQRQRLAIARMIL 510
Cdd:PRK10938  76 QK--LVSDEwQRNNTDMLSPGEDDTGRTTAEIIQ--DEVKdparceQLAQqfGITALLDRRFKYLSTGETRKTLLCQALM 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  511 AEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLI-VAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIAEgGLYAR 588
Cdd:PRK10938 152 SEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQ 230


                 .
gi 15596057  589 L 589
Cdd:PRK10938 231 L 231

ABC_UvrA_II

cd03271

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...

375-583

9.54e-06

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 9.54e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 375 LEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRgSIRYGGVPLE---EIGLDCVrEHVAVVLQHP--------- 442
Cdd:cd03271  11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARR-LHLKKEQPGNhdrIEGLEHI-DKVIVIDQSPigrtprsnp 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 443 --------------------ALFNDSVRANLTMGRERSD---QACWRALE----IAQLADGVRRLPQ-GLDTV-VGRSGV 493
Cdd:cd03271  89 atytgvfdeirelfcevckgKRYNRETLEVRYKGKSIADvldMTVEEALEffenIPKIARKLQTLCDvGLGYIkLGQPAT 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 494 RLSGGQRQRLAIARMILAE---PKVVILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQADRVLvfDGGh 569
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWII--DLG- 245

                       250
                ....*....|....*
gi 15596057 570 iAEDGDH-QQLIAEG 583
Cdd:cd03271 246 -PEGGDGgGQVVASG 259

PRK00635

excinuclease ABC subunit A; Provisional

483-563

1.05e-05

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.05e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   483 GLDTV-VGRSGVRLSGGQRQRLAIARMILA---EPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRLSAVK 557
Cdd:PRK00635  797 GLDYLpLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVK 876


                  ....*.
gi 15596057   558 QADRVL 563
Cdd:PRK00635  877 VADYVL 882

PLN03073

ABC transporter F family; Provisional

329-551

1.09e-05

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.09e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  329 ALQRINELLARADEPRYP---PLRDPFAGRTTvgIEVRGLDFAY-GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQL 404
Cdd:PLN03073 477 ALDRLGHVDAVVNDPDYKfefPTPDDRPGPPI--ISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  405 LLGLYSAQRGSIryggvpleeigLDCVREHVAVVLQHPALFND-SVRANLTMGRersdqaCWraleiaqlaDGVrrLPQG 483
Cdd:PLN03073 555 ISGELQPSSGTV-----------FRSAKVRMAVFSQHHVDGLDlSSNPLLYMMR------CF---------PGV--PEQK 606

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057  484 LDTVVGRSGVR----------LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGrtTLIVAH 551
Cdd:PLN03073 607 LRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

477-553

1.11e-05

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.11e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596057  477 VRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLEGRTTLIVAHRL 553
Cdd:PRK13409 197 VERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271

ABC_6TM_ABCB9_like

cd18784

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...

104-233

1.17e-05

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: 47.31 E-value: 1.17e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 104 FARLSkdivYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLA 183
Cdd:cd18784  64 MARLN----IRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLS 139

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15596057 184 LLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVR 233
Cdd:cd18784 140 LVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVR 189

ABC_6TM_exporter_like

cd18540

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

77-316

1.33e-05

Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 47.47 E-value: 1.33e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  77 GYIGLMLAATLLLRGAALVFNVLQAKLfarlSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLdkfvGE 156
Cdd:cd18540  43 GFILLYLGLILIQALSVFLFIRLAGKI----EMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRL----GE 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 157 TLSRFLV----ALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEV 232
Cdd:cd18540 115 IISWGLVdlvwGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTT 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 233 RAGNRQGYFLGRLGHRAQEVRDYAVasqwksdAAGRASGLLF---QFGIDVFRAAAMLT----VLLSDLSIGQMLAVFSY 305
Cdd:cd18540 195 KTLVREEKNLREFKELTEEMRRASV-------RAARLSALFLpivLFLGSIATALVLWYggilVLAGAITIGTLVAFISY 267

                       250
                ....*....|.
gi 15596057 306 LWFMIGPVEQL 316
Cdd:cd18540 268 ATQFFEPIQQL 278

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

493-567

1.82e-05

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 1.82e-05

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596057 493 VRLSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDG 567
Cdd:cd03222  70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFEG 147

ABC_6TM_AarD_CydD

cd18584

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...

81-194

2.12e-05

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: 46.63 E-value: 2.12e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  81 LMLAATLLLRGAalvFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFvgetLSR 160
Cdd:cd18584  41 LLLLAALLLRAL---LAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGY----FAR 113

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15596057 161 FLVAL-LTLLGTAAILV---WMHWQLALLILLFNPLVI 194
Cdd:cd18584 114 YLPQLvLAAIVPLLILVavfPLDWVSALILLVTAPLIP 151

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

334-526

3.06e-05

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.06e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  334 NELLARADEPRYPPLRDPFAGRttvgIEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLG------ 407
Cdd:PRK10938 239 GVQLPEPDEPSARHALPANEPR----IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgy 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  408 -----LYSAQRGSirygGVPLEEIgldcvREHVAVV---LQHPALFNDSVRANLTMGRERSdqacwraLEIAQ-LADGVR 478
Cdd:PRK10938 315 sndltLFGRRRGS----GETIWDI-----KKHIGYVsssLHLDYRVSTSVRNVILSGFFDS-------IGIYQaVSDRQQ 378

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596057  479 RLPQ------GLDTVVGRSGVR-LSGGQrQRLA-IARMILAEPKVVILDEATSALD 526
Cdd:PRK10938 379 KLAQqwldilGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

358-578

3.18e-05

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 3.18e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  358 VGIEVRGLDfaygEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPleeigldcvrehvaV 437
Cdd:PRK11288 256 VRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP--------------I 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  438 VLQHPAlfnDSVRANLTMGRErsDQACWRALEIAQLADGV----RR--LPQGL-----------DTVVGRSGVR------ 494
Cdd:PRK11288 318 DIRSPR---DAIRAGIMLCPE--DRKAEGIIPVHSVADNInisaRRhhLRAGClinnrweaenaDRFIRSLNIKtpsreq 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  495 ----LSGGQRQRLAIARMiLAEP-KVVILDEATSALD--AATE-YALHQALGDflEGRTTLIVAHRLSAVKQ-ADRVLVF 565
Cdd:PRK11288 393 limnLSGGNQQKAILGRW-LSEDmKVILLDEPTRGIDvgAKHEiYNVIYELAA--QGVAVLFVSSDLPEVLGvADRIVVM 469

                        250
                 ....*....|...
gi 15596057  566 DGGHIAEDGDHQQ 578
Cdd:PRK11288 470 REGRIAGELAREQ 482

PRK10636

putative ABC transporter ATP-binding protein; Provisional

382-526

3.53e-05

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 3.53e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  382 IGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGG---------------VPLEEIGLDCVREH--VAVVLQHPAL 444
Cdd:PRK10636  24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPALEYVIDGDREYrqLEAQLHDANE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  445 FNDSVRANLTMGRERSDQACWRALEIAQLADGVRRLPQGLDTVVGrsgvRLSGGQRQRLAIARMILAEPKVVILDEATSA 524
Cdd:PRK10636 104 RNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVS----DFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179


                 ..
gi 15596057  525 LD 526
Cdd:PRK10636 180 LD 181

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

360-526

3.75e-05

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 3.75e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  360 IEVRGLDFAYGEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGLYSAQRGSIRYGGVPLEEIG-LDCVREHVAVV 438
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhRRAVCPRIAYM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  439 LQ------HPALfndSVRANLT-MGRERSDQACWRALEIAQLADGVrrlpqGLDTVVGRSGVRLSGGQRQRLAIARMILA 511
Cdd:NF033858  82 PQglgknlYPTL---SVFENLDfFGRLFGQDAAERRRRIDELLRAT-----GLAPFADRPAGKLSGGMKQKLGLCCALIH 153

                        170
                 ....*....|....*
gi 15596057  512 EPKVVILDEATSALD 526
Cdd:NF033858 154 DPDLLILDEPTTGVD 168

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

489-583

1.95e-04

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: 44.62 E-value: 1.95e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057   489 GRSGVRLSGGQRQRLAIARMILAE---PKVVILDEATSALDAATEYALHQALGDFLE-GRTTLIVAHRLSAVKQADRVLv 564
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYII- 902

                          90       100
                  ....*....|....*....|
gi 15596057   565 fDGGhiAEDGDH-QQLIAEG 583
Cdd:TIGR00630 903 -DLG--PEGGDGgGTVVASG 919

PLN03140

ABC transporter G family member; Provisional

485-537

1.95e-04

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 1.95e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15596057   485 DTVVGRSGVR-LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQAL 537
Cdd:PLN03140  326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL 379

ABC_6TM_AarD_CydDC_like

cd18561

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...

83-253

2.11e-04

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: 43.42 E-value: 2.11e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  83 LAATLLLRGAALVFNVLQAKlfaRLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHLVTDLDTLDKFVGETLSRFL 162
Cdd:cd18561  42 IAGVIVLRAALLWLRERVAH---RAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 163 VALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALTETLEAIQEVRAGNRQGYFL 242
Cdd:cd18561 119 VALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRG 198

                       170
                ....*....|.
gi 15596057 243 GRLGHRAQEVR 253
Cdd:cd18561 199 NELAARAEDLR 209

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

495-571

2.30e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.30e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596057  495 LSGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFL-EGRTTLIVAHRL-SAVKQADRVLVFDGGHIA 571
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNGLVA 470

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

375-563

2.76e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 2.76e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 375 LEQLDLNIGAGEKVALVGASGGGKSTLvqlllglysaqrgsiryggvpLEEIGLdcvrehvaVVLQhpalfndsvRANLT 454
Cdd:cd03227  11 FVPNDVTFGEGSLTIITGPNGSGKSTI---------------------LDAIGL--------ALGG---------AQSAT 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 455 MGRERSDQACWRALEIAQLAdgVRRlpqgldtvvgrsgVRLSGGQRQRLAIA-RMILAEPK---VVILDEATSALDAATE 530
Cdd:cd03227  53 RRRSGVKAGCIVAAVSAELI--FTR-------------LQLSGGEKELSALAlILALASLKprpLYILDEIDRGLDPRDG 117

                       170       180       190
                ....*....|....*....|....*....|....
gi 15596057 531 YALHQALGDFLEGRTTLIVA-HRLSAVKQADRVL 563
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVItHLPELAELADKLI 151

ABC_6TM_PrtD_LapB_HlyB_like

cd18566

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...

64-319

2.83e-04

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: 43.34 E-value: 2.83e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  64 MDRLLPADWQVAFGYIGLMLAATLLLRGaalVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHL 143
Cdd:cd18566  29 YDRVIPNESIPTLQVLVIGVVIAILLES---LLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 144 vTDLDTLDKFVGetlSRFLVALLTLLGTA---AILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQ 220
Cdd:cd18566 106 -NSLEQIREFLT---GQALLALLDLPFVLiflGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQN 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 221 ALTETLEAIQEVRAGNRQGYFLGRLghrAQEVRDYAVASQWKSDAAGRASGLlfqfgIDVFRAAAMLTVLL--------S 292
Cdd:cd18566 182 FLIETLTGIHTIKAMAMEPQMLRRY---ERLQANAAYAGFKVAKINAVAQTL-----GQLFSQVSMVAVVAfgallvinG 253

                       250       260
                ....*....|....*....|....*..
gi 15596057 293 DLSIGQMLAVFSYLWFMIGPVEQLLGL 319
Cdd:cd18566 254 DLTVGALIACTMLSGRVLQPLQRAFGL 280

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

385-553

8.81e-04

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 8.81e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 385 GEKVALVGASGGGKSTLVQLL-------LGLYSAQ----------RGSI--RYggvpLEEIGLDCVRehVAVVLQH---- 441
Cdd:COG1245  99 GKVTGILGPNGIGKSTALKILsgelkpnLGDYDEEpswdevlkrfRGTElqDY----FKKLANGEIK--VAHKPQYvdli 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 442 PALFNDSVRANLtmgrERSDqacwralEIAQLADGVRRLpqGLDTVVGRSGVRLSGGQRQRLAIARMILAEPKVVILDEA 521
Cdd:COG1245 173 PKVFKGTVRELL----EKVD-------ERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239

                       170       180       190
                ....*....|....*....|....*....|...
gi 15596057 522 TSALDAATEYALHQALGDFLE-GRTTLIVAHRL 553
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEeGKYVLVVEHDL 272

PRK15093

peptide ABC transporter ATP-binding protein SapD;

370-581

1.33e-03

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.33e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  370 GEDKVLEQLDLNIGAGEKVALVGASGGGKSTLVQLLLGL------YSAQRgsIRYGGVPLEEIGL----DCVREHVAVVL 439
Cdd:PRK15093  18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADR--MRFDDIDLLRLSPrerrKLVGHNVSMIF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  440 QHP-ALFNDSVRanltMGRERSdQA--CW---------------RALE------IAQLADGVRRLPqgldtvvgrsgVRL 495
Cdd:PRK15093  96 QEPqSCLDPSER----VGRQLM-QNipGWtykgrwwqrfgwrkrRAIEllhrvgIKDHKDAMRSFP-----------YEL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  496 SGGQRQRLAIARMILAEPKVVILDEATSALDAATEYALHQALGDFLE--GRTTLIVAHRLSAVKQ-ADRVLVFDGGHIAE 572
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTVE 239


                 ....*....
gi 15596057  573 DGDHQQLIA 581
Cdd:PRK15093 240 TAPSKELVT 248

PLN03073

ABC transporter F family; Provisional

496-551

3.53e-03

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 3.53e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596057  496 SGGQRQRLAIARMILAEPKVVILDEATSALDaateyaLHQALgdFLEG------RTTLIVAH 551
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD------LHAVL--WLETyllkwpKTFIVVSH 399

ABC_6TM_HetC_like

cd18568

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...

64-319

5.17e-03

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: 39.08 E-value: 5.17e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  64 MDRLLPADwqvAFGYIGLMLAATLLLRGAALVFNVLQAKLFARLSKDIVYRIRLRLIERLRHIALGEYETLGGGSISAHL 143
Cdd:cd18568  29 LDRVLVHK---NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRF 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 144 VTDLDTLDKFVGETLSRFLvALLTLLGTAAILVWMHWQLALLILLFNPLVIWSTVQLGKRVKHLKKLENDSTARFTQALT 223
Cdd:cd18568 106 QENQKIRRFLTRSALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLV 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 224 ETLEAIQEVRAGNRQGYFLGRLGHRAQEVRDYAVASQWKSDAAGRASGLLFQFG-IDVFRAAAMLtVLLSDLSIGQMLAv 302
Cdd:cd18568 185 EALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGtIAVLWYGAYL-VISGQLTIGQLVA- 262

                       250
                ....*....|....*...
gi 15596057 303 FSYLWFM-IGPVEQLLGL 319
Cdd:cd18568 263 FNMLFGSvINPLLALVGL 280

ABC_6TM_ATM1_ABCB7

cd18582

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...

65-321

7.90e-03

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: 38.63 E-value: 7.90e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057  65 DRLLPADWQVAFGYIGLMLAATLLlRGAALVFNVLQAKLFARLSKDIVYRIRLRLierLRHI-ALgeyetlgggSISAHL 143
Cdd:cd18582  24 DALSAPASALLAVPLLLLLAYGLA-RILSSLFNELRDALFARVSQRAVRRLALRV---FRHLhSL---------SLRFHL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 144 -------VTDLDTLDKFVgETLSRFLV-----ALLTLLGTAAILVWM-HWQLALLILLFNPL-VIWSTVQLGKRVKHLK- 208
Cdd:cd18582  91 srktgalSRAIERGTRGI-EFLLRFLLfnilpTILELLLVCGILWYLyGWSYALITLVTVALyVAFTIKVTEWRTKFRRe 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 209 --KLENDSTARFTQALT--ETleaiqeVRAGNRQGYFLGRLGHRAQEVRDYAVASQWksdaagraSGLLFQFGIDVFRAA 284
Cdd:cd18582 170 mnEADNEANAKAVDSLLnyET------VKYFNNEEYEAERYDKALAKYEKAAVKSQT--------SLALLNIGQALIISL 235

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15596057 285 AMLTVLL--------SDLSIGQMLAVFSYLWFMIGPVeQLLGLQY 321
Cdd:cd18582 236 GLTAIMLlaaqgvvaGTLTVGDFVLVNTYLLQLYQPL-NFLGFVY 279

ABC_6TM_ABCC_D2

cd18580

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...

146-242

8.65e-03

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: 38.64 E-value: 8.65e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596057 146 DLDTLDKFVGETLSRFLVALLTLLGTAAILVWMHWQLALLIllfnPLVIWSTVQLGKR----VKHLKKLENDSTARFTQA 221
Cdd:cd18580 105 DIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL----PPLLVVYYLLQRYylrtSRQLRRLESESRSPLYSH 180

                        90       100
                ....*....|....*....|.
gi 15596057 222 LTETLEAIQEVRAGNRQGYFL 242
Cdd:cd18580 181 FSETLSGLSTIRAFGWQERFI 201

PRK01889

GTPase RsgA; Reviewed

385-417

8.95e-03

GTPase RsgA; Reviewed

Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 8.95e-03

                         10        20        30
                 ....*....|....*....|....*....|...
gi 15596057  385 GEKVALVGASGGGKSTLVQLLLGLYSAQRGSIR 417
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227

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