NCBI Conserved Domain Search

Conserved domains on [gi|515713280|ref|WP_017145880|]

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MULTISPECIES: yersiniabactin ABC transporter ATP-binding/permease protein YbtQ [Klebsiella]

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];

16-584

4.15e-159

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 467.72 E-value: 4.15e-159

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  16 WRQLISSVGSQAGMLRRSMIALLLAALMQGIAFACLYPIVDALLRG-EASPLLTWALVFSATAFAALALRWYGLgfeYRG 94
Cdd:COG1132    9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGgDLSALLLLLLLLLGLALLRALLSYLQR---YLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  95 HLA--QATHELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGL 172
Cdd:COG1132   86 ARLaqRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 173 VMLLIFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHRQSA 252
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 253 GATMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRIEQFMALPPLPV 332
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 333 AERGEMP---ERYDIRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI 409
Cdd:COG1132  326 DPPGAVPlppVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 410 RHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQR 489
Cdd:COG1132  405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 490 ISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564

                        570
                 ....*....|....*
gi 515713280 570 QGRYQALWQAQMAAR 584
Cdd:COG1132  565 GGLYARLYRLQFGEE 579

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

16-584

4.15e-159

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 467.72 E-value: 4.15e-159

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  16 WRQLISSVGSQAGMLRRSMIALLLAALMQGIAFACLYPIVDALLRG-EASPLLTWALVFSATAFAALALRWYGLgfeYRG 94
Cdd:COG1132    9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGgDLSALLLLLLLLLGLALLRALLSYLQR---YLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  95 HLA--QATHELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGL 172
Cdd:COG1132   86 ARLaqRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 173 VMLLIFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHRQSA 252
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 253 GATMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRIEQFMALPPLPV 332
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 333 AERGEMP---ERYDIRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI 409
Cdd:COG1132  326 DPPGAVPlppVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 410 RHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQR 489
Cdd:COG1132  405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 490 ISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564

                        570
                 ....*....|....*
gi 515713280 570 QGRYQALWQAQMAAR 584
Cdd:COG1132  565 GGLYARLYRLQFGEE 579

ABCC_MsbA

cd03251

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

344-577

3.78e-104

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: 314.17 E-value: 3.78e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03251    1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIV 503
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALW 577
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234

MsbA_lipidA

TIGR02203

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

15-582

2.42e-97

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: 308.57 E-value: 2.42e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   15 IWRQLISSVGSQAGMLRRSMIALLLAALMQGIAFACLYPIVDALLrGEASPLLTWALvfsaTAFAALALRWYGLGfEYRG 94
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGF-GGRDRSVLWWV----PLVVIGLAVLRGIC-SFVS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   95 HLAQA------THELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDW 168
Cdd:TIGR02203  75 TYLLSwvsnkvVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  169 RLGLVMLLIFPMLVpfyyWRRPAMRRQMQTLGEAHQRLSGD----IVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQ 244
Cdd:TIGR02203 155 QLTLIVVVMLPVLS----ILMRRVSKRLRRISKEIQNSMGQvttvAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  245 SRTHRQSAGATMLIAGVVELGLQVVVLAGVVWVVTGTLN----LAFLIAAAAMImrfsEPMAMFISYTSVVELIASALQR 320
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTagdfTAFITAMIALI----RPLKSLTNVNAPMQRGLAAAES 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  321 IEQFMALPPLPVAERGEMPE-RYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQ 399
Cdd:TIGR02203 307 LFTLLDSPPEKDTGTRAIERaRGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  400 GEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARP-QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEM 478
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  479 GGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVV 558
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546

                         570       580
                  ....*....|....*....|....
gi 515713280  559 EQGTHAQLLSRQGRYQALWQAQMA 582
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQLHNMQFR 570

PRK11176

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

343-580

4.11e-83

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 271.51 E-value: 4.11e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARP-QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAP 501
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 502 IVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQ 580
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579

ABC_tran

pfam00005

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

361-510

3.41e-36

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: 132.39 E-value: 3.41e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDD-TLLANL 439
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280  440 LIARPQATQQEVEEAARAAqclEFISRLPQGWL--TPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAE---EALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

357-546

3.19e-14

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.50 E-value: 3.19e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdirhltaeqlNSLISVVFQDVWLfDDTLL 436
Cdd:NF040873   4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEV-PDSLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANL-------------LIARPQAT-QQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKDAPI 502
Cdd:NF040873  72 LTVrdlvamgrwarrgLWRRLTRDdRAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEADL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLSTIAGA 546
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRA 185

GguA

NF040905

sugar ABC transporter ATP-binding protein;

360-559

1.61e-08

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 1.61e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLM------RYadpqQGEISIGGV-----DIRhlTAEQLNslISVVFQDV 428
Cdd:NF040905  16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSY----EGEILFDGEvcrfkDIR--DSEALG--IVIIHQEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WLFDDTLLA-NLLIARPQATQQEV---EEAARAAQCLEFI--SRLPQgwlTPMGEMGGqlsgGERQRISIARALLKDAPI 502
Cdd:NF040905  88 ALIPYLSIAeNIFLGNERAKRGVIdwnETNRRARELLAKVglDESPD---TLVTDIGV----GKQQLVEIAKALSKDVKL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 503 VILDEPTAAL-DIDSElavqKAIDHLVHNR----TVIIIAHRLSTIAG-AGNILVMEEGEVVE 559
Cdd:NF040905 161 LILDEPTAALnEEDSA----ALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219

AAA

smart00382

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

375-546

1.96e-08

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: 53.53 E-value: 1.96e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   375 ALVGASGAGKTTVSKLLMRYADPQQGE-ISIGGVDIRHLTAEQLnslisvvfqdvwlfddtllanlliarpqatqqevee 453
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------------ 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   454 aaraaqclefisrlpqgWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV----- 528
Cdd:smart00382  50 -----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllk 112

                          170       180
                   ....*....|....*....|
gi 515713280   529 --HNRTVIIIAHRLSTIAGA 546
Cdd:smart00382 113 seKNLTVILTTNDEKDLGPA 132

40850658_otr

NF000106

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

455-571

7.64e-04

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 7.64e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 455 ARAAQCLEFISRLPQGwltpmGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVI 534
Cdd:NF000106 123 ARADELLERFSLTEAA-----GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 515713280 535 IIAHRLSTIAG--AGNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:NF000106 198 LLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

360-571

9.31e-04

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 9.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI---RHLTAEQ-------------LNSLISV 423
Cdd:NF033858  16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadaRHRRAVCpriaympqglgknLYPTLSV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 vFQDVWLFddtllANLLIARPQATQQEVEEAARAAQCLEFISRlpqgwltPMGemggQLSGGERQRISIARALLKDAPIV 503
Cdd:NF033858  96 -FENLDFF-----GRLFGQDAAERRRRIDELLRATGLAPFADR-------PAG----KLSGGMKQKLGLCCALIHDPDLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 504 ILDEPTAALDIDS-----ELavqkaIDHLVHNR---TVIII------AHRLSTIAgagnilVMEEGEVVEQGTHAQLLSR 569
Cdd:NF033858 159 ILDEPTTGVDPLSrrqfwEL-----IDRIRAERpgmSVLVAtaymeeAERFDWLV------AMDAGRVLATGTPAELLAR 227


                 ..
gi 515713280 570 QG 571
Cdd:NF033858 228 TG 229

GguA

NF040905

sugar ABC transporter ATP-binding protein;

480-558

2.72e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.72e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELPELLGmCDRIYVMNEGRI 482


                 .
gi 515713280 558 V 558
Cdd:NF040905 483 T 483

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

16-584

4.15e-159

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 467.72 E-value: 4.15e-159

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  16 WRQLISSVGSQAGMLRRSMIALLLAALMQGIAFACLYPIVDALLRG-EASPLLTWALVFSATAFAALALRWYGLgfeYRG 94
Cdd:COG1132    9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGgDLSALLLLLLLLLGLALLRALLSYLQR---YLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  95 HLA--QATHELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGL 172
Cdd:COG1132   86 ARLaqRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 173 VMLLIFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHRQSA 252
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 253 GATMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRIEQFMALPPLPV 332
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 333 AERGEMP---ERYDIRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI 409
Cdd:COG1132  326 DPPGAVPlppVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 410 RHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQR 489
Cdd:COG1132  405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 490 ISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564

                        570
                 ....*....|....*
gi 515713280 570 QGRYQALWQAQMAAR 584
Cdd:COG1132  565 GGLYARLYRLQFGEE 579

SunT

COG2274

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

31-581

3.62e-116

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: 361.46 E-value: 3.62e-116

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  31 RRSMIALLLAALMQGIaFACLYP-----IVDALLRGEASPLLTW-ALVFSATAFAALALRWYglgfeyRGHL-----AQA 99
Cdd:COG2274  155 RRLLLQVLLASLLINL-LALATPlftqvVIDRVLPNQDLSTLWVlAIGLLLALLFEGLLRLL------RSYLllrlgQRI 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 100 THELRLRLGEQLRRVPLERLQRGRAGEtnalLLGSVDENLNYVIAIANILLLTIVTPLTA--SLATLW-IDWRLGLVMLL 176
Cdd:COG2274  228 DLRLSSRFFRHLLRLPLSFFESRSVGD----LASRFRDVESIREFLTGSLLTALLDLLFVliFLIVLFfYSPPLALVVLL 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 177 IFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDG---EKSRALLAHF-NALESLQSRTHRQSA 252
Cdd:COG2274  304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESrfrRRWENLLAKYlNARFKLRRLSNLLST 383

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 253 GATML--IAGVVELGLqvvvlaGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRIEQFMALPPL 330
Cdd:COG2274  384 LSGLLqqLATVALLWL------GAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE 457

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 331 PVAERGEMP---ERYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV 407
Cdd:COG2274  458 REEGRSKLSlprLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 408 DIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGER 487
Cdd:COG2274  538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 488 QRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLL 567
Cdd:COG2274  618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697

                        570
                 ....*....|....
gi 515713280 568 SRQGRYQALWQAQM 581
Cdd:COG2274  698 ARKGLYAELVQQQL 711

CydC

COG4987

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

102-578

2.28e-108

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: 336.74 E-value: 2.28e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 102 ELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDenlnyviAIANILLLTIVTPLTASLATL-------WIDWRLGLVM 174
Cdd:COG4987   89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVD-------ALDNLYLRVLLPLLVALLVILaavaflaFFSPALALVL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 175 LLIFPM---LVPFYYWRrpAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHRQS 251
Cdd:COG4987  162 ALGLLLaglLLPLLAAR--LGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLS 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 252 AGATMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISytSVVEL--IASALQRIEQFMALPP 329
Cdd:COG4987  240 ALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPA--AAQHLgrVRAAARRLNELLDAPP 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 330 lPVAERGE---MPERYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG 406
Cdd:COG4987  318 -AVTEPAEpapAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 407 VDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGE 486
Cdd:COG4987  397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 487 RQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQL 566
Cdd:COG4987  477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556

                        490
                 ....*....|..
gi 515713280 567 LSRQGRYQALWQ 578
Cdd:COG4987  557 LAQNGRYRQLYQ 568

CydD

COG4988

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

17-571

2.87e-108

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: 336.34 E-value: 2.87e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  17 RQLISSVGSQAGMLRRSMIALLLAALMqGIAFA-CLYPIVDALLRGEASP--LLTWALVFsataFAALALRwYGLGF--E 91
Cdd:COG4988    6 KRLKRLARGARRWLALAVLLGLLSGLL-IIAQAwLLASLLAGLIIGGAPLsaLLPLLGLL----LAVLLLR-ALLAWlrE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  92 YRGHLA--QATHELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWR 169
Cdd:COG4988   80 RAAFRAaaRVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 170 LGLVMLLIFPmLVPFYYW-----RRPAMRRQMQTLgeahQRLSGDIVEFAQGMMVLRTCGSDGEKSRALlahFNALESLQ 244
Cdd:COG4988  160 SGLILLVTAP-LIPLFMIlvgkgAAKASRRQWRAL----ARLSGHFLDRLRGLTTLKLFGRAKAEAERI---AEASEDFR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 245 SRTHRQ--------------SAGATMLIAgvVELGLQVVvlagvvwvvTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSV 310
Cdd:COG4988  232 KRTMKVlrvaflssavleffASLSIALVA--VYIGFRLL---------GGSLTLFAALFVLLLAPEFFLPLRDLGSFYHA 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 311 VELIASALQRIEQFMALPPlPVAERGE----MPERYDIRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTT 386
Cdd:COG4988  301 RANGIAAAEKIFALLDAPE-PAAPAGTaplpAAGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKST 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 387 VSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISR 466
Cdd:COG4988  379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 467 LPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGA 546
Cdd:COG4988  459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538

                        570       580
                 ....*....|....*....|....*
gi 515713280 547 GNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:COG4988  539 DRILVLDDGRIVEQGTHEELLAKNG 563

ABCC_MsbA

cd03251

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

344-577

3.78e-104

Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 314.17 E-value: 3.78e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03251    1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIV 503
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALW 577
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234

ATM1

COG5265

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

328-584

1.69e-98

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: 312.52 E-value: 1.69e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 328 PPLPVAErGEmperydIRFDTICYRYDdSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV 407
Cdd:COG5265  349 PPLVVGG-GE------VRFENVSFGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 408 DIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGER 487
Cdd:COG5265  421 DIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEK 500

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 488 QRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLL 567
Cdd:COG5265  501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580

                        250
                 ....*....|....*..
gi 515713280 568 SRQGRYQALWQAQMAAR 584
Cdd:COG5265  581 AQGGLYAQMWARQQEEE 597

MsbA_lipidA

TIGR02203

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

15-582

2.42e-97

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 308.57 E-value: 2.42e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   15 IWRQLISSVGSQAGMLRRSMIALLLAALMQGIAFACLYPIVDALLrGEASPLLTWALvfsaTAFAALALRWYGLGfEYRG 94
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGF-GGRDRSVLWWV----PLVVIGLAVLRGIC-SFVS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   95 HLAQA------THELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDW 168
Cdd:TIGR02203  75 TYLLSwvsnkvVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  169 RLGLVMLLIFPMLVpfyyWRRPAMRRQMQTLGEAHQRLSGD----IVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQ 244
Cdd:TIGR02203 155 QLTLIVVVMLPVLS----ILMRRVSKRLRRISKEIQNSMGQvttvAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  245 SRTHRQSAGATMLIAGVVELGLQVVVLAGVVWVVTGTLN----LAFLIAAAAMImrfsEPMAMFISYTSVVELIASALQR 320
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTagdfTAFITAMIALI----RPLKSLTNVNAPMQRGLAAAES 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  321 IEQFMALPPLPVAERGEMPE-RYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQ 399
Cdd:TIGR02203 307 LFTLLDSPPEKDTGTRAIERaRGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  400 GEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARP-QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEM 478
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  479 GGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVV 558
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546

                         570       580
                  ....*....|....*....|....
gi 515713280  559 EQGTHAQLLSRQGRYQALWQAQMA 582
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQLHNMQFR 570

ABCC_ATM1_transporter

cd03253

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

344-580

4.47e-97

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: 296.06 E-value: 4.47e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03253    1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIV 503
Cdd:cd03253   80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQ 580
Cdd:cd03253  160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236

ABC_MTABC3_MDL1_MDL2

cd03249

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

344-580

2.95e-92

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: 283.66 E-value: 2.95e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD-PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:cd03249    1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQ 580
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238

ABCC_Glucan_exporter_like

cd03254

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

343-571

1.03e-88

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: 274.10 E-value: 1.03e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDdSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:cd03254    2 EIEFENVNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:cd03254   81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:cd03254  161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229

PRK11176

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

343-580

4.11e-83

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 271.51 E-value: 4.11e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARP-QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAP 501
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 502 IVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQ 580
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

146-580

2.77e-82

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 269.52 E-value: 2.77e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 146 ANILLLTIVTPLTaslatLWIDWRLGLVML---LIFPMLVPFyywrrpAMRR--QMQTLGEAHQR-LSGDIVEFAQGMMV 219
Cdd:PRK13657 139 ATLVALVVLLPLA-----LFMNWRLSLVLVvlgIVYTLITTL------VMRKtkDGQAAVEEHYHdLFAHVSDAIGNVSV 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 220 LRTCGSDGEKSRALLAHFNALESLQ----------SRTHRQSAGATMLIAGVVELGLQVVvlagvvwvvtGTLN----LA 285
Cdd:PRK13657 208 VQSYNRIEAETQALRDIADNLLAAQmpvlswwalaSVLNRAASTITMLAILVLGAALVQK----------GQLRvgevVA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 286 FLIAAAAMIMRFsEPMAMFISytsvveLIASALQRIEQFMAL--PPLPVAERGEMPE----RYDIRFDTICYRYDDSGdP 359
Cdd:PRK13657 278 FVGFATLLIGRL-DQVVAFIN------QVFMAAPKLEEFFEVedAVPDVRDPPGAIDlgrvKGAVEFDDVSFSYDNSR-Q 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANL 439
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNI 429

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELA 519
Cdd:PRK13657 430 RVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 520 VQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQ 580
Cdd:PRK13657 510 VKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570

CydD

TIGR02857

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

30-552

7.24e-76

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: 250.67 E-value: 7.24e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   30 LRRSMI-ALLLAALMQGIAFACLYPIVDALLRGEA-SPLLTWALVFSATAFAALALRWYGLGFEYRGHLAqATHELRLRL 107
Cdd:TIGR02857   5 LALLALlGVLGALLIIAQAWLLARVVDGLISAGEPlAELLPALGALALVLLLRALLGWLQERAAARAAAA-VKSQLRERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  108 GEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPmLVPFYYW 187
Cdd:TIGR02857  84 LEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAP-LIPIFMI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  188 -----RRPAMRRQMQTLgeahQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAhfnALESLQSRTHR-------QSAG-- 253
Cdd:TIGR02857 163 ligwaAQAAARKQWAAL----SRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRR---SSEEYRERTMRvlriaflSSAVle 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  254 --ATMLIAGV-VELGLQVVVlagvvwvvtGTLNLAFLIAAAAMIMRFSEPMAMF-ISYTSVVELIAsALQRIEQFMALPP 329
Cdd:TIGR02857 236 lfATLSVALVaVYIGFRLLA---------GDLDLATGLFVLLLAPEFYLPLRQLgAQYHARADGVA-AAEALFAVLDAAP 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  330 LPVAERGEMPERYD--IRFDTICYRYDDSgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV 407
Cdd:TIGR02857 306 RPLAGKAPVTAAPAssLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  408 DIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGER 487
Cdd:TIGR02857 385 PLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280  488 QRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVM 552
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529

MsbA_rel

TIGR02204

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

330-580

2.32e-75

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.

Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 250.77 E-value: 2.32e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  330 LPVAERGEmperydIRFDTICYRYDDSGD-PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVD 408
Cdd:TIGR02204 330 LPVPLRGE------IEFEQVNFAYPARPDqPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVD 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  409 IRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQ 488
Cdd:TIGR02204 404 LRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  489 RISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563

                         250
                  ....*....|..
gi 515713280  569 RQGRYQALWQAQ 580
Cdd:TIGR02204 564 KGGLYARLARLQ 575

ABCC_MRP_Like

cd03228

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

344-556

3.71e-73

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: 231.50 E-value: 3.71e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03228    1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLliarpqatqqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDAPIV 503
Cdd:cd03228   81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGE 556
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

PRK11160

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

149-578

9.62e-69

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 233.18 E-value: 9.62e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 149 LLLTIVTPLTASLATL--------WIDWRLG-------LVMLLIFPMLvpFYYWRRPAMRRQMQTLGEAHQRLsgdiVEF 213
Cdd:PRK11160 133 LYLRLISPLVAALVVIlvltiglsFFDLTLAltlggilLLLLLLLPLL--FYRLGKKPGQDLTHLRAQYRVQL----TEW 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 214 AQGMMVLRTCGSDgEKSRALLAhfNALESLQSRTHRQ------SAGATMLIAGV-VELGLQVVVLAGVVWVVTGTLNLAF 286
Cdd:PRK11160 207 LQGQAELTLFGAE-DRYRQQLE--QTEQQWLAAQRRQanltglSQALMILANGLtVVLMLWLAAGGVGGNAQPGALIALF 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 287 LIAAAA---MIMrfsePMAMFISYTSVVelIASAlQRIEQFMALPPLPV--AERGEMPERYDIRFDTICYRYDDSGDPAL 361
Cdd:PRK11160 284 VFAALAafeALM----PVAGAFQHLGQV--IASA-RRINEITEQKPEVTfpTTSTAAADQVSLTLNNVSFTYPDQPQPVL 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 362 NNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLI 441
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL 436

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 442 ARPQATQQEVEEAARAAQcLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQ 521
Cdd:PRK11160 437 AAPNASDEALIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL 515

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 522 KAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQ 578
Cdd:PRK11160 516 ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572

ABCC_Hemolysin

cd03252

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

344-580

2.62e-67

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: 218.89 E-value: 2.62e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03252    1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIV 503
Cdd:cd03252   81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQ 580
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237

chvA

TIGR01192

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...

163-579

4.74e-62

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]

Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 215.52 E-value: 4.74e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  163 TLWIDWRLGLVMLLIFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALES 242
Cdd:TIGR01192 151 AFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLS 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  243 LQSRTHRQSAGATMLIAGVVELGLQVVVLAGVVWVVTGTLN----LAFLIAAAAMIMRFSEpMAMFISytsvveLIASAL 318
Cdd:TIGR01192 231 AQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSvgevIAFIGFANLLIGRLDQ-MSGFIT------QIFEAR 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  319 QRIEQFMALPP--LPVAERGEMPE----RYDIRFDTICYRYDDSGDpALNNLSLTFPAASMSALVGASGAGKTTVSKLLM 392
Cdd:TIGR01192 304 AKLEDFFDLEDsvFQREEPADAPElpnvKGAVEFRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQ 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  393 RYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWL 472
Cdd:TIGR01192 383 RVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYD 462

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  473 TPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVM 552
Cdd:TIGR01192 463 TLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFL 542

                         410       420
                  ....*....|....*....|....*..
gi 515713280  553 EEGEVVEQGTHAQLLSRQGRYQALWQA 579
Cdd:TIGR01192 543 DQGRLIEKGSFQELIQKDGRFYKLLRR 569

ABCC_MRP_domain2

cd03244

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

343-562

5.90e-61

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 201.57 E-value: 5.90e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:cd03244    2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLliaRP--QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDA 500
Cdd:cd03244   82 IIPQDPVLFSGTIRSNL---DPfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 501 PIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGT 562
Cdd:cd03244  159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220

bacteriocin_ABC

TIGR01193

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

144-576

6.12e-60

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: 212.29 E-value: 6.12e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  144 AIANILL-----LTIVtpLTASLATLWIDWRLGLVMLLIFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMM 218
Cdd:TIGR01193 268 ALASTILslfldMWIL--VIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIE 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  219 VLRTCGSDGEKSRALLAHF-NALESlqSRTHRQSAGATMLIAGVVELGLQVVVL-AGVVWVVTGTLNLAFLIAAAAMIMR 296
Cdd:TIGR01193 346 TIKSLTSEAERYSKIDSEFgDYLNK--SFKYQKADQGQQAIKAVTKLILNVVILwTGAYLVMRGKLTLGQLITFNALLSY 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  297 FSEPMAMFISYTSVVELIASALQRIEQFMaLPPLPVAERGEMPER----YDIRFDTICYRYDdSGDPALNNLSLTFPAAS 372
Cdd:TIGR01193 424 FLTPLENIINLQPKLQAARVANNRLNEVY-LVDSEFINKKKRTELnnlnGDIVINDVSYSYG-YGSNILSDISLTIKMNS 501

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  373 MSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLI-ARPQATQQEV 451
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEI 581

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  452 EEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSElavQKAIDHLV--H 529
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLnlQ 658

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 515713280  530 NRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQAL 576
Cdd:TIGR01193 659 DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705

PRK10789

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

34-600

8.86e-59

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 206.10 E-value: 8.86e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  34 MIALLLAALMQGIAFACLYPIVDALLRGEASP--LLTWALVFSATAFAALALR--WYGLGFEYRGHLAQathELRLRLGE 109
Cdd:PRK10789   1 VALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTgqILMWIGTMVLIAVVVYLLRyvWRVLLFGASYQLAV---ELREDFYR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 110 QLRRVPLERLQRGRAGETNALLLGSVDEnlnyVIAIANILLLTIVTPLTASLATL-----WIDWRLGLVMLLifPMlvpf 184
Cdd:PRK10789  78 QLSRQHPEFYLRHRTGDLMARATNDVDR----VVFAAGEGVLTLVDSLVMGCAVLivmstQISWQLTLLALL--PM---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 185 yywrrPAMRRQMQTLGEA-HQRLsgdivEFAQGMM-VLRTCGSDGEKSRALLAHFnALESLQSRTHRQSAGAT----MLI 258
Cdd:PRK10789 148 -----PVMAIMIKRYGDQlHERF-----KLAQAAFsSLNDRTQESLTSIRMIKAF-GLEDRQSALFAADAEDTgkknMRV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 259 AGV---------VELGLQVVVLAG--VVWVVTGTLNL----AFLIAAAAMIMrfsePMAMFISYTSVVELIASALQRIEQ 323
Cdd:PRK10789 217 ARIdarfdptiyIAIGMANLLAIGggSWMVVNGSLTLgqltSFVMYLGLMIW----PMLALAWMFNIVERGSAAYSRIRA 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 324 FMALPPlpVAERGEMP---ERYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQG 400
Cdd:PRK10789 293 MLAEAP--VVKDGSEPvpeGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 401 EISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGG 480
Cdd:PRK10789 371 DIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 450

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 481 QLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQ 560
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQR 530

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|
gi 515713280 561 GTHAQLLSRQGRYQALWQAQMAARVWRDAEvDASEERLHE 600
Cdd:PRK10789 531 GNHDQLAQQSGWYRDMYRYQQLEAALDDAP-EIREEAVDA 569

PRK10790

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

161-582

5.26e-57

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 201.87 E-value: 5.26e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 161 LATLWIDWRLGLVMLLIFPM--LVPFYYWR--RPAMRRQMQTLGEahqrLSGDIVEFAQGMMVL---RTCGSDGEK-SRA 232
Cdd:PRK10790 158 VAMFSLDWRMALVAIMIFPAvlVVMVIYQRysTPIVRRVRAYLAD----INDGFNEVINGMSVIqqfRQQARFGERmGEA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 233 LLAHFNA------LESLQSRTHRQSAGATMLIAGVVELGLQVvvlagvvwvvTGTLNLAFLIAAAAMIMRFSEPMAMFIS 306
Cdd:PRK10790 234 SRSHYMArmqtlrLDGFLLRPLLSLFSALILCGLLMLFGFSA----------SGTIEVGVLYAFISYLGRLNEPLIELTT 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 307 YTSVVELIASALQRIEQFMALPPLPVAERGEMPERYDIRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTT 386
Cdd:PRK10790 304 QQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGRIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKST 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 387 VSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPqATQQEVEEAARAAQCLEFISR 466
Cdd:PRK10790 383 LASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARS 461

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 467 LPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGA 546
Cdd:PRK10790 462 LPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEA 541

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 515713280 547 GNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQMA 582
Cdd:PRK10790 542 DTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577

ABCC_bacteriocin_exporters

cd03245

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

343-561

4.72e-56

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: 188.57 E-value: 4.72e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:cd03245    2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:cd03245   82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQG 561
Cdd:cd03245  162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220

CydC

TIGR02868

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

79-540

1.13e-55

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: 196.81 E-value: 1.13e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   79 AALALRWYGLG---FEYRGHLAqaTHELRLRLGEQLRRVPLERLQRGRAGETNAL----LLGSVDENlnyVIAIANILLL 151
Cdd:TIGR02868  55 AAVAVRAFGIGravFRYLERLV--GHDAALRSLGALRVRVYERLARQALAGRRRLrrgdLLGRLGAD---VDALQDLYVR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  152 TIVTPLTASL-------ATLWIDWRLGLVM---LLIFPMLVPFYYWRrpAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLR 221
Cdd:TIGR02868 130 VIVPAGVALVvgaaavaAIAVLSVPAALILaagLLLAGFVAPLVSLR--AARAAEQALARLRGELAAQLTDALDGAAELV 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  222 TCGSDGE---KSRALLAHFNALESLQSRTHRQSAGATMLIAGVVELGLqvvVLAGVVWVVTGTLNLAFLIAAAAMIMRFS 298
Cdd:TIGR02868 208 ASGALPAalaQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGA---LWAGGPAVADGRLAPVTLAVLVLLPLAAF 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  299 EPMAMFISYTSVVELIASALQRIEQFMAlPPLPVAE------RGEMPERYDIRFDTICYRYDDSgDPALNNLSLTFPAAS 372
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVLD-AAGPVAEgsapaaGAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGE 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  373 MSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVE 452
Cdd:TIGR02868 363 RVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELW 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  453 EAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRT 532
Cdd:TIGR02868 443 AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRT 522


                  ....*...
gi 515713280  533 VIIIAHRL 540
Cdd:TIGR02868 523 VVLITHHL 530

NHLM_micro_ABC1

TIGR03796

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

12-576

1.83e-54

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: 197.09 E-value: 1.83e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   12 WRVIWRQLISSvgsqagmlRRSMIALLLAALMQGI------AFACLYpIVDALLRGEASPLLTWALVFSATAFAALALRW 85
Cdd:TIGR03796 142 LRALWRRLRGS--------RGALLYLLLAGLLLVLpglvipAFSQIF-VDEILVQGRQDWLRPLLLGMGLTALLQGVLTW 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   86 YGLGFEYRGHLAQAThELRLRLGEQLRRVPLERLQRGRAGEtnalLLGSVDENLNYVIAIANIL---LLTIVTPLTASLA 162
Cdd:TIGR03796 213 LQLYYLRRLEIKLAV-GMSARFLWHILRLPVRFFAQRHAGD----IASRVQLNDQVAEFLSGQLattALDAVMLVFYALL 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  163 TLWIDWRLGLVMLLIFPMLVPFYYW----RRPAMRRQMQTLGeahqRLSGDIVEFAQGMMVLRTCGSD--------GEKS 230
Cdd:TIGR03796 288 MLLYDPVLTLIGIAFAAINVLALQLvsrrRVDANRRLQQDAG----KLTGVAISGLQSIETLKASGLEsdffsrwaGYQA 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  231 RALlahfNALESLQSRTHRQSAGATML--IAGVVELGLQVVVLAGvvwvvtGTLNLAFLIAAAAMIMRFSEPMAMFISYT 308
Cdd:TIGR03796 364 KLL----NAQQELGVLTQILGVLPTLLtsLNSALILVVGGLRVME------GQLTIGMLVAFQSLMSSFLEPVNNLVGFG 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  309 SVVELIASALQRIEQFMALPPLPVAERGE----MPERYD-----IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGA 379
Cdd:TIGR03796 434 GTLQELEGDLNRLDDVLRNPVDPLLEEPEgsaaTSEPPRrlsgyVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGG 513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  380 SGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQ 459
Cdd:TIGR03796 514 SGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAA 593

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  460 CLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSElavqKAIDHLVHNR--TVIIIA 537
Cdd:TIGR03796 594 IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVA 669

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 515713280  538 HRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQAL 576
Cdd:TIGR03796 670 HRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708

ArpD

COG4618

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

316-569

1.88e-53

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: 191.50 E-value: 1.88e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 316 SALQRIEQFMALPPLPvAERGEMPE-RYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRY 394
Cdd:COG4618  303 QAYRRLNELLAAVPAE-PERMPLPRpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 395 ADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANllIAR-PQATQQEVEEAARAAQCLEFISRLPQGWLT 473
Cdd:COG4618  382 WPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAEN--IARfGDADPEKVVAAAKLAGVHEMILRLPDGYDT 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 474 PMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAHRLSTIAGAGNILVM 552
Cdd:COG4618  460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVL 539

                        250
                 ....*....|....*..
gi 515713280 553 EEGEVVEQGTHAQLLSR 569
Cdd:COG4618  540 RDGRVQAFGPRDEVLAR 556

ABCC_TAP

cd03248

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

344-557

3.95e-53

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: 181.13 E-value: 3.95e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD-PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:cd03248   12 VKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:cd03248   92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEV 557
Cdd:cd03248  172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

PRK11174

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

357-584

1.22e-52

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 189.67 E-value: 1.22e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAdPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLL 436
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDS 516
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 517 ELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQMAAR 584
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588

3a01208

TIGR00958

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

54-576

1.95e-49

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 183.00 E-value: 1.95e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   54 IVDALLRGEASPLLTWAL----VFSATAFAALALRwyGLGFEYRghLAQATHELRLRLGEQLRRVPLERLQRGRAGETNA 129
Cdd:TIGR00958 187 VIDTLGGDKGPPALASAIffmcLLSIASSVSAGLR--GGSFNYT--MARINLRIREDLFRSLLRQDLGFFDENKTGELTS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  130 LLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPMLV----PFYYWRRPAMRRQMQTLGEahqr 205
Cdd:TIGR00958 263 RLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFlaekVFGKRYQLLSEELQEAVAK---- 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  206 lSGDIVEFAQGMMvlRTCGS----DGEKSRallahFN-ALESLQSRTHR-----------QSAGATMLIAGVVELGLQVV 269
Cdd:TIGR00958 339 -ANQVAEEALSGM--RTVRSfaaeEGEASR-----FKeALEETLQLNKRkalayagylwtTSVLGMLIQVLVLYYGGQLV 410

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  270 VlagvvwvvTGTLNLAFLIAAAAMIMRFSEPMAMFIS-YTSVVELIASAlQRIEQFMALPPLPVAERGEMPERYD--IRF 346
Cdd:TIGR00958 411 L--------TGKVSSGNLVSFLLYQEQLGEAVRVLSYvYSGMMQAVGAS-EKVFEYLDRKPNIPLTGTLAPLNLEglIEF 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  347 DTICYRYDDSGD-PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVF 425
Cdd:TIGR00958 482 QDVSFSYPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVG 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  426 QDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVIL 505
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLIL 641

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280  506 DEPTAALDIDSELAVQKaiDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQAL 576
Cdd:TIGR00958 642 DEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710

ABCC_cytochrome_bd

cd03247

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

344-561

9.27e-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: 159.40 E-value: 9.27e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIrHLTAEQLNSLISV 423
Cdd:cd03247    1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLliarpqatqqeveeaaraaqclefisrlpqgwltpmgemGGQLSGGERQRISIARALLKDAPIV 503
Cdd:cd03247   80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQG 561
Cdd:cd03247  121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

type_I_sec_PrtD

TIGR01842

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

317-568

1.55e-43

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: 163.67 E-value: 1.55e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  317 ALQRIEQFMALPPLPvAERGEMPE-RYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYA 395
Cdd:TIGR01842 290 AYKRLNELLANYPSR-DPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIW 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  396 DPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANllIAR--PQATQQEVEEAARAAQCLEFISRLPQGWLT 473
Cdd:TIGR01842 369 PPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAEN--IARfgENADPEKIIEAAKLAGVHELILRLPDGYDT 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  474 PMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAHRLSTIAGAGNILVM 552
Cdd:TIGR01842 447 VIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVL 526

                         250
                  ....*....|....*.
gi 515713280  553 EEGEVVEQGTHAQLLS 568
Cdd:TIGR01842 527 QDGRIARFGERDEVLA 542

ABCC_NFT1

cd03369

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

339-562

1.34e-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: 152.18 E-value: 1.34e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 339 PERYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLN 418
Cdd:cd03369    2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 419 SLISVVFQDVWLFDDTLLANLLIARPQaTQQEVEEAARAAqclefisrlpqgwltpmgEMGGQLSGGERQRISIARALLK 498
Cdd:cd03369   82 SSLTIIPQDPTLFSGTIRSNLDPFDEY-SDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALLK 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 499 DAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGT 562
Cdd:cd03369  143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206

EcfA2

COG1122

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

344-570

2.68e-42

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: 152.10 E-value: 2.68e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:COG1122    1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVW--LFDDTL-------LANLLIARPQAtQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:COG1122   80 VFQNPDdqLFAPTVeedvafgPENLGLPREEI-RERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225

ABCC_Protease_Secretion

cd03246

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

344-557

3.87e-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: 146.98 E-value: 3.87e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03246    1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLLiarpqatqqeveeaaraaqclefisrlpqgwltpmgemggqlSGGERQRISIARALLKDAPIV 503
Cdd:cd03246   81 LPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAHRLSTIAGAGNILVMEEGEV 557
Cdd:cd03246  119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173

ABC_cobalt_CbiO_domain1

cd03225

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

345-556

4.01e-40

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: 145.30 E-value: 4.01e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 345 RFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVV 424
Cdd:cd03225    1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 425 FQ--DVWLFDDTL-------LANLLIARPQAtQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARA 495
Cdd:cd03225   81 FQnpDDQFFGPTVeeevafgLENLGLPEEEI-EERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 496 LLKDAPIVILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLSTIAGAGN-ILVMEEGE 556
Cdd:cd03225  149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLELADrVIVLEDGK 211

ABC_NikE_OppD_transporters

cd03257

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

351-561

1.03e-39

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: 144.96 E-value: 1.03e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 351 YRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQD 427
Cdd:cd03257   11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRrkeIQMVFQD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 -------VWLFDDTLLANLLIARPQATQQEVEEAARAAQCL-----EFISRLPQgwltpmgemggQLSGGERQRISIARA 495
Cdd:cd03257   91 pmsslnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQRQRVAIARA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 496 LLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03257  160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228

FtsE

COG2884

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

344-565

1.60e-38

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.34 E-value: 1.60e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:COG2884    2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANLLIA------RPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIA 493
Cdd:COG2884   81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 494 RALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIA-HRLSTIAGAGN-ILVMEEGEVVEQGTHAQ 565
Cdd:COG2884  150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223

GsiA

COG1123

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

315-579

5.65e-38

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

Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.36 E-value: 5.65e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 315 ASALQRIEQFMALPPLPVAERGEMPERYD----IRFDTICYRYDDSGD---PALNNLSLTFPAASMSALVGASGAGKTTV 387
Cdd:COG1123  228 EEILAAPQALAAVPRLGAARGRAAPAAAAaeplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 388 SKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQD----------VWlfdDTL---LANLLIARPQATQQEV 451
Cdd:COG1123  308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELrrrVQMVFQDpysslnprmtVG---DIIaepLRLHGLLSRAERRERV 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 452 EEAARAAQ-CLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-- 528
Cdd:COG1123  385 AELLERVGlPPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQre 453

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515713280 529 HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSR-QGRY-QALWQA 579
Cdd:COG1123  454 LGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANpQHPYtRALLAA 507

GsiA

COG1123

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

344-594

3.75e-37

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: 144.66 E-value: 3.75e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ---QGEISIGGVDIRHLTAEQLNSL 420
Cdd:COG1123    5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDDTL---------LANLLIARPQAtQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRIS 491
Cdd:COG1123   85 IGMVFQDPMTQLNPVtvgdqiaeaLENLGLSRAEA-RARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 492 IARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:COG1123  153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232

                        250       260
                 ....*....|....*....|....*.
gi 515713280 569 RQGRYQALWQAQMAARVWRDAEVDAS 594
Cdd:COG1123  233 APQALAAVPRLGAARGRAAPAAAAAE 258

DppF

COG1124

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

351-569

2.12e-36

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: 136.47 E-value: 2.12e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 351 YRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQD--- 427
Cdd:COG1124   11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpya 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 ----VWLFDDTLLANLLIARPQATQQEVEEAARAAQ-CLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPI 502
Cdd:COG1124   91 slhpRHTVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIARALILEPEL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 503 VILDEPTAALDidseLAVQKAIDHLV------HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG1124  160 LLLDEPTSALD----VSVQAEILNLLkdlreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229

CcmA

COG1131

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

344-569

2.25e-36

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.96 E-value: 2.25e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLtAEQLNSLISV 423
Cdd:COG1131    1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANL-LIAR-----PQATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:COG1131   78 VPQEPALYPDlTVRENLrFFARlyglpRKEARERIDELLELFGLTDAADRKV-----------GTLSGGMKQRLGLALAL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG1131  147 LHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221

ABC_tran

pfam00005

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

361-510

3.41e-36

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.39 E-value: 3.41e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDD-TLLANL 439
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280  440 LIARPQATQQEVEEAARAAqclEFISRLPQGWL--TPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAE---EALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

NatA

COG4555

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

359-572

8.25e-36

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: 134.60 E-value: 8.25e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEqLNSLISVVFQDVWLFDD-TLLA 437
Cdd:COG4555   15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVRE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLliaRPQATQQEVEEAARAAQCLEFISRLpqgwltpmgEMG-------GQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:COG4555   94 NI---RYFAELYGLFDEELKKRIEELIELL---------GLEefldrrvGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 511 ALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSRQGR 572
Cdd:COG4555  162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225

ABC_OpuCA_Osmoprotection

cd03295

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

344-570

9.29e-36

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: 134.35 E-value: 9.29e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:cd03295    1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANL-----LIARPQATQQEveeaaRAAQCLEFISRLPQGWltpMGEMGGQLSGGERQRISIARALL 497
Cdd:cd03295   80 VIQQIGLFPHmTVEENIalvpkLLKWPKEKIRE-----RADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARALA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAHRL-STIAGAGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:cd03295  152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227

LolD

COG1136

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

344-560

1.28e-35

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.63 E-value: 1.28e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD--PALNNLSLTFPAASMSALVGASGAGKTT----VSkLLMRyadPQQGEISIGGVDIRHLTAEQL 417
Cdd:COG1136    5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTllniLG-GLDR---PTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 418 ----NSLISVVFQDVWLFDD-TLLANLLIARPQATQQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGE 486
Cdd:COG1136   81 arlrRRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARELLErvglgdRLDHRP-----------SQLSGGQ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 487 RQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQ 560
Cdd:COG1136  150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225

FepC

COG1120

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

344-568

2.22e-35

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];

Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 133.63 E-value: 2.22e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:COG1120    2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVwlfddTLLANL---------------LIARPQAT-QQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGER 487
Cdd:COG1120   80 VPQEP-----PAPFGLtvrelvalgryphlgLFGRPSAEdREAVEEALERTGLEHLADR-------PVDE----LSGGER 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 488 QRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHA 564
Cdd:COG1120  144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPE 223


                 ....
gi 515713280 565 QLLS 568
Cdd:COG1120  224 EVLT 227

ABC_ATPase

cd00267

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

349-556

3.71e-35

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: 129.67 E-value: 3.71e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQdv 428
Cdd:cd00267    5 LSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 wlfddtllanlliarpqatqqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:cd00267   81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515713280 509 TAALDIDSELAVQKAI-DHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGE 556
Cdd:cd00267  108 TSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAADrVIVLKDGK 157

MRP_assoc_pro

TIGR00957

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

339-576

6.38e-35

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: 141.62 E-value: 6.38e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   339 PERYDIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLN 418
Cdd:TIGR00957 1280 PPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR 1359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   419 SLISVVFQDVWLFDDTLLANLliaRP--QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARAL 496
Cdd:TIGR00957 1360 FKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARAL 1436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQAL 576
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516

ABC_MJ0796_LolCDE_FtsE

cd03255

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

344-557

1.07e-34

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: 130.69 E-value: 1.07e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD--PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL- 420
Cdd:cd03255    1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ---ISVVFQDVWLFDD-TLLANLLIARPQATQQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:cd03255   81 rrhIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELLErvglgdRLNHYP-----------SELSGGQQQRV 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAGAGNILVMEEGEV 557
Cdd:cd03255  150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218

FetA

COG4619

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

344-557

1.57e-34

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.94 E-value: 1.57e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:COG4619    1 LELEGLSFRVG--GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLliARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEmggqLSGGERQRISIARALLKDAPIV 503
Cdd:COG4619   79 VPQEPALWGGTVRDNL--PFPFQLRERKFDRERALELLERLGLPPDILDKPVER----LSGGERQRLALIRALLLQPDVL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIA-GAGNILVMEEGEV 557
Cdd:COG4619  153 LLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209

ABC_Iron-Siderophores_B12_Hemin

cd03214

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

349-561

2.87e-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: 128.32 E-value: 2.87e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQdv 428
Cdd:cd03214    5 LSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 wlfddtllanlliarpqatqqeveeAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:cd03214   81 -------------------------ALELLGLAHLADR-------PFNE----LSGGERQRVLLARALAQEPPILLLDEP 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 509 TAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03214  125 TSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180

MlaF

COG1127

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

344-567

4.93e-34

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: 129.33 E-value: 4.93e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:COG1127    6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANL---LIARPQATQQEVEEaaRAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:COG1127   84 IGMLFQGGALFDSlTVFENVafpLREHTDLSEAEIRE--LVLEKLElvglpgAADKMP-----------SELSGGMRKRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLL 567
Cdd:COG1127  151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELL 230

ABCC_SUR2

cd03288

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

343-570

6.14e-34

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.

Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 129.64 E-value: 6.14e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLIS 422
Cdd:cd03288   19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQDVWLFDDTLLANLLIARpQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:cd03288   99 IILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:cd03288  178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245

ABC_Carb_Solutes_like

cd03259

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

344-561

2.00e-33

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: 126.87 E-value: 2.00e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISV 423
Cdd:cd03259    1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANLLIA-----RPQATQQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:cd03259   77 VFQDYALFPHlTVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARAL 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLS-TIAGAGNILVMEEGEVVEQG 561
Cdd:cd03259  146 AREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213

PTZ00265

multidrug resistance protein (mdr1); Provisional

359-574

2.14e-33

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.70 E-value: 2.14e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAD------------------------------------------ 396
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefslt 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  397 ------------PQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFI 464
Cdd:PTZ00265 1262 keggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFI 1341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  465 SRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAHRLST 542
Cdd:PTZ00265 1342 ESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIAS 1421

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 515713280  543 IAGAGNILVMEE----GEVVE-QGTHAQLLSRQ-GRYQ 574
Cdd:PTZ00265 1422 IKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQdGVYK 1459

ABC_Org_Solvent_Resistant

cd03261

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

344-566

3.25e-33

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: 127.23 E-value: 3.25e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:cd03261    1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANllIARP-----QATQQEVEEaaRAAQCLEFISRLPQGWLTPmgemgGQLSGGERQRISIAR 494
Cdd:cd03261   79 MGMLFQSGALFDSlTVFEN--VAFPlrehtRLSEEEIRE--IVLEKLEAVGLRGAEDLYP-----AELSGGMKKRVALAR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 495 ALLKDAPIVILDEPTAALD-IDSElavqkAIDHLVH------NRTVIIIAHRLSTIAGAG-NILVMEEGEVVEQGTHAQL 566
Cdd:cd03261  150 ALALDPELLLYDEPTAGLDpIASG-----VIDDLIRslkkelGLTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGTPEEL 224

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

344-567

1.74e-32

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 1.74e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:PRK13632   8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQD-------VWLFDDTL--LANLLIArPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:PRK13632  88 IFQNpdnqfigATVEDDIAfgLENKKVP-PKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHL--VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLL 567
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230

ABCC_MRP_domain1

cd03250

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

344-556

2.16e-32

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: 123.73 E-value: 2.16e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDD---SGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVdirhltaeqlnsl 420
Cdd:cd03250    1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDDTLLANLLIARPqATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDA 500
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 501 PIVILDEPTAALDIDSELAV-QKAI-DHLVHNRTVIIIAHRLSTIAGAGNILVMEEGE 556
Cdd:cd03250  147 DIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204

PLN03232

ABC transporter C family member; Provisional

297-571

2.28e-32

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.56 E-value: 2.28e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  297 FSEPMAMFISYTS-VVELIASAL-------------QRIEQFMALPPLPVA------ERGEMPERYDIRFDTICYRYDDS 356
Cdd:PLN03232 1168 FASTMGLLLSYTLnITTLLSGVLrqaskaenslnsvERVGNYIDLPSEATAiiennrPVSGWPSRGSIKFEDVHLRYRPG 1247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLL 436
Cdd:PLN03232 1248 LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVR 1327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  437 ANLliaRPQATQQEVE--EAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDI 514
Cdd:PLN03232 1328 FNI---DPFSEHNDADlwEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280  515 DSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:PLN03232 1405 RTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461

PvdE

COG4615

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

31-507

1.15e-31

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];

Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 129.15 E-value: 1.15e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  31 RRSMIALLLAALMQGIAFACLYPIVDALLRGEASPLLTWALVFSATAFAALALRWY-GLGFEYRGHlaQATHELRLRLGE 109
Cdd:COG4615   12 RWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ--HAVARLRLRLSR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 110 QLRRVPLERLQRGRAGETNALLLGSVDenlnyVIAIANILLLTIVTPLTASLATL----WIDWRLGLVMLLIFPMLVPFY 185
Cdd:COG4615   90 RILAAPLERLERIGAARLLAALTEDVR-----TISQAFVRLPELLQSVALVLGCLaylaWLSPPLFLLTLVLLGLGVAGY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 186 YWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTcgsDGEKSRALLAhfNALE--SLQSRTHRQSAGATMLIAGVVE 263
Cdd:COG4615  165 RLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKL---NRRRRRAFFD--EDLQptAERYRDLRIRADTIFALANNWG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 264 ----LGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRfsEPMAMFISYTSVVELIASALQRIEQFMALPPLPVAERGEMP 339
Cdd:COG4615  240 nllfFALIGLILFLLPALGWADPAVLSGFVLVLLFLR--GPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 340 ERYD------IRFDTICYRYDDSGDP---ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMR-YAdPQQGEISIGGVDI 409
Cdd:COG4615  318 APPApadfqtLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYR-PESGEILLDGQPV 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 410 RHLTAEQLNSLISVVFQDVWLFDDtllanLLIARPQATQQEVEEaaraaqclefisrlpqgWLTPMgEMGG--------- 480
Cdd:COG4615  397 TADNREAYRQLFSAVFSDFHLFDR-----LLGLDGEADPARARE-----------------LLERL-ELDHkvsvedgrf 453

                        490       500       510
                 ....*....|....*....|....*....|
gi 515713280 481 ---QLSGGERQRISIARALLKDAPIVILDE 507
Cdd:COG4615  454 sttDLSQGQRKRLALLVALLEDRPILVFDE 483

PLN03130

ABC transporter C family member; Provisional

297-571

1.20e-31

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 131.40 E-value: 1.20e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  297 FSEPMAMFISYT--------------SVVELIASALQRIEQFMALPPL--PVAERGEMPERY----DIRFDTICYRYDDS 356
Cdd:PLN03130 1171 FASTMGLLLSYAlnitslltavlrlaSLAENSLNAVERVGTYIDLPSEapLVIENNRPPPGWpssgSIKFEDVVLRYRPE 1250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLL 436
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVR 1330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  437 ANLliaRPQATQQEVE--EAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDI 514
Cdd:PLN03130 1331 FNL---DPFNEHNDADlwESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280  515 DSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:PLN03130 1408 RTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464

ThiQ

COG3840

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

344-570

1.23e-31

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.56 E-value: 1.23e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgdpALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQlnSLISV 423
Cdd:COG3840    2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANLLIA-----RPQATQQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:COG3840   76 LFQENNLFPHlTVAQNIGLGlrpglKLTAEQRAqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 497 LKDAPIVILDEPTAALDIdselAVQKAIDHLV------HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG3840  145 VRKRPILLLDEPFSALDP----ALRQEMLDLVdelcreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220


                 .
gi 515713280 570 Q 570
Cdd:COG3840  221 E 221

DppD

COG0444

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

359-569

3.46e-31

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: 123.62 E-value: 3.46e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ---QGEISIGGVDIRHLTAEQLNSL----ISVVFQD---- 427
Cdd:COG0444   19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKIrgreIQMIFQDpmts 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 ---VW----LFDDTLLANLLIARPQATqqeveeaARAAQCLE---------FISRLPqgwltpmgemgGQLSGGERQRIS 491
Cdd:COG0444   99 lnpVMtvgdQIAEPLRIHGGLSKAEAR-------ERAIELLErvglpdperRLDRYP-----------HELSGGMRQRVM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 492 IARALLKDAPIVILDEPTAALDIdselAVQKAI-DHLV-----HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHA 564
Cdd:COG0444  161 IARALALEPKLLIADEPTTALDV----TIQAQIlNLLKdlqreLGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVE 236


                 ....*
gi 515713280 565 QLLSR 569
Cdd:COG0444  237 ELFEN 241

ZnuC

COG1121

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

338-570

5.65e-31

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 5.65e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 338 MPERYDIRFDTICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRhltaeQL 417
Cdd:COG1121    1 MMMMPAIELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 418 NSLISVVFQDV---WLF----DDTLLANL-----LIARPQATQQE-VEEAARAAQCLEFISRlpqgwltPMGEmggqLSG 484
Cdd:COG1121   74 RRRIGYVPQRAevdWDFpitvRDVVLMGRygrrgLFRRPSRADREaVDEALERVGLEDLADR-------PIGE----LSG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 485 GERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTH 563
Cdd:COG1121  143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPP 222


                 ....*..
gi 515713280 564 AQLLSRQ 570
Cdd:COG1121  223 EEVLTPE 229

ABC_DR_subfamily_A

cd03230

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

352-557

2.05e-30

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: 117.11 E-value: 2.05e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHlTAEQLNSLISVVFQDVWLF 431
Cdd:cd03230    9 RYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DD-TLLANLliarpqatqqeveeaaraaqclefisrlpqgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:cd03230   86 ENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713280 511 ALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:cd03230  125 GLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173

PTZ00265

multidrug resistance protein (mdr1); Provisional

337-556

2.37e-29

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 124.37 E-value: 2.37e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  337 EMPERYDIRFDTICYRYDDSGDPAL-NNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV-DIRHLTA 414
Cdd:PTZ00265  376 KLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINL 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  415 EQLNSLISVVFQDVWLFDDTLLANLL-----IARPQATQQEVEEAARAAQ------------CL---------------- 461
Cdd:PTZ00265  456 KWWRSKIGVVSQDPLLFSNSIKNNIKyslysLKDLEALSNYYNEDGNDSQenknkrnscrakCAgdlndmsnttdsneli 535

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  462 ------------------------EFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSE 517
Cdd:PTZ00265  536 emrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 515713280  518 LAVQKAIDHLV--HNRTVIIIAHRLSTIAGAGNILVMEEGE 556
Cdd:PTZ00265  616 YLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRE 656

MRP_assoc_pro

TIGR00957

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

285-573

1.05e-28

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 122.36 E-value: 1.05e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   285 AFLIAAAAMIMRFsePMAMFISYTSVVELIASALQRIEQFMA---LPPLPVAERGEMP-ERYDIRFDTICYRYDDSGDPA 360
Cdd:TIGR00957  576 AFVSLALFNILRF--PLNILPMVISSIVQASVSLKRLRIFLSheeLEPDSIERRTIKPgEGNSITVHNATFTWARDLPPT 653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVdirhltaeqlnslISVVFQDVWLFDDTLLANLL 440
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   441 IARP--QATQQEVEEAARAAQCLEFisrLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDsel 518
Cdd:TIGR00957  721 FGKAlnEKYYQQVLEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH--- 794

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280   519 aVQKAI-DHLV------HNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRY 573
Cdd:TIGR00957  795 -VGKHIfEHVIgpegvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855

ABC_Metallic_Cations

cd03235

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

345-561

1.05e-28

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

Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.78 E-value: 1.05e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 345 RFDTICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIrhltaEQLNSLISVV 424
Cdd:cd03235    1 EVEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 425 FQ----------DVWlfdDTLLANLLIARPQATQQEVEEAARAAQCLEFisrlpqgwlTPMGEMG----GQLSGGERQRI 490
Cdd:cd03235   74 PQrrsidrdfpiSVR---DVVLMGLYGHKGLFRRLSKADKAKVDEALER---------VGLSELAdrqiGELSGGQQQRV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQG 561
Cdd:cd03235  142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213

ABC_PotA_N

cd03300

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

344-562

1.20e-28

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: 114.26 E-value: 1.20e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISV 423
Cdd:cd03300    1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLAN----LLIAR--PQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:cd03300   77 VFQNYALFPHlTVFENiafgLRLKKlpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARAL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLvHNR---TVIIIAHRLS-TIAGAGNILVMEEGEVVEQGT 562
Cdd:cd03300  146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRL-QKElgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214

ABC_MetN_methionine_transporter

cd03258

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

344-569

1.35e-28

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: 113.83 E-value: 1.35e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD--PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL- 420
Cdd:cd03258    2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 --ISVVFQDVWLFDD-TLLANllIARPQ--ATQQEVEEAARAAQCLEFI------SRLPqgwltpmgemgGQLSGGERQR 489
Cdd:cd03258   82 rrIGMIFQHFNLLSSrTVFEN--VALPLeiAGVPKAEIEERVLELLELVgledkaDAYP-----------AQLSGGQKQR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 490 ISIARALLKDAPIVILDEPTAALD---IDSELAVQKAIdhlvhNR----TVIIIAHRLSTIAGAGN-ILVMEEGEVVEQG 561
Cdd:cd03258  149 VGIARALANNPKVLLCDEATSALDpetTQSILALLRDI-----NRelglTIVLITHEMEVVKRICDrVAVMEKGEVVEEG 223


                 ....*...
gi 515713280 562 THAQLLSR 569
Cdd:cd03258  224 TVEEVFAN 231

ABC_Mj1267_LivG_branched

cd03219

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

360-568

3.95e-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: 112.53 E-value: 3.95e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLFDD-TLLA 437
Cdd:cd03219   15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLIARPQAT----------QQEVEEAARAAQCLEFIsRLPQGWLTPMGEmggqLSGGERQRISIARALLKDAPIVILDE 507
Cdd:cd03219   95 NVMVAAQARTgsglllararREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 508 PTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:cd03219  170 PAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232

PhnC

COG3638

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

344-566

5.93e-28

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 112.46 E-value: 5.93e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:COG3638    3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANLLIAR-----------PQATQQEVEeaaRAAQCLEFISRLPQGWltpmgEMGGQLSGGERQ 488
Cdd:COG3638   82 IGMIFQQFNLVPRlSVLTNVLAGRlgrtstwrsllGLFPPEDRE---RALEALERVGLADKAY-----QRADQLSGGQQQ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 489 RISIARALLKDAPIVILDEPTAALDIdsELAvQKAIDHLV-----HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGT 562
Cdd:COG3638  154 RVAIARALVQEPKLILADEPVASLDP--KTA-RQVMDLLRriareDGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGP 230


                 ....
gi 515713280 563 HAQL 566
Cdd:COG3638  231 PAEL 234

ABC_PstB_phosphate_transporter

cd03260

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

344-566

6.97e-28

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

Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 111.89 E-value: 6.97e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAD-----PQQGEISIGGVDIRHL--TAEQ 416
Cdd:cd03260    1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 417 LNSLISVVFQDVWLFDDTLLANLLIA-RPQATQQEVEEAARAAQCLEfisrlpQGWLTpmGEM-----GGQLSGGERQRI 490
Cdd:cd03260   79 LRRRVGMVFQKPNPFPGSIYDNVAYGlRLHGIKLKEELDERVEEALR------KAALW--DEVkdrlhALGLSGGQQQRL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQL 566
Cdd:cd03260  151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227

ABC_ThiQ_thiamine_transporter

cd03298

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

344-561

9.88e-28

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: 111.05 E-value: 9.88e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYddsGDPALNnLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDirHLTAEQLNSLISV 423
Cdd:cd03298    1 VRLDKIRFSY---GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD--VTAAPPADRPVSM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANLLIARP------QATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:cd03298   75 LFQENNLFAHlTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03298  144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211

ABC_cobalt_CbiO_domain2

cd03226

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

349-558

2.14e-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: 109.65 E-value: 2.14e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDDSGDpALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRhltAEQLNSLISVVFQDV 428
Cdd:cd03226    5 ISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 --WLFDDTLLANLLIARPQA--TQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVI 504
Cdd:cd03226   81 dyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLI 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 505 LDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAGAGNILV-MEEGEVV 558
Cdd:cd03226  150 FDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVCDRVLlLANGAIV 205

ABC_PhnC_transporter

cd03256

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

344-566

2.84e-27

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: 110.35 E-value: 2.84e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:cd03256    1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANLLIAR--------PQATQQEVEEAARAAQCLEFISRLPQGWltpmgEMGGQLSGGERQRIS 491
Cdd:cd03256   80 IGMIFQQFNLIERlSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAY-----QRADQLSGGQQQRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 492 IARALLKDAPIVILDEPTAALDIDSELAVQKAI--DHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQL 566
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREYADrIVGLKDGRIVFDGPPAEL 232

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

344-569

2.97e-27

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.65 E-value: 2.97e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:PRK13635   6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQD-------VWLFDDTL--LANLLIARPQaTQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:PRK13635  86 VFQNpdnqfvgATVQDDVAfgLENIGVPREE-MVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230

ABC_Class3

cd03229

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

344-556

3.85e-27

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: 108.04 E-value: 3.85e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAE--QLNSLI 421
Cdd:cd03229    1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 422 SVVFQDVWLFDD-TLLANLLIArpqatqqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDA 500
Cdd:cd03229   79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 501 PIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAG-AGNILVMEEGE 556
Cdd:cd03229  120 DVLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

360-569

7.65e-27

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: 114.78 E-value: 7.65e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRyADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQD--------- 427
Cdd:COG4172  301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDpfgslsprm 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 -VwlfDDTLLANLLIARPQATQQEVEEAARAAqcLE-------FISRLPQgwltpmgemggQLSGGERQRISIARALLKD 499
Cdd:COG4172  380 tV---GQIIAEGLRVHGPGLSAAERRARVAEA--LEevgldpaARHRYPH-----------EFSGGQRQRIAIARALILE 443

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 500 APIVILDEPTAALDidseLAVQKAIDHLV------HNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG4172  444 PKLLVLDEPTSALD----VSVQAQILDLLrdlqreHGLAYLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQVFDA 516

ABC_TM1139_LivF_branched

cd03224

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

353-568

1.75e-26

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: 107.52 E-value: 1.75e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 353 YDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLF 431
Cdd:cd03224   10 YGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DD-TLLANLLIARpqATQQEVEEAARAAQCLEFISRLPQGWltpmGEMGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:cd03224   88 PElTVEENLLLGA--YARRRAKRKARLERVYELFPRLKERR----KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 511 ALdidSELAVQKAIDHLVHNR----TVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:cd03224  162 GL---APKIVEEIFEAIRELRdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221

MalK

COG3839

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

343-562

2.00e-26

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.55 E-value: 2.00e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTvsklLMRY-A---DPQQGEISIGGVDIRHLTAEQLN 418
Cdd:COG3839    3 SLELENVSKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMiAgleDPTSGEILIGGRDVTDLPPKDRN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 419 slISVVFQDVWLFDD-TLLAN----LLIAR-PQATQQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRIS 491
Cdd:COG3839   77 --IAMVFQSYALYPHmTVYENiafpLKLRKvPKAEIDRrVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 492 IARALLKDAPIVILDEPTAALdiDSELAVQ-----KAIdhlvHNR---TVIIIAHRLS---TIagAGNILVMEEGEVVEQ 560
Cdd:COG3839  144 LGRALVREPKVFLLDEPLSNL--DAKLRVEmraeiKRL----HRRlgtTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215


                 ..
gi 515713280 561 GT 562
Cdd:COG3839  216 GT 217

LivG

COG0411

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

360-562

2.31e-26

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: 108.20 E-value: 2.31e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLFDD-TLLA 437
Cdd:COG0411   19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLIAR---------------PQATQQEVEEAARAAQCLEFISrlpqgwLTP-MGEMGGQLSGGERQRISIARALLKDAP 501
Cdd:COG0411   99 NVLVAAharlgrgllaallrlPRARREEREARERAEELLERVG------LADrADEPAGNLSYGQQRRLEIARALATEPK 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 502 IVILDEPTAALDiDSElaVQKAIDHLV-----HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGT 562
Cdd:COG0411  173 LLLLDEPAAGLN-PEE--TEELAELIRrlrdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236

ABC_FtsE

cd03292

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

344-538

2.62e-26

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages

Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 106.72 E-value: 2.62e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:cd03292    1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANLLIARP--QATQQEVEEaaRAAQCLEFIsrlpqGWLTPMGEMGGQLSGGERQRISIARALL 497
Cdd:cd03292   80 IGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHlVHNR--TVIIIAH 538
Cdd:cd03292  153 NSPTILIADEPTGNLDPDTTWEIMNLLKK-INKAgtTVVVATH 194

GlnQ

COG1126

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

344-569

5.15e-26

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 106.62 E-value: 5.15e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIrHLTAEQLNSL--- 420
Cdd:COG1126    2 IEIENLHKSFGDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLrrk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLANLLIA------RPQAtqqEVEEAARAAqcLE------FISRLPqgwltpmgemgGQLSGGER 487
Cdd:COG1126   79 VGMVFQQFNLFPHlTVLENVTLApikvkkMSKA---EAEERAMEL--LErvgladKADAYP-----------AQLSGGQQ 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 488 QRISIARALlkdA--PIVIL-DEPTAALdiDSELA--VQKAIDHLVHN-RTVII----------IAHRlstiagagnILV 551
Cdd:COG1126  143 QRVAIARAL---AmePKVMLfDEPTSAL--DPELVgeVLDVMRDLAKEgMTMVVvthemgfareVADR---------VVF 208

                        250
                 ....*....|....*...
gi 515713280 552 MEEGEVVEQGTHAQLLSR 569
Cdd:COG1126  209 MDGGRIVEEGPPEEFFEN 226

fecE

PRK11231

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;

361-568

6.83e-26

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 6.83e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQdVWLFDDTLLANLL 440
Cdd:PRK11231  18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHLTPEGITVREL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 441 IA---RP---------QATQQEVEEAARAAQCLEFISRLpqgwLTpmgemggQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:PRK11231  97 VAygrSPwlslwgrlsAEDNARVNQAMEQTRINHLADRR----LT-------DLSGGQRQRAFLAMVLAQDTPVVLLDEP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 509 TAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

349-568

1.01e-25

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.39 E-value: 1.01e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDV 428
Cdd:PRK13548   8 LSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WL-FDDTLLANLLIAR------PQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALL---- 497
Cdd:PRK13548  86 SLsFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLARVLAqlwe 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 498 --KDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLS-TIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230

ABC_drug_resistance_like

cd03264

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

360-561

1.28e-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: 104.97 E-value: 1.28e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAAsMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHlTAEQLNSLISVVFQD--------VWLF 431
Cdd:cd03264   15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEfgvypnftVREF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DDTLLANLLIARPQAtQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:cd03264   93 LDYIAWLKGIPSKEV-KARVDEVLELVNLGDRAKKKI-----------GSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515713280 512 LDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03264  161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211

cbiO

PRK13646

energy-coupling factor transporter ATPase;

344-577

3.58e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 3.58e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdSGDP----ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAE---- 415
Cdd:PRK13646   3 IRFDNVSYTYQ-KGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyir 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 416 QLNSLISVVFQ--DVWLFDDTLLANLLIArPQATQQEVEEA-ARAAQCL-EF-ISRlpqgwlTPMGEMGGQLSGGERQRI 490
Cdd:PRK13646  82 PVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVkNYAHRLLmDLgFSR------DVMSQSPFQMSGGQMRKI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLL 567
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234

                        250
                 ....*....|
gi 515713280 568 sRQGRYQALW 577
Cdd:PRK13646 235 -KDKKKLADW 243

TauB

COG1116

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

344-559

4.80e-25

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.40 E-value: 4.80e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD--PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEqlnslI 421
Cdd:COG1116    8 LELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 422 SVVFQDV----WLfddTLLANLLIARPQATQQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRIS 491
Cdd:COG1116   83 GVVFQEPallpWL---TVLDNVALGLELRGVPKAERRERARELLElvglagFEDAYP-----------HQLSGGMRQRVA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 492 IARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAH------RLSTiagagNILVMEE--GEVVE 559
Cdd:COG1116  149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavFLAD-----RVVVLSArpGRIVE 221

ABC_CysA_sulfate_importer

cd03296

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

342-562

5.41e-25

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: 103.96 E-value: 5.41e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 342 YDIRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslI 421
Cdd:cd03296    1 MSIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--V 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 422 SVVFQDVWLFDD-TLLANL---LIARPQATQQ-EVEEAARAAQCLEFI------SRLPQgwltpmgemggQLSGGERQRI 490
Cdd:cd03296   77 GFVFQHYALFRHmTVFDNVafgLRVKPRSERPpEAEIRAKVHELLKLVqldwlaDRYPA-----------QLSGGQRQRV 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 491 SIARALLKDAPIVILDEPTAALD--IDSEL-AVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGT 562
Cdd:cd03296  146 ALARALAVEPKVLLLDEPFGALDakVRKELrRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220

cbiO

PRK13640

energy-coupling factor transporter ATPase;

344-569

9.16e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.50 E-value: 9.16e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKL---LMRYADPQQGEISIGGVDIRHLTAEQLNSL 420
Cdd:PRK13640   6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQD-------VWLFDDTL--LANLLIARPQaTQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRIS 491
Cdd:PRK13640  86 VGIVFQNpdnqfvgATVGDDVAfgLENRAVPRPE-MIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 492 IARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233

AbcC

COG1135

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

344-569

9.95e-25

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 9.95e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDP--ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL- 420
Cdd:COG1135    2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 --ISVVFQDvwlfddtllANLL--------IARP--QATQQEVEEAARAAQCLEFI------SRLPqgwltpmgemgGQL 482
Cdd:COG1135   82 rkIGMIFQH---------FNLLssrtvaenVALPleIAGVPKAEIRKRVAELLELVglsdkaDAYP-----------SQL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 483 SGGERQRISIARALLKDAPIVILDEPTAALD---IDSELAVQKAIdhlvhNR----TVIIIAHRLSTI-AGAGNILVMEE 554
Cdd:COG1135  142 SGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSILDLLKDI-----NRelglTIVLITHEMDVVrRICDRVAVLEN 216

                        250
                 ....*....|....*
gi 515713280 555 GEVVEQGTHAQLLSR 569
Cdd:COG1135  217 GRIVEQGPVLDVFAN 231

PotA

COG3842

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

343-562

1.76e-24

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.18 E-value: 1.76e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTvsklLMR----YADPQQGEISIGGVDIRHLTAEQLN 418
Cdd:COG3842    5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGLPPEKRN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 419 slISVVFQDVWLFDD-TLLANllIA-------RPQAtqqevEEAARAAQCLE------FISRLPqgwltpmgemgGQLSG 484
Cdd:COG3842   79 --VGMVFQDYALFPHlTVAEN--VAfglrmrgVPKA-----EIRARVAELLElvglegLADRYP-----------HQLSG 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 485 GERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLS---TIagAGNILVMEEGEVVE 559
Cdd:COG3842  139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQ 216


                 ...
gi 515713280 560 QGT 562
Cdd:COG3842  217 VGT 219

AppF

COG4608

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

360-569

1.89e-24

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.43 E-value: 1.89e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQD--------- 427
Cdd:COG4608   33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDpyaslnprm 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 -VwlfDDTLLANLLIARpQATQQEVEEaaRAAQCL-------EFISRLPQgwltpmgemggQLSGGERQRISIARALLKD 499
Cdd:COG4608  113 tV---GDIIAEPLRIHG-LASKAERRE--RVAELLelvglrpEHADRYPH-----------EFSGGQRQRIGIARALALN 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 500 APIVILDEPTAALDIdselAVQKAIDHLV------HNRTVIIIAHRLST---IagAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG4608  176 PKLIVCDEPVSALDV----SIQAQVLNLLedlqdeLGLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYAR 248

ABCC_CFTR1

cd03291

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

357-570

1.95e-24

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.

Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 103.40 E-value: 1.95e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEIsiggvdiRHltaeqlNSLISVVFQDVWLFDDTLL 436
Cdd:cd03291   49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KH------SGRISFSSQFSWIMPGTIK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLlIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDS 516
Cdd:cd03291  116 ENI-IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 517 ELAV-QKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:cd03291  195 EKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249

CcmA

COG4133

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

344-546

4.12e-24

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: 100.25 E-value: 4.12e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLtAEQLNSLISV 423
Cdd:COG4133    3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANLLIAR----PQATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLK 498
Cdd:COG4133   80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLLS 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713280 499 DAPIVILDEPTAALDIDSELAVQKAI-DHLVHNRTVIIIAHRLSTIAGA 546
Cdd:COG4133  149 PAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAA 197

ABCG_EPDR

cd03213

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

361-561

8.95e-24

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.

Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 99.16 E-value: 8.95e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQ--GEISIGGVDIRhltAEQLNSLISVVFQDvwlfdDTLLAN 438
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLD---KRSFRKIIGYVPQD-----DILHPT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 439 LliarpqaTqqeVEEAaraaqcLEFISRLpQGwltpmgemggqLSGGERQRISIARALLKDAPIVILDEPTAALDIDSEL 518
Cdd:cd03213   97 L-------T---VRET------LMFAAKL-RG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515713280 519 AVQKAIDHLVH-NRTVIIIAHRLST--IAGAGNILVMEEGEVVEQG 561
Cdd:cd03213  149 QVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194

ABC_Pro_Gly_Betaine

cd03294

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

359-567

9.98e-24

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: 101.18 E-value: 9.98e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL----ISVVFQDVWLFDD- 433
Cdd:cd03294   38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHr 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 434 TLLANLLIARPQATQQEVEEAARAAQCLEFISrlpqgwLTPMGE-MGGQLSGGERQRISIARALLKDAPIVILDEPTAAL 512
Cdd:cd03294  118 TVLENVAFGLEVQGVPRAEREERAAEALELVG------LEGWEHkYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 513 D--IDSELAvqkaiDHLV-----HNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLL 567
Cdd:cd03294  192 DplIRREMQ-----DELLrlqaeLQKTIVFITHDLDEALRLGDrIAIMKDGRLVQVGTPEEIL 249

nickel_nikE

TIGR02769

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

359-568

1.05e-23

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: 101.04 E-value: 1.05e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQDVW-LFDDT 434
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQDSPsAVNPR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  435 LLANLLIARPQATQQEVEEAARAAQCLEFIS----------RLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVI 504
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIAELLDmvglrsedadKLPR-----------QLSGGQLQRINIARALAVKPKLIV 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280  505 LDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLS 240

ABC_ModC_like

cd03299

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

355-569

1.68e-23

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: 99.33 E-value: 1.68e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 355 DSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISVVFQDVWLFDDT 434
Cdd:cd03299    9 DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFPHM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 435 L--------LANLLIARPQaTQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILD 506
Cdd:cd03299   87 TvykniaygLKKRKVDKKE-IERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLD 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 507 EPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLSR 569
Cdd:cd03299  155 EPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADkVAIMLNGKLIQVGKPEEVFKK 220

ABC_NrtD_SsuB_transporters

cd03293

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

344-538

1.91e-23

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: 98.70 E-value: 1.91e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDP--ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRhltaeQLNSLI 421
Cdd:cd03293    1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 422 SVVFQDVWLFD-DTLLANLLIARPQATQQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRISIAR 494
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLElvglsgFENAYP-----------HQLSGGMRQRVALAR 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQkaiDHLV-----HNRTVIIIAH 538
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQ---EELLdiwreTGKTVLLVTH 190

ArtP

COG4161

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

344-564

3.87e-23

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 3.87e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI---RHLTAEQLNSL 420
Cdd:COG4161    3 IQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ---ISVVFQDVWLFDD-TLLANLLIARPQATQQEVEEA-ARAAQCL------EFISRLPQgwltpmgemggQLSGGERQR 489
Cdd:COG4161   81 rqkVGMVFQQYNLWPHlTVMENLIEAPCKVLGLSKEQArEKAMKLLarlrltDKADRFPL-----------HLSGGQQQR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 490 ISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR-TVIIIAHRLStIAG--AGNILVMEEGEVVEQGTHA 564
Cdd:COG4161  150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVE-FARkvASQVVYMEKGRIIEQGDAS 226

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

352-566

6.85e-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: 97.19 E-value: 6.85e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHlTAEQLNSLISVVFQdvwlf 431
Cdd:cd03263    9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQ----- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DDTLLANLliarpqaTqqeveeaarAAQCLEFISRLpQG-----------WLTPMGEMG-------GQLSGGERQRISIA 493
Cdd:cd03263   83 FDALFDEL-------T---------VREHLRFYARL-KGlpkseikeeveLLLRVLGLTdkankraRTLSGGMKRKLSLA 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 494 RALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAH------RLSTiagagNILVMEEGEVVEQGTHAQL 566
Cdd:cd03263  146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCD-----RIAIMSDGKLRCIGSPQEL 219

ABC_Carb_Monos_I

cd03216

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

344-558

9.28e-23

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: 95.19 E-value: 9.28e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLT-AEQLNSLIS 422
Cdd:cd03216    1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQdvwlfddtllanlliarpqatqqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDAPI 502
Cdd:cd03216   79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 503 VILDEPTAALDiDSElaVQKAIDHLV----HNRTVIIIAHRLSTI-AGAGNILVMEEGEVV 558
Cdd:cd03216  104 LILDEPTAALT-PAE--VERLFKVIRrlraQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161

ABCC_SUR1_N

cd03290

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

356-555

1.01e-22

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: 96.63 E-value: 1.01e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 356 SGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEI--SIGGVDIRHLTAEQLNSLISVVF--QDVWLF 431
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRYSVAYaaQKPWLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DDTLLANLLIARPqATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:cd03290   92 NATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515713280 512 LDID-SELAVQKAIDHLVHN--RTVIIIAHRLSTIAGAGNILVMEEG 555
Cdd:cd03290  171 LDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217

thiQ

TIGR01277

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...

365-561

1.45e-22

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: 96.08 E-value: 1.45e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  365 SLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDirHLTAEQLNSLISVVFQDVWLFDD-TLLANLLIA- 442
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  443 ----RPQATQQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILDEPTAALD---- 513
Cdd:TIGR01277  96 hpglKLNAEQQEkVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllr 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515713280  514 -----IDSELAVQKaidhlvhNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:TIGR01277 165 eemlaLVKQLCSER-------QRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

344-566

1.48e-22

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: 96.28 E-value: 1.48e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEqLNSLISV 423
Cdd:cd03265    1 IEVENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLfDDTLLA--NLLI-ARPQATQQEvEEAARAAQCLEFIsrlpqGWLTPMGEMGGQLSGGERQRISIARALLKDA 500
Cdd:cd03265   78 VFQDLSV-DDELTGweNLYIhARLYGVPGA-ERRERIDELLDFV-----GLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 501 PIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQL 566
Cdd:cd03265  151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219

ABC_MalK_N

cd03301

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

344-561

2.12e-22

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.

Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.78 E-value: 2.12e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISV 423
Cdd:cd03301    1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLAN------LLIARPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:cd03301   77 VFQNYALYPHmTVYDNiafglkLRKVPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAI 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 497 LKDAPIVILDEPTAALdiDSELAVQKAID----HLVHNRTVIIIAH-RLSTIAGAGNILVMEEGEVVEQG 561
Cdd:cd03301  146 VREPKVFLMDEPLSNL--DAKLRVQMRAElkrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213

CeuD

COG4604

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...

344-567

3.20e-22

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.31 E-value: 3.20e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:COG4604    2 IEIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDvwlfddtllaNLLIAR------------P-------QATQQEVEEAaraaqcLEFISrlpqgwLTPM-GEMGGQLS 483
Cdd:COG4604   80 LRQE----------NHINSRltvrelvafgrfPyskgrltAEDREIIDEA------IAYLD------LEDLaDRYLDELS 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 484 GGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQ 560
Cdd:COG4604  138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFASCyADHIVAMKDGRVVAQ 217


                 ....*..
gi 515713280 561 GTHAQLL 567
Cdd:COG4604  218 GTPEEII 224

MglA

COG1129

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

359-566

3.46e-22

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 3.46e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLT---AEQLNslISVVFQDVWLFDD-T 434
Cdd:COG1129   18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAAG--IAIIHQELNLVPNlS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 435 LLANLLIARPQATQQEVEEAARAAQCLEFISRL-----PQgwlTPMGEmggqLSGGERQRISIARALLKDAPIVILDEPT 509
Cdd:COG1129   96 VAENIFLGREPRRGGLIDWRAMRRRARELLARLgldidPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 510 AALDiDSElavqkaIDHLV--------HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQL 566
Cdd:COG1129  169 ASLT-ERE------VERLFriirrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

344-562

3.81e-22

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.48 E-value: 3.81e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISV 423
Cdd:PRK09452  15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH--VNT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANLLIA-RPQATQQE-----VEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:PRK09452  91 VFQSYALFPHmTVFENVAFGlRMQKTPAAeitprVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAH-RLSTIAGAGNILVMEEGEVVEQGT 562
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

344-588

4.54e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.34 E-value: 4.54e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:PRK13647   5 IEVEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQD---------VWlfDDTLLANL-LIARPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIA 493
Cdd:PRK13647  84 VFQDpddqvfsstVW--DDVAFGPVnMGLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 494 RALLKDAPIVILDEPTAALDIDSELAVQKAIDHLvHNR--TVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229

                        250
                 ....*....|....*...
gi 515713280 571 GRYQALWQAQMAARVWRD 588
Cdd:PRK13647 230 IVEQAGLRLPLVAQIFED 247

LolD_lipo_ex

TIGR02211

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...

361-559

6.46e-22

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]

Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 94.34 E-value: 6.46e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL----ISVVFQDVWLFDD-TL 435
Cdd:TIGR02211  21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLrnkkLGFIYQFHHLLPDfTA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  436 LAN----LLIARpqatqQEVEEAARAAQclEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:TIGR02211 101 LENvampLLIGK-----KSVKEAKERAY--EMLEKV--GLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515713280  512 LDIDSELAVQKAIDHL--VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVE 559
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELnrELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221

LivF

COG0410

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

352-568

8.03e-22

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

Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 94.66 E-value: 8.03e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWL 430
Cdd:COG0410   12 GYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FDD-TLLANLLIARPQATQQEvEEAARAAQCLEFISRLpqgwltpmGEM----GGQLSGGERQRISIARALLKDAPIVIL 505
Cdd:COG0410   90 FPSlTVEENLLLGAYARRDRA-EVRADLERVYELFPRL--------KERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 506 DEPTAALdidSELAVQKAIDHLVH-NR---TVII----------IAHRlstiagagnILVMEEGEVVEQGTHAQLLS 568
Cdd:COG0410  161 DEPSLGL---APLIVEEIFEIIRRlNRegvTILLveqnarfaleIADR---------AYVLERGRIVLEGTAAELLA 225

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

344-552

8.56e-22

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 8.56e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:PRK10247   8 LQLQNVGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLANLLIarP-QATQQEVEEAARAAQCLEFisRLPQGWLT-PMGEmggqLSGGERQRISIARALLKDAP 501
Cdd:PRK10247  86 CAQTPTLFGDTVYDNLIF--PwQIRNQQPDPAIFLDDLERF--ALPDTILTkNIAE----LSGGEKQRISLIRNLQFMPK 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515713280 502 IVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAGAGNILVM 552
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

357-561

8.71e-22

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.60 E-value: 8.71e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQlnSLISVVFQDVWLFDD-TL 435
Cdd:PRK11607  31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmTV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 436 LANLLIARPQATQQEVEEAARAAQCL------EFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEPT 509
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLglvhmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPM 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 510 AALDIDSELAVQ-KAIDHLVH-NRTVIIIAH-RLSTIAGAGNILVMEEGEVVEQG 561
Cdd:PRK11607 178 GALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

344-562

9.34e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 9.34e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISV 423
Cdd:PRK13648   8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQD--------VWLFDDTL-LANLLIARPQaTQQEVEEAARAAQCLEFISRLPQGwltpmgemggqLSGGERQRISIAR 494
Cdd:PRK13648  88 VFQNpdnqfvgsIVKYDVAFgLENHAVPYDE-MHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHL--VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGT 562
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225

CFTR_protein

TIGR01271

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

357-576

1.51e-21

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: 99.60 E-value: 1.51e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEIsiggvdiRHltaeqlNSLISVVFQDVWLFDDTLL 436
Cdd:TIGR01271  438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------KH------SGRISFSPQTSWIMPGTIK 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   437 ANLLIARpQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDS 516
Cdd:TIGR01271  505 DNIIFGL-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280   517 ELAV-QKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQAL 576
Cdd:TIGR01271  584 EKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644

ABC_HisP_GlnQ

cd03262

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

360-557

1.82e-21

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: 92.98 E-value: 1.82e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI--RHLTAEQLNSLISVVFQDVWLFDD-TLL 436
Cdd:cd03262   15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIARPQATQQEVEEA-ARAAQCLEFISRLPQGWLTPmgemgGQLSGGERQRISIARALLKDAPIVILDEPTAALD-- 513
Cdd:cd03262   95 ENITLAPIKVKGMSKAEAeERALELLEKVGLADKADAYP-----AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpe 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515713280 514 -IDSELAVQKAIDHlvHNRTVIIIAHRLSTIAGAGN-ILVMEEGEV 557
Cdd:cd03262  170 lVGEVLDVMKDLAE--EGMTMVVVTHEMGFAREVADrVIFMDDGRI 213

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

360-563

3.33e-21

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 3.33e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG--VDIRHLTAE----QLNSLISVVFQDVWLFDD 433
Cdd:PRK11124  17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDkairELRRNVGMVFQQYNLWPH 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 434 -TLLANLL--------IARPQATQQEVEEAARAaQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVI 504
Cdd:PRK11124  97 lTVQQNLIeapcrvlgLSKDQALARAEKLLERL-RLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVLL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 505 LDEPTAALD---------IDSELAvQKAIdhlvhnrTVIIIAHRLStIAG--AGNILVMEEGEVVEQGTH 563
Cdd:PRK11124 165 FDEPTAALDpeitaqivsIIRELA-ETGI-------TQVIVTHEVE-VARktASRVVYMENGHIVEQGDA 225

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

360-574

4.08e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.53 E-value: 4.08e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSK-----LLMRYADPQQGEISIG------GVDIRHLT-----AEQLNSLISV 423
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGdkknnhELITNPYSkkiknFKELRRRVSM 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQ--DVWLFDDTLLANLLIArPQATQQEVEEAA-RAAQCLE-------FISRLPQGwltpmgemggqLSGGERQRISIA 493
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKkLAKFYLNkmglddsYLERSPFG-----------LSGGQKRRVAIA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 494 RALLKDAPIVILDEPTAALDIDSELAVQKAI-DHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLEVADeVIVMDKGKILKTGTPYEIFTDQH 268


                 ...
gi 515713280 572 RYQ 574
Cdd:PRK13631 269 IIN 271

cbiO

PRK13643

energy-coupling factor transporter ATPase;

344-562

4.79e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 4.79e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDS---GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQ---- 416
Cdd:PRK13643   2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 417 LNSLISVVFQ--DVWLFDDTLLANLLIArPQATQQEVEEAAR-AAQCLEFISRLPQGW-LTPMgemggQLSGGERQRISI 492
Cdd:PRK13643  82 VRKKVGVVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKiAAEKLEMVGLADEFWeKSPF-----ELSGGQMRRVAI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 493 ARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGT 562
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

376-562

9.71e-21

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: 93.33 E-value: 9.71e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  376 LVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEqlNSLISVVFQDVWLFDD-TLLANllIARPqATQQEVEEA 454
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHmTVEEN--VAFG-LKMRKVPRA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  455 ARAAQCLEFISrlpqgwLTPMGEMGG----QLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN 530
Cdd:TIGR01187  76 EIKPRVLEALR------LVQLEEFADrkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 515713280  531 R--TVIIIAHRLS-TIAGAGNILVMEEGEVVEQGT 562
Cdd:TIGR01187 150 LgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGT 184

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

359-561

1.10e-20

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: 91.24 E-value: 1.10e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVD-----IRHLtaeqlnSLISVVF---QDVWl 430
Cdd:cd03267   35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrKKFL------RRIGVVFgqkTQLW- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FD----DTLLANLLIAR--PQATQQEVEEAARAAQCLEFISrlpqgwlTPMGemggQLSGGERQRISIARALLKDAPIVI 504
Cdd:cd03267  108 WDlpviDSFYLLAAIYDlpPARFKKRLDELSELLDLEELLD-------TPVR----QLSLGQRMRAEIAAALLHEPEILF 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 505 LDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03267  177 LDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236

CysA

COG1118

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

359-569

1.15e-20

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 1.15e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLmryA---DPQQGEISIGGVDIR-HLTAEQLNslISVVFQDVWLFDD- 433
Cdd:COG1118   16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AgleTPDSGRIVLNGRDLFtNLPPRERR--VGFVFQHYALFPHm 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 434 TLLANLLIARPQATQQEVEEAARAAQCLEFI------SRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILDE 507
Cdd:COG1118   91 TVAENIAFGLRVRPPSKAEIRARVEELLELVqleglaDRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 508 PTAALDIdselAVQKAI-DHLVH-----NRTVIIIAH------RLstiagAGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:COG1118  160 PFGALDA----KVRKELrRWLRRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224

PLN03130

ABC transporter C family member; Provisional

294-576

1.26e-20

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 96.73 E-value: 1.26e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  294 IMRFsePMAMFISYTSVVELIASALQRIEQFM-----ALPPLPVAErgemPERYDIRFDTICYRYDDSGD-PALNNLSLT 367
Cdd:PLN03130  566 VLRF--PLFMLPNLITQAVNANVSLKRLEELLlaeerVLLPNPPLE----PGLPAISIKNGYFSWDSKAErPTLSNINLD 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  368 FPAASMSALVGASGAGKTT-VSKLLmryadpqqGEI---SIGGVDIRHLTAeqlnslisVVFQDVWLFDDTLLANLLIAR 443
Cdd:PLN03130  640 VPVGSLVAIVGSTGEGKTSlISAML--------GELpprSDASVVIRGTVA--------YVPQVSWIFNATVRDNILFGS 703

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  444 PqATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAV-QK 522
Cdd:PLN03130  704 P-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDK 782

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515713280  523 AIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQAL 576
Cdd:PLN03130  783 CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

357-569

1.53e-20

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: 93.25 E-value: 1.53e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  357 GDPALNnLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV---DIRH---LTAEQlnSLISVVFQDVWL 430
Cdd:TIGR02142  10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgifLPPEK--RRIGYVFQEARL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  431 FDD-TLLANLLI----ARPQATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVIL 505
Cdd:TIGR02142  87 FPHlSVRGNLRYgmkrARPSERRISFERVIELLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLM 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280  506 DEPTAALDIDSELAV----QKAIDHLvhNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:TIGR02142 156 DEPLAALDDPRKYEIlpylERLHAEF--GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222

ABCC_CFTR2

cd03289

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

352-574

1.64e-20

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: 91.84 E-value: 1.64e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADpQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLF 431
Cdd:cd03289   11 KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DDTLLANLliaRP--QATQQEVEEAARAAQCLEFISRLPqGWLTPMGEMGGQ-LSGGERQRISIARALLKDAPIVILDEP 508
Cdd:cd03289   90 SGTFRKNL---DPygKWSDEEIWKVAEEVGLKSVIEQFP-GQLDFVLVDGGCvLSHGHKQLMCLARSVLSKAKILLLDEP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 509 TAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQ 574
Cdd:cd03289  166 SAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFK 231

cbiO

PRK13644

energy-coupling factor transporter ATPase;

344-568

2.06e-20

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 2.06e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQ-LNSLIS 422
Cdd:PRK13644   2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 VVFQ--DVWLFDDTLLANL------LIARPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:PRK13644  81 IVFQnpETQFVGRTVEEDLafgpenLCLPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

344-561

4.59e-20

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.

Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.96 E-value: 4.59e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDP--ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSlI 421
Cdd:cd03266    2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 422 SVVFQDVWLFDD-TLLANLLI------ARPQATQQEVEEAARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIAR 494
Cdd:cd03266   81 GFVSDSTGLYDRlTARENLEYfaglygLKGDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIAR 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03266  150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218

livG

PRK11300

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional

360-566

5.02e-20

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 5.02e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLnSLISVV--FQDVWLFDD-TLL 436
Cdd:PRK11300  20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFREmTVI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIAR---------------PQATQQEVEEAARAAQCLEFISrlpqgwLTPMG-EMGGQLSGGERQRISIARALLKDA 500
Cdd:PRK11300  99 ENLLVAQhqqlktglfsgllktPAFRRAESEALDRAATWLERVG------LLEHAnRQAGNLAYGQQRRLEIARCMVTQP 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 501 PIVILDEPTAALDIDSELAVQKAIDHL--VHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQL 566
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGISDrIYVVNQGTPLANGTPEEI 241

CFTR_protein

TIGR01271

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

352-568

5.41e-20

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 94.98 E-value: 5.41e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   352 RYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADpQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLF 431
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   432 DDTLLANLlIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:TIGR01271 1305 SGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280   512 LDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440

PRK11264

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

357-568

5.75e-20

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.42 E-value: 5.75e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI---RHLTAEQ-----LNSLISVVFQDV 428
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WLFDD-TLLANLlIARPQATQQEVEEAARAaqclefisrLPQGWLTPMGEMGGQ------LSGGERQRISIARALLKDAP 501
Cdd:PRK11264  95 NLFPHrTVLENI-IEGPVIVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 502 IVILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVADrAIFMDQGRIVEQGPAKALFA 233

ModF

COG1119

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

344-567

6.19e-20

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: 89.37 E-value: 6.19e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQG-EISI-----GGVDIRHL----- 412
Cdd:COG1119    4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWELrkrig 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 413 -----TAEQLNSLISVvfQDVWL--FDDTllanllIARPQATQQevEEAARAAQCLEF--ISRLPQgwlTPMgemgGQLS 483
Cdd:COG1119   82 lvspaLQLRFPRDETV--LDVVLsgFFDS------IGLYREPTD--EQRERARELLELlgLAHLAD---RPF----GTLS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 484 GGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN--RTVIIIAHRLSTI-AGAGNILVMEEGEVVEQ 560
Cdd:COG1119  145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIpPGITHVLLLKDGRVVAA 224


                 ....*..
gi 515713280 561 GTHAQLL 567
Cdd:COG1119  225 GPKEEVL 231

PLN03232

ABC transporter C family member; Provisional

285-598

7.99e-20

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 94.27 E-value: 7.99e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  285 AFLIAAAAMIMRFsePMAMFISYTSVVELIASALQRIEQFM-----ALPPLPVAERGeMPErydIRFDTICYRYD-DSGD 358
Cdd:PLN03232  557 AFTSLSLFAVLRS--PLNMLPNLLSQVVNANVSLQRIEELLlseerILAQNPPLQPG-APA---ISIKNGYFSWDsKTSK 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  359 PALNNLSLTFPAASMSALVGASGAGKTT-VSKLLmryadpqqGEIS---IGGVDIRhltaeqlnSLISVVFQDVWLFDDT 434
Cdd:PLN03232  631 PTLSDINLEIPVGSLVAIVGGTGEGKTSlISAML--------GELShaeTSSVVIR--------GSVAYVPQVSWIFNAT 694

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  435 LLANLLIArpqaTQQEVEEAARA--AQCLEF-ISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:PLN03232  695 VRENILFG----SDFESERYWRAidVTALQHdLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  512 LdiDSELAVQ---KAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAqmAARVWRD 588
Cdd:PLN03232  771 L--DAHVAHQvfdSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN--AGKMDAT 846

                         330
                  ....*....|
gi 515713280  589 AEVDASEERL 598
Cdd:PLN03232  847 QEVNTNDENI 856

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

343-569

8.42e-20

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.08 E-value: 8.42e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDdSGDP----ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdiRHLTAE--- 415
Cdd:PRK13634   2 DITFQKVEHRYQ-YKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE---RVITAGkkn 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 416 -QLNSL---ISVVFQ--DVWLFDDTLLANLLIArPQATQQEVEEA-ARAAQCLEFISrLPQGWLT--PMgemggQLSGGE 486
Cdd:PRK13634  78 kKLKPLrkkVGIVFQfpEHQLFEETVEKDICFG-PMNFGVSEEDAkQKAREMIELVG-LPEELLArsPF-----ELSGGQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 487 RQRISIARALLKDAPIVILDEPTAALDIDS--ELAVQKAIDHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTH 563
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGrkEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230


                 ....*.
gi 515713280 564 AQLLSR 569
Cdd:PRK13634 231 REIFAD 236

ABC_ModC_molybdenum_transporter

cd03297

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

363-561

8.90e-20

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

Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 88.12 E-value: 8.90e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 363 NLSLTFPAaSMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV---DIR---HLTAEQLNslISVVFQDVWLFD---- 432
Cdd:cd03297   16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkkiNLPPQQRK--IGLVFQQYALFPhlnv 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 -DTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:cd03297   93 rENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLLDEPFSA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515713280 512 LDIDSELAVQKAID--HLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03297  162 LDRALRLQLLPELKqiKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214

PRK13633

energy-coupling factor transporter ATPase;

344-562

1.03e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 1.03e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD----PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDirhlTAEQLN- 418
Cdd:PRK13633   5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDEENl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 419 ----SLISVVFQDVwlfDDTLLA------------NLLIArPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQL 482
Cdd:PRK13633  81 wdirNKAGMVFQNP---DNQIVAtiveedvafgpeNLGIP-PEEIRERVDESLKKVGMYEYRRHAPH-----------LL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 483 SGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHL--VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQ 560
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225


                 ..
gi 515713280 561 GT 562
Cdd:PRK13633 226 GT 227

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

361-561

1.36e-19

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.

Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 87.71 E-value: 1.36e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ---QGEISIGGvdiRHLTAEQLNSLISVVFQDvwlfdDTLLA 437
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQD-----DILLP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NL---------LIARPQATQQEVEEAARAAqclefISRLPQGWLTPMGEMG-GQLSGGERQRISIARALLKDAPIVILDE 507
Cdd:cd03234   95 GLtvretltytAILRLPRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 508 PTAALDIDSELAVQKAIDHLVH-NRTVIIIAH-------RLSTiagagNILVMEEGEVVEQG 561
Cdd:cd03234  170 PTSGLDSFTALNLVSTLSQLARrNRIVILTIHqprsdlfRLFD-----RILLLSSGEIVYSG 226

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

365-599

1.38e-19

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis

Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 90.55 E-value: 1.38e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 365 SLTFPAASMSALVGASGAGKTTVSKL---LMRyadPQQGEISIGG---VDIRH---LTAEQLNslISVVFQDVWLFDD-T 434
Cdd:COG4148   19 DFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQDSARgifLPPHRRR--IGYVFQEARLFPHlS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 435 LLANLLIARPQATQQE-VEEAARAAQCLEfISRLpqgwltpMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALD 513
Cdd:COG4148   94 VRGNLLYGRKRAPRAErRISFDEVVELLG-IGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 514 IDSELAVQKAIDHLvHNRT---VIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSRQGRYQALWQAQMAARVwrDA 589
Cdd:COG4148  166 LARKAEILPYLERL-RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVL--EA 242

                        250
                 ....*....|
gi 515713280 590 EVDASEERLH 599
Cdd:COG4148  243 TVAAHDPDYG 252

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

360-569

1.45e-19

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 1.45e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIR---HLTAEQLNSLISVVFQDVW------- 429
Cdd:PRK11308  30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYgslnprk 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 430 ----LFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQgwltpMgemggqLSGGERQRISIARALLKDAPIVIL 505
Cdd:PRK11308 110 kvgqILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPH-----M------FSGGQRQRIAIARALMLDPDVVVA 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 506 DEPTAALDIdselAVQKAIDHLV------HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:PRK11308 179 DEPVSALDV----SVQAQVLNLMmdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245

cbiO

PRK13641

energy-coupling factor transporter ATPase;

344-570

1.53e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.12 E-value: 1.53e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdSGDP----ALNNLSLTFPAASMSALVGASGAGKTTvsklLMRYAD----PQQGEISIGGvdiRHLTAE 415
Cdd:PRK13641   3 IKFENVDYIYS-PGTPmekkGLDNISFELEEGSFVALVGHTGSGKST----LMQHFNallkPSSGTITIAG---YHITPE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 416 -------QLNSLISVVFQ--DVWLFDDTLLANLLIArPQ---ATQQEVEEAAraaqcLEFISRLpqGWLTPMGEMGG-QL 482
Cdd:PRK13641  75 tgnknlkKLRKKVSLVFQfpEAQLFENTVLKDVEFG-PKnfgFSEDEAKEKA-----LKWLKKV--GLSEDLISKSPfEL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 483 SGGERQRISIARALLKDAPIVILDEPTAALDIDSELAV-QKAIDHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQ 560
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKH 226

                        250
                 ....*....|
gi 515713280 561 GTHAQLLSRQ 570
Cdd:PRK13641 227 ASPKEIFSDK 236

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

359-568

2.51e-19

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 2.51e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWL-FDDTLLA 437
Cdd:PRK09536  17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLIARP----------QATQQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKDAPIVILDE 507
Cdd:PRK09536  97 VVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFADR-------PVTS----LSGGERQRVLLARALAQATPVLLLDE 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 508 PTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAGAGNILV-MEEGEVVEQGTHAQLLS 568
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVlLADGRVRAAGPPADVLT 228

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

361-558

3.86e-19

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 3.86e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL----ISVVFQDVwlfddTLL 436
Cdd:PRK10535  24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRY-----HLL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIARP---QATQQEVEEAARAAQCLEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALD 513
Cdd:PRK10535  99 SHLTAAQNvevPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515713280 514 IDSELAVQkAIDHLVHNR--TVIIIAHRLSTIAGAGNILVMEEGEVV 558
Cdd:PRK10535 177 SHSGEEVM-AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

360-561

3.91e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 3.91e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAdPQQGEISIGGVDIRHLTAEQL---NSLISVVFQDVwlfDDTLL 436
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSLN 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIarpqatQQEVEEAARAAQCLEFISRLPQGWLTPMGEMG----------GQLSGGERQRISIARALLKDAPIVILD 506
Cdd:PRK15134 377 PRLNV------LQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILD 450

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 507 EPTAALDidseLAVQKAIDHLV------HNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQG 561
Cdd:PRK15134 451 EPTSSLD----KTVQAQILALLkslqqkHQLAYLFISHDLHVVrALCHQVIVLRQGEVVEQG 508

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

348-569

5.12e-19

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 90.51 E-value: 5.12e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 348 TICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKT----TVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL--- 420
Cdd:COG4172   13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgn 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 -ISVVFQD--VWLfddtllaNLL------IARPQATQQEVEEAARAAQCLEFISR--LPQgwltPMGEMGG---QLSGGE 486
Cdd:COG4172   93 rIAMIFQEpmTSL-------NPLhtigkqIAEVLRLHRGLSGAAARARALELLERvgIPD----PERRLDAyphQLSGGQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 487 RQRISIARALLKDAPIVILDEPTAALDIdselAVQKAIDHLV------HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVE 559
Cdd:COG4172  162 RQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDLLkdlqreLGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237

                        250
                 ....*....|
gi 515713280 560 QGTHAQLLSR 569
Cdd:COG4172  238 QGPTAELFAA 247

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

349-569

5.94e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 5.94e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDDSGDpALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQ-- 426
Cdd:PRK13652   9 LCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 DVWLFDDTLLANL------LIARPQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDA 500
Cdd:PRK13652  88 DDQIFSPTVEQDIafgpinLGLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 501 PIVILDEPTAALDidsELAVQKAIDHL-----VHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:PRK13652 157 QVLVLDEPTAGLD---PQGVKELIDFLndlpeTYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228

PTZ00243

ABC transporter; Provisional

346-579

6.43e-19

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 91.38 E-value: 6.43e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  346 FDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVF 425
Cdd:PTZ00243 1311 FEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  426 QDVWLFDDTLLANLliaRP--QATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLK-DAPI 502
Cdd:PTZ00243 1391 QDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGF 1467

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280  503 VILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQL-LSRQGRYQALWQA 579
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEA 1545

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

361-569

9.20e-19

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 9.20e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMR----YADPQ-QGEISIGGVDIRHLTAEQLNSLISVVFQ------DVW 429
Cdd:PRK14247  19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpipNLS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 430 LFDDTLLA---NLLIARPQATQQEVEEAARAAQCLEFI-SRLpqgwltpmGEMGGQLSGGERQRISIARALLKDAPIVIL 505
Cdd:PRK14247  99 IFENVALGlklNRLVKSKKELQERVRWALEKAQLWDEVkDRL--------DAPAGKLSGGQQQRLCIARALAFQPEVLLA 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 506 DEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLSR 569
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWGPTREVFTN 235

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

340-570

9.81e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 9.81e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 340 ERYDIRFDTICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG--VDIRHLTAEQL 417
Cdd:PRK13636   2 EDYILKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 418 NSLISVVFQD-------VWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLtpmgemggqlSGGERQRI 490
Cdd:PRK13636  81 RESVGMVFQDpdnqlfsASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL----------SFGQKKRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAHRLSTIA-GAGNILVMEEGEVVEQGTHAQLL 567
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230


                 ...
gi 515713280 568 SRQ 570
Cdd:PRK13636 231 AEK 233

PTZ00243

ABC transporter; Provisional

361-598

1.03e-18

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 90.61 E-value: 1.03e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMryadpQQGEISIGGVdirhlTAEQLnslISVVFQDVWLFDDTLLANLL 440
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL-----SQFEISEGRV-----WAERS---IAYVPQQAWIMNATVRGNIL 742

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  441 IARPQATQQeVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDID-SELA 519
Cdd:PTZ00243  743 FFDEEDAAR-LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERV 821

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280  520 VQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLsRQGRYQALWQAQMAARVWRDAEVDASEERL 598
Cdd:PTZ00243  822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAAELKENKDSKEGDADAEVAEV 899

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

361-570

1.82e-18

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 1.82e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISVVFQDVWLFDD-TLLANL 439
Cdd:PRK11432  22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--ICMVFQSYALFPHmSLGENV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 -----LIARPQA-TQQEVEEAaraaqcLEFISrlpqgwLTPMGE-MGGQLSGGERQRISIARAL-LKdaPIVIL-DEPTA 510
Cdd:PRK11432 100 gyglkMLGVPKEeRKQRVKEA------LELVD------LAGFEDrYVDQISGGQQQRVALARALiLK--PKVLLfDEPLS 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 511 ALDIDSELAVQKAIDHLVH--NRTVIIIAHRLS-TIAGAGNILVMEEGEVVEQGThAQLLSRQ 570
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGS-PQELYRQ 227

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

344-570

1.96e-18

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 1.96e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdsgdpalnNLSLTFP----AASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQlnS 419
Cdd:PRK10771   2 LKLTDITWLYH--------HLPMRFDltveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--R 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 420 LISVVFQDVWLFddtllANLLIA-----------RPQATQQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGER 487
Cdd:PRK10771  72 PVSMLFQENNLF-----SHLTVAqniglglnpglKLNAAQREkLHAIARQMGIEDLLARLP-----------GQLSGGQR 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 488 QRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHA 564
Cdd:PRK10771 136 QRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTD 215


                 ....*.
gi 515713280 565 QLLSRQ 570
Cdd:PRK10771 216 ELLSGK 221

PRK10575

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

361-567

1.98e-18

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 1.98e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLL 440
Cdd:PRK10575  27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 441 -IAR----------PQATQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEPT 509
Cdd:PRK10575 107 aIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 510 AALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIAGAGNILV-MEEGEVVEQGTHAQLL 567
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAELM 236

cbiO

PRK13637

energy-coupling factor transporter ATPase;

360-565

3.19e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.48 E-value: 3.19e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI--RHLTAEQLNSLISVVFQ--DVWLFDDTL 435
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypEYQLFEETI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 436 -------LANLLIarpqaTQQEVEEAARAAQCLEFISRLPQGWLTPMgemggQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:PRK13637 102 ekdiafgPINLGL-----SEEEIENRVKRAMNIVGLDYEDYKDKSPF-----ELSGGQKRRVAIAGVVAMEPKILILDEP 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 509 TAALDI---DSELAVQKAIdHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQ 565
Cdd:PRK13637 172 TAGLDPkgrDEILNKIKEL-HKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231

PRK10070

proline/glycine betaine ABC transporter ATP-binding protein ProV;

360-568

3.90e-18

proline/glycine betaine ABC transporter ATP-binding protein ProV;

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.01 E-value: 3.90e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL----ISVVFQDVWL----- 430
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALmphmt 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 -FDDTLLANLLIARPQATQQE-VEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:PRK10070 123 vLDNTAFGMELAGINAEERREkALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 509 TAALD--IDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK10070 192 FSALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDrIAIMQNGEVVQVGTPDEILN 254

cbiO

PRK13650

energy-coupling factor transporter ATPase;

351-576

4.40e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 4.40e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 351 YRYD-DSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdiRHLTAE---QLNSLISVVFQ 426
Cdd:PRK13650  12 FKYKeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEEnvwDIRHKIGMVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 D-------VWLFDDTL--LANLLIARpQATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALL 497
Cdd:PRK13650  89 NpdnqfvgATVEDDVAfgLENKGIPH-EEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQGRYQA 575
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRddYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQ 236


                 .
gi 515713280 576 L 576
Cdd:PRK13650 237 L 237

cbiO

PRK13645

energy-coupling factor transporter ATPase;

343-570

4.76e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 4.76e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGD---PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI-----RHLTA 414
Cdd:PRK13645   6 DIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 415 EQLNSLISVVFQ--DVWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISrLPQGWL--TPMgemggQLSGGERQRI 490
Cdd:PRK13645  86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDYVkrSPF-----ELSGGQKRRV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN--RTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLL 567
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239


                 ...
gi 515713280 568 SRQ 570
Cdd:PRK13645 240 SNQ 242

PhnK

COG1101

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

360-558

5.21e-18

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.98 E-value: 5.21e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTT----VSKLLMryadPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWL---FD 432
Cdd:COG1101   21 ALDGLNLTIEEGDFVTVIGSNGAGKSTllnaIAGSLP----PDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 DTLLANLLIA---------RPQATQQEVEEAAraaqclEFISRLPQGwL-----TPMGemggQLSGGERQRISIARALLK 498
Cdd:COG1101   97 MTIEENLALAyrrgkrrglRRGLTKKRRELFR------ELLATLGLG-LenrldTKVG----LLSGGQRQALSLLMATLT 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 499 DAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTIAGAGN-ILVMEEGEVV 558
Cdd:COG1101  166 KPKLLLLDEHTAALDPKTAALVLELTEKIVeeNNLTTLMVTHNMEQALDYGNrLIMMHEGRII 228

PRK15056

manganese/iron ABC transporter ATP-binding protein;

348-561

6.57e-18

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 6.57e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 348 TICYRyddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQD 427
Cdd:PRK15056  13 TVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 VWLF----DDTLLANL-----LIARPQATQQEVEEAARA-AQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARALL 497
Cdd:PRK15056  90 DWSFpvlvEDVVMMGRyghmgWLRRAKKRDRQIVTAALArVDMVEFRHR-----------QIGELSGGQKKRVFLARAIA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQG 561
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

343-568

7.35e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 7.35e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGK--TTVSKLLMRYADP---QQGEISIGGVDIRHLTAEQL 417
Cdd:PRK15134   7 AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKsvTALSILRLLPSPPvvyPSGDIRFHGESLLHASEQTL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 418 NSL----ISVVFQD--VWL-----FDDTLLANLLIARPQATqqeveEAARAA--QCLEFIS-RLPQGWLTpmgEMGGQLS 483
Cdd:PRK15134  87 RGVrgnkIAMIFQEpmVSLnplhtLEKQLYEVLSLHRGMRR-----EAARGEilNCLDRVGiRQAAKRLT---DYPHQLS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 484 GGERQRISIARALLKDAPIVILDEPTAALDIdselAVQKAIDHLVH------NRTVIIIAHRLSTIAG-AGNILVMEEGE 556
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDV----SVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGR 234

                        250
                 ....*....|..
gi 515713280 557 VVEQGTHAQLLS 568
Cdd:PRK15134 235 CVEQNRAATLFS 246

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

361-568

8.55e-18

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 8.55e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGV------DIRHLTAEQLNSLISVVFQD------V 428
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQpnpfphL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WLFDDTL--LANLLIARPQATQQEVEEAARAAQCL-EFISRLpqgwltpmGEMGGQLSGGERQRISIARALLKDAPIVIL 505
Cdd:PRK14246 106 SIYDNIAypLKSHGIKEKREIKKIVEECLRKVGLWkEVYDRL--------NSPASQLSGGQQQRLTIARALALKPKVLLM 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 506 DEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIFT 241

ABC_BcrA_bacitracin_resist

cd03268

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

359-561

9.22e-18

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.

Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 82.26 E-value: 9.22e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTA--EQLNSLIsvvfqDVWLFDDTLL 436
Cdd:cd03268   14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalRRIGALI-----EAPGFYPNLT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 A--NLLIArpqATQQEVEEAaRAAQCLEFISrlpqgwltpMGEMG----GQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:cd03268   89 AreNLRLL---ARLLGIRKK-RIDEVLDVVG---------LKDSAkkkvKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515713280 511 ALDIDSELAVQKAI-DHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQG 561
Cdd:cd03268  156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208

SapF

COG4167

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];

360-568

1.12e-17

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.35 E-value: 1.12e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVwlfDDTLLANL 439
Cdd:COG4167   28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIAR----P--QATQ-QEVEEAARAAQCLEFISRLPQGWLTP--MgemggqLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:COG4167  105 NIGQileePlrLNTDlTAEEREERIFATLRLVGLLPEHANFYphM------LSSGQKQRVALARALILQPKIIIADEALA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 511 ALDIdselAVQKAIDHLV------HNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:COG4167  179 ALDM----SVRSQIINLMlelqekLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFA 239

cbiO

PRK13649

energy-coupling factor transporter ATPase;

344-566

1.21e-17

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 1.21e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdSGDP----ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTA----E 415
Cdd:PRK13649   3 INLQNVSYTYQ-AGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 416 QLNSLISVVFQ--DVWLFDDTLLANLLIArPQ---ATQQEVEEAARAAQCL-----EFISRLPqgwltpmgemgGQLSGG 485
Cdd:PRK13649  82 QIRKKVGLVFQfpESQLFEETVLKDVAFG-PQnfgVSQEEAEALAREKLALvgiseSLFEKNP-----------FELSGG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 486 ERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTH 563
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229


                 ...
gi 515713280 564 AQL 566
Cdd:PRK13649 230 KDI 232

TauB

COG4525

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

352-513

1.22e-17

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.99 E-value: 1.22e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSGD--PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQlnsliSVVFQDvw 429
Cdd:COG4525   12 RYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-----GVVFQK-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 430 lfdDTLLANLLIARPQA---TQQEVEEAARAAQCLEFISrlpqgwLTPMGEMGG----QLSGGERQRISIARALLKDAPI 502
Cdd:COG4525   85 ---DALLPWLNVLDNVAfglRLRGVPKAERRARAEELLA------LVGLADFARrriwQLSGGMRQRVGIARALAADPRF 155

                        170
                 ....*....|.
gi 515713280 503 VILDEPTAALD 513
Cdd:COG4525  156 LLMDEPFGALD 166

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

359-567

1.33e-17

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: 82.21 E-value: 1.33e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLFDD-TLL 436
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKlTVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIARPQATQQEVEEAARAAQCL-EF-ISRLPQgwltpmgEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDI 514
Cdd:cd03218   94 ENILAVLEIRGLSKKEREEKLEELLeEFhITHLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 515 DSELAVQKAIDHLV----------HN-RTVIIIAHRlstiagagnILVMEEGEVVEQGTHAQLL 567
Cdd:cd03218  167 IAVQDIQKIIKILKdrgigvlitdHNvRETLSITDR---------AYIIYEGKVLAEGTPEEIA 221

PstB

COG1117

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

360-561

1.48e-17

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.78 E-value: 1.48e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAD--PQQ---GEISIGGVDI--RHLTAEQLNSLISVVFQdvwlfd 432
Cdd:COG1117   26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQ------ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 dtlLANLL-------IA--------RPQATQQE-VEEAARAAQcL--EFISRLpqgwltpmGEMGGQLSGGERQRISIAR 494
Cdd:COG1117  100 ---KPNPFpksiydnVAyglrlhgiKSKSELDEiVEESLRKAA-LwdEVKDRL--------KKSALGLSGGQQQRLCIAR 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 495 AL-LKdaPIVIL-DEPTAALDIDSELAVQKAIDHLVHNRTVIIIAH------RLSTiagagNILVMEEGEVVEQG 561
Cdd:COG1117  168 ALaVE--PEVLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVSD-----YTAFFYLGELVEFG 235

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

344-562

1.87e-17

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 1.87e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDP--ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL- 420
Cdd:PRK11153   2 IELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 --ISVVFQDVWL------FDDTLLANLLIARPQAtqqevEEAARAAQCLEFI------SRLPqgwltpmgemgGQLSGGE 486
Cdd:PRK11153  82 rqIGMIFQHFNLlssrtvFDNVALPLELAGTPKA-----EIKARVTELLELVglsdkaDRYP-----------AQLSGGQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 487 RQRISIARALLKDaPIVIL-DEPTAALD---IDSELAVQKAIdhlvhNR----TVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:PRK11153 146 KQRVAIARALASN-PKVLLcDEATSALDpatTRSILELLKDI-----NRelglTIVLITHEMDVVKRiCDRVAVIDAGRL 219


                 ....*
gi 515713280 558 VEQGT 562
Cdd:PRK11153 220 VEQGT 224

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

344-559

2.40e-17

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: 81.33 E-value: 2.40e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDP--ALNNLSLTFPAASMSALVGASGAGKTTvskLLMRYA---DPQQGEISIGGVDIRHLTAEQL- 417
Cdd:COG4181    9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKST---LLGLLAgldRPTSGTVRLAGQDLFALDEDARa 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 418 ---NSLISVVFQDvwlFddTLLANL-----------LIARPQAtqqeveeAARAAQCLEfisrlpqgwltpmgEMG---- 479
Cdd:COG4181   86 rlrARHVGFVFQS---F--QLLPTLtalenvmlpleLAGRRDA-------RARARALLE--------------RVGlghr 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 -----GQLSGGERQRISIARALLKDAPIVILDEPTAALD-------IDSELAVQKAidhlvHNRTVIIIAHRLSTIAGAG 547
Cdd:COG4181  140 ldhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDaatgeqiIDLLFELNRE-----RGTTLVLVTHDPALAARCD 214

                        250
                 ....*....|..
gi 515713280 548 NILVMEEGEVVE 559
Cdd:COG4181  215 RVLRLRAGRLVE 226

cbiO

PRK13642

energy-coupling factor transporter ATPase;

344-568

2.79e-17

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 2.79e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGD-PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdiRHLTAEQLNSL-- 420
Cdd:PRK13642   5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLrr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 -ISVVFQD-------VWLFDDTL--LANLLIARPQATQQeVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:PRK13642  82 kIGMVFQNpdnqfvgATVEDDVAfgMENQGIPREEMIKR-VDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHL--VHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

360-566

2.95e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 2.95e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQL---NSLISVVFQDVwlfddtlL 436
Cdd:PRK15079  36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-------L 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANL--------LIA------RPQATQQEVEEAARAAQCL-----EFISRLPQgwltpmgemggQLSGGERQRISIARALL 497
Cdd:PRK15079 109 ASLnprmtigeIIAeplrtyHPKLSRQEVKDRVKAMMLKvgllpNLINRYPH-----------EFSGGQCQRIGIARALI 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 498 KDAPIVILDEPTAALDIdselAVQKAIDHLVHN------RTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQL 566
Cdd:PRK15079 178 LEPKLIICDEPVSALDV----SIQAQVVNLLQQlqremgLSLIFIAHDLAVVKHISDrVLVMYLGHAVELGTYDEV 249

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

359-520

4.53e-17

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: 80.56 E-value: 4.53e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISI----GGVDIRHLTAEQLNSL----ISVVFQ---- 426
Cdd:COG4778   25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREILALrrrtIGYVSQflrv 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 -------DVwlfddtllanllIARPQATQQEVEEAA--RAAQCLEFIsRLPQG-W-LTPmgemgGQLSGGERQRISIARA 495
Cdd:COG4778  105 iprvsalDV------------VAEPLLERGVDREEAraRARELLARL-NLPERlWdLPP-----ATFSGGEQQRVNIARG 166

                        170       180
                 ....*....|....*....|....*
gi 515713280 496 LLKDAPIVILDEPTAALDIDSELAV 520
Cdd:COG4778  167 FIADPPLLLLDEPTASLDAANRAVV 191

BtuD

COG4138

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...

361-568

6.13e-17

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 6.13e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTvskLLMRYAD--PQQGEISIGGVDIRHLTAEQLNSLISVVFQ--------DVWL 430
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAYLSQqqsppfamPVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FddtlLAnlLIARPQATQQEVEEA-ARAAQCLEFISRLPQgwltpmgeMGGQLSGGERQRISIARALLK-------DAPI 502
Cdd:COG4138   89 Y----LA--LHQPAGASSEAVEQLlAQLAEALGLEDKLSR--------PLTQLSGGEWQRVRLAAVLLQvwptinpEGQL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLS-TIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:COG4138  155 LLLDEPMNSLDVAQQAALDRLLRELCQqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222

cbiO

TIGR01166

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...

357-537

6.77e-17

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 79.00 E-value: 6.77e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  357 GDP-ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRH----LTAeqLNSLISVVFQDVwlf 431
Cdd:TIGR01166   3 GGPeVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYsrkgLLE--RRQRVGLVFQDP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  432 DDTLLA------------NLLIARPQATQQeVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKD 499
Cdd:TIGR01166  78 DDQLFAadvdqdvafgplNLGLSEAEVERR-VREALTAVGASGLRERPTH-----------CLSGGEKKRVAIAGAVAMR 145

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 515713280  500 APIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIA 537
Cdd:TIGR01166 146 PDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

357-554

1.02e-16

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.06 E-value: 1.02e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ---QGEISIGGVDIRHLTAEQLNslISVVFQDVWLFDD 433
Cdd:COG4136   13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--IGILFQDDLLFPH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 434 -TLLANLLIARPQATQQEvEEAARAAQCLEFISrlpqgwLTPMGE-MGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:COG4136   91 lSVGENLAFALPPTIGRA-QRRARVEQALEEAG------LAGFADrDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515713280 512 LDID-----SELAVQKAIDhlvHNRTVIIIAHRLSTIAGAGNILVMEE 554
Cdd:COG4136  164 LDAAlraqfREFVFEQIRQ---RGIPALLVTHDEEDAPAAGRVLDLGN 208

PRK14243

phosphate transporter ATP-binding protein; Provisional

360-572

1.30e-16

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 1.30e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAD-----PQQGEISIGGVDI--RHLTAEQLNSLISVVFQDVWLFD 432
Cdd:PRK14243  25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 DTLLANLLI-ARPQATQQE----VEEAAR-AAQCLEFISRLPQGwltpmgemGGQLSGGERQRISIARALLKDAPIVILD 506
Cdd:PRK14243 105 KSIYDNIAYgARINGYKGDmdelVERSLRqAALWDEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMD 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 507 EPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGThaqllsRQGR 572
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG------RYGY 236

PRK14239

phosphate transporter ATP-binding protein; Provisional

360-540

1.52e-16

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.82 E-value: 1.52e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAD--PQ---QGEISIGGVDIRHLTAE--QLNSLISVVFQDVWLFD 432
Cdd:PRK14239  20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 DTLLANLL-------IARPQATQQEVEEAARAAQCL-EFISRLPQGWLTpmgemggqLSGGERQRISIARALLKDAPIVI 504
Cdd:PRK14239 100 MSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIWdEVKDRLHDSALG--------LSGGQQQRVCIARVLATSPKIIL 171

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515713280 505 LDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRL 540
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

353-566

1.53e-16

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: 79.11 E-value: 1.53e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  353 YDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLF 431
Cdd:TIGR03410  10 YGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  432 DD-TLLANLLI---ARPQATQQEVEEA-ARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARALLKDAPIVILD 506
Cdd:TIGR03410  88 PRlTVEENLLTglaALPRRSRKIPDEIyELFPVLKEMLGR-----------RGGDLSGGQQQQLAIARALVTRPKLLLLD 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280  507 EPTAAL------DIdselavQKAIDHLVHNR--TVIIIAHRLS-TIAGAGNILVMEEGEVVEQGTHAQL 566
Cdd:TIGR03410 157 EPTEGIqpsiikDI------GRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

356-566

1.68e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 1.68e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 356 SGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLFDD- 433
Cdd:PRK15439  22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 434 TLLANLL--IARPQATQQEVEEAARAAQC-LEFISRlpqgwltpmgemGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:PRK15439 102 SVKENILfgLPKRQASMQKMKQLLAALGCqLDLDSS------------AGSLEVADRQIVEILRGLMRDSRILILDEPTA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 511 ALD-IDSELAVQKAIDHLVHNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQL 566
Cdd:PRK15439 170 SLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

361-568

1.95e-16

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 1.95e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQDV--------- 428
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdIQMVFQDSisavnprkt 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 --WLFDDTL--LANLLIARPQATQQEVEEAARAAqcLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVI 504
Cdd:PRK10419 108 vrEIIREPLrhLLSLDKAERLARASEMLRAVDLD--DSVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLI 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 505 LDEPTAALDIDSELAVQKAIDHLVHNRTV--IIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

360-562

1.98e-16

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.54 E-value: 1.98e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ---QGEISIGGVDIRHLTAEQLNSL----ISVVFQD----- 427
Cdd:PRK09473  31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLraeqISMIFQDpmtsl 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 --VWLFDDTLLANLLIARPQATQQEVEEAAR---AAQCLEFISRlpqgwltpMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:PRK09473 111 npYMRVGEQLMEVLMLHKGMSKAEAFEESVRmldAVKMPEARKR--------MKMYPHEFSGGMRQRVMIAMALLCRPKL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 503 VILDEPTAALDIdselAVQKAIDHLVH------NRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGT 562
Cdd:PRK09473 183 LIADEPTTALDV----TVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245

YddA

COG4178

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

280-555

2.04e-16

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 2.04e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 280 GTLNLAFLIAAAAMIMRFSEPMAMFI-SYTSVVELIASaLQRIEQFM----ALPPLPVAERGEMPERYD-IRFD--TIcy 351
Cdd:COG4178  294 GEITLGGLMQAASAFGQVQGALSWFVdNYQSLAEWRAT-VDRLAGFEealeAADALPEAASRIETSEDGaLALEdlTL-- 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 rYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTvsklLMR-------YAdpqQGEIsiggvdirhltaeQLNSLISVV 424
Cdd:COG4178  371 -RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRaiaglwpYG---SGRI-------------ARPAGARVL 429

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 425 F--QDVWLFDDTLLANLliARPQA----TQQEVEEAARAAQCLEFISRL--PQGWltpmgemGGQLSGGERQRISIARAL 496
Cdd:COG4178  430 FlpQRPYLPLGTLREAL--LYPATaeafSDAELREALEAVGLGHLAERLdeEADW-------DQVLSLGEQQRLAFARLL 500

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 497 LKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEG 555
Cdd:COG4178  501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

357-561

2.36e-16

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 2.36e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNnLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG---VDIR---HLTAEQLNslISVVFQDVWL 430
Cdd:PRK11144  11 GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEkgiCLPPEKRR--IGYVFQDARL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FDD-TLLANLLIARPQATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILDEPT 509
Cdd:PRK11144  88 FPHyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 510 AALDID---------SELA--VQKAIDHLVHNRTVIIiahRLstiagAGNILVMEEGEVVEQG 561
Cdd:PRK11144 157 ASLDLPrkrellpylERLAreINIPILYVSHSLDEIL---RL-----ADRVVVLEQGKVKAFG 211

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

356-568

2.55e-16

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 2.55e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 356 SGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADP-----QQGEISIGGVDI-RHLTAEQLNSLISVVFQDVW 429
Cdd:PRK14271  32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 430 LFDDTLLANLLI---ARPQATQQEVEEAARAaqclefisRLPQGWL-----TPMGEMGGQLSGGERQRISIARALLKDAP 501
Cdd:PRK14271 112 PFPMSIMDNVLAgvrAHKLVPRKEFRGVAQA--------RLTEVGLwdavkDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 502 IVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDrAALFFDGRLVEEGPTEQLFS 251

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

360-558

2.60e-16

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 2.60e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG--VDIRHlTAEQLNSLISVVFQDVWLFDD-TLL 436
Cdd:COG3845   20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-PRDAIALGIGMVHQHFMLVPNlTVA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIARPQATQQEVEEAARAAQCLEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAAL---D 513
Cdd:COG3845   99 ENIVLGLEPTKGGRLDRKAARARIRELSERY--GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqE 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515713280 514 IDSELAVqkaIDHLVHN-RTVIIIAHRLSTI-AGAGNILVMEEGEVV 558
Cdd:COG3845  177 ADELFEI---LRRLAAEgKSIIFITHKLREVmAIADRVTVLRRGKVV 220

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

349-568

2.92e-16

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 2.92e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDDsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLN--SLISVVFQ 426
Cdd:PRK13639   7 LKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTVGIVFQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 DVwlfDDTLLA------------NLLIARPQaTQQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:PRK13639  86 NP---DDQLFAptveedvafgplNLGLSKEE-VEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 495 ALLKDAPIVILDEPTAALDIDSELAVQKAIDHLvhNR---TVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226

PRK10908

cell division ATP-binding protein FtsE;

344-513

3.60e-16

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 3.60e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDdSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQ---LNSL 420
Cdd:PRK10908   2 IRFEHVSKAYL-GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDV-WLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLPQGWLTPMgemggQLSGGERQRISIARALLKD 499
Cdd:PRK10908  81 IGMIFQDHhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNK 155

                        170
                 ....*....|....
gi 515713280 500 APIVILDEPTAALD 513
Cdd:PRK10908 156 PAVLLADEPTGNLD 169

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

360-561

5.05e-16

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 5.05e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLT---AEQLNslISVVFQDVWLFDD-TL 435
Cdd:PRK09700  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLG--IGIIYQELSVIDElTV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 436 LANLLIAR---------PQATQQEVEEaaRAAQCLefisrLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILD 506
Cdd:PRK09700  98 LENLYIGRhltkkvcgvNIIDWREMRV--RAAMML-----LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 507 EPTAALdidselaVQKAIDHLV--------HNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQG 561
Cdd:PRK09700 171 EPTSSL-------TNKEVDYLFlimnqlrkEGTAIVYISHKLAEIRRICDrYTVMKDGSSVCSG 227

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

353-562

5.73e-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: 81.98 E-value: 5.73e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   353 YDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIrHLTAEQLNSLISVVFQDVWLFD 432
Cdd:TIGR01257  938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFH 1016

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   433 DTLLANLLIARPQATQQEVEEAAraaqcLEFISRLPQ-GWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGRSWEEAQ-----LEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 515713280   512 LDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGT 562
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDrIAIISQGRLYCSGT 1143

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

302-568

5.82e-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: 81.00 E-value: 5.82e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  302 AMFISYTSVVElIASALQRIEQFMALPPLPVAERGEMPERYDIRFDTICYRY---DDSGDPALNNLSLTFPAASMSALVG 378
Cdd:TIGR03269 239 AIWLENGEIKE-EGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVG 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  379 ASGAGKTTVSKLLMRYADPQQGEIS--IG---------GVDIRHltaeQLNSLISVVFQDVWLF-DDTLLANLL------ 440
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTSGEVNvrVGdewvdmtkpGPDGRG----RAKRYIGILHQEYDLYpHRTVLDNLTeaigle 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  441 ----IARPQA--TQQEV---EEAARaaqclEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:TIGR03269 394 lpdeLARMKAviTLKMVgfdEEKAE-----EILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVILDEPTGT 457

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  512 LDIDSELAVQKAIDHLVH--NRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLS 568
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDrAALMRDGKIVKIGDPEEIVE 517

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

361-513

6.24e-16

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.36 E-value: 6.24e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNslISVVFQDVWLFDD-TLLANl 439
Cdd:PRK10851  18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDN- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 lIA----------RPQ--ATQQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVILDE 507
Cdd:PRK10851  95 -IAfgltvlprreRPNaaAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162


                 ....*.
gi 515713280 508 PTAALD 513
Cdd:PRK10851 163 PFGALD 168

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

349-513

6.72e-16

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 6.72e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQlnsliSVVFQDV 428
Cdd:PRK11248   7 LYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WLFD-DTLLANLLIARPQATQQEVEEAARAAQCL------EFISRLPqgWltpmgemggQLSGGERQRISIARALLKDAP 501
Cdd:PRK11248  80 GLLPwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLkkvgleGAEKRYI--W---------QLSGGQRQRVGIARALAANPQ 148

                        170
                 ....*....|..
gi 515713280 502 IVILDEPTAALD 513
Cdd:PRK11248 149 LLLLDEPFGALD 160

Uup

COG0488

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

344-559

8.14e-16

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 8.14e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIG-GVDIRHLT--AEQLNSl 420
Cdd:COG0488  316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIGYFDqhQEELDP- 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 isvvfqdvwlfDDTLLANLLIARPQATQQEVeeaaRAaqcleFISRL---PQGWLTPMGEmggqLSGGERQRISIARALL 497
Cdd:COG0488  393 -----------DKTVLDELRDGAPGGTEQEV----RG-----YLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHlvHNRTVIIIAH-R--LSTIagAGNILVMEEGEVVE 559
Cdd:COG0488  449 SPPNVLLLDEPTNHLDIETLEALEEALDD--FPGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

363-568

9.24e-16

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 9.24e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 363 NLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLlIA 442
Cdd:PRK10253  25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL-VA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 443 RPQATQQ--------EVEEAARAAQCLEFISRLPqgwltpmGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDI 514
Cdd:PRK10253 104 RGRYPHQplftrwrkEDEEAVTKAMQATGITHLA-------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 515 DSELAVQKAIDHLvhNR----TVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK10253 177 SHQIDLLELLSEL--NRekgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVT 233

Uup

COG0488

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

349-538

1.02e-15

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.02e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 349 ICYRYDdsGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISI-GGVDIRHLTAEQL----NSLISV 423
Cdd:COG0488    4 LSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLPQEPPldddLTVLDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDDTLLA-NLLIARPQATQQEVEEAARAAQCLEFI-------------SRL---PQGWLTPMGEmggqLSGGE 486
Cdd:COG0488   82 VLDGDAELRALEAElEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilSGLgfpEEDLDRPVSE----LSGGW 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 487 RQRISIARALLKDAPIVILDEPTAALDIDS----ElavqkaiDHLVHNR-TVIIIAH 538
Cdd:COG0488  158 RRRVALARALLSEPDLLLLDEPTNHLDLESiewlE-------EFLKNYPgTVLVVSH 207

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

344-569

1.32e-15

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.67 E-value: 1.32e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIR--HLTAEQLNSLI 421
Cdd:PRK09493   2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 422 SVVFQDVWLFDD-TLLANLLIArPQATQQEVEEAARAaQCLEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKDA 500
Cdd:PRK09493  80 GMVFQQFYLFPHlTALENVMFG-PLRVRGASKEEAEK-QARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 501 PIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAGAGNILV-MEEGEVVEQGTHAQLLSR 569
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKN 226

PRK10261

glutathione transporter ATP-binding protein; Provisional

360-561

1.35e-15

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.35e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQDVWL-FDDTL 435
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPYAsLDPRQ 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 436 LANLLIARP---QATQQEVEEAARAAQCLEFISRLPQ-GWLTPMgemggQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:PRK10261 419 TVGDSIMEPlrvHGLLPGKAAAARVAWLLERVGLLPEhAWRYPH-----EFSGGQRQRICIARALALNPKVIIADEAVSA 493

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 512 LD-------IDSELAVQK----AIDHLVHNRTVI-IIAHRLStiagagnilVMEEGEVVEQG 561
Cdd:PRK10261 494 LDvsirgqiINLLLDLQRdfgiAYLFISHDMAVVeRISHRVA---------VMYLGQIVEIG 546

PRK10261

glutathione transporter ATP-binding protein; Provisional

348-566

1.51e-15

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 1.51e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 348 TICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG----------VDIRHLTAEQL 417
Cdd:PRK10261  19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 418 NSL----ISVVFQD-VWLFDDTLLANLLIARPQATQQEV--EEAARAAQCLEFISRLPQGWlTPMGEMGGQLSGGERQRI 490
Cdd:PRK10261  99 RHVrgadMAMIFQEpMTSLNPVFTVGEQIAESIRLHQGAsrEEAMVEAKRMLDQVRIPEAQ-TILSRYPHQLSGGMRQRV 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 491 SIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRT--VIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQL 566
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

345-543

2.00e-15

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.00e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 345 RFDTICYRYddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHL-TAEQLNSLISV 423
Cdd:PRK11288   6 SFDGIGKTF--PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsTTAALAAGVAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQDVWLFDD-TLLANLLIARPQATQQEVEEAARAAQCLEFISRL-----PQgwlTPMGEmggqLSGGERQRISIARALL 497
Cdd:PRK11288  84 IYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQMVEIAKALA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515713280 498 KDAPIVILDEPTAAL---DIDSELAVqkaIDHLVHNRTVII-IAHRLSTI 543
Cdd:PRK11288 157 RNARVIAFDEPTSSLsarEIEQLFRV---IRELRAEGRVILyVSHRMEEI 203

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

351-569

2.17e-15

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 2.17e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 351 YRYDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI----RHLTAeqLNSLISVVFQ 426
Cdd:PRK13638   9 FRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLA--LRQQVATVFQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 D----VWLFD-DTLLA----NLLIARPQATQQeVEEAARAAQCLEFISRLPQGwltpmgemggqLSGGERQRISIARALL 497
Cdd:PRK13638  85 DpeqqIFYTDiDSDIAfslrNLGVPEAEITRR-VDEALTLVDAQHFRHQPIQC-----------LSHGQKKRVAIAGALV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLSR 569
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEISDaVYVLRQGQILTHGAPGEVFAC 226

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

361-557

2.70e-15

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 2.70e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEqlnslISVVFQDVWLFD-DTLLANL 439
Cdd:PRK11247  28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMFQDARLLPwKKVIDNV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIA-----RPQATQ--QEVEEAARAaqclefisrlpqgwltpmGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAAL 512
Cdd:PRK11247 103 GLGlkgqwRDAALQalAAVGLADRA------------------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515713280 513 DIDSELAVQKAIDHL--VHNRTVIIIAHRLS-TIAGAGNILVMEEGEV 557
Cdd:PRK11247 165 DALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

361-561

2.74e-15

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: 74.87 E-value: 2.74e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ--QGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLFDDTLLA 437
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLgIFLAFQYPPEIPGVKNA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLiarpqatqQEVEEAaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDAPIVILDEPTAALDIDSE 517
Cdd:cd03217   96 DFL--------RYVNEG---------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515713280 518 LAVQKAIDHLVH-NRTVIIIAHRlstiagaGNIL---------VMEEGEVVEQG 561
Cdd:cd03217  141 RLVAEVINKLREeGKSVLIITHY-------QRLLdyikpdrvhVLYDGRIVKSG 187

PRK10619

histidine ABC transporter ATP-binding protein HisP;

361-568

4.30e-15

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.39 E-value: 4.30e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHL----------TAEQLNSL---ISVVFQ- 426
Cdd:PRK10619  21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLrtrLTMVFQh 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 -DVWLFDdTLLANLLIARPQA---TQQEVEEaaRAAQCLEFISRLPQGwltpMGEMGGQLSGGERQRISIARALLKDAPI 502
Cdd:PRK10619 101 fNLWSHM-TVLENVMEAPIQVlglSKQEARE--RAVKYLAKVGIDERA----QGKYPVHLSGGQQQRVSIARALAMEPEV 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

344-538

6.36e-15

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.

Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.10 E-value: 6.36e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIG-GVDIRHLTaeqlnslis 422
Cdd:cd03221    1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGsTVKIGYFE--------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 423 vvfqdvwlfddtllanlliarpqatqqeveeaaraaqclefisrlpqgwltpmgemggQLSGGERQRISIARALLKDAPI 502
Cdd:cd03221   70 ----------------------------------------------------------QLSGGEKMRLALAKLLLENPNL 91

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 515713280 503 VILDEPTAALDIDSelaVQKAIDHLV-HNRTVIIIAH 538
Cdd:cd03221   92 LLLDEPTNHLDLES---IEALEEALKeYPGTVILVSH 125

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

361-571

8.16e-15

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.33 E-value: 8.16e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLM---RYaDPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQD------VWL 430
Cdd:COG0396   16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKY-EVTSGSILLDGEDILELSPDERARAgIFLAFQYpveipgVSV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FDdtLLANLLIAR------PQATQQEVEEAARAaqcL----EFISRlpqgwltpmgEMGGQLSGGERQRISIARALLKDA 500
Cdd:COG0396   95 SN--FLRTALNARrgeelsAREFLKLLKEKMKE---LgldeDFLDR----------YVNEGFSGGEKKRNEILQMLLLEP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 501 PIVILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAH--RLSTIAGAGNILVMEEGEVVEQGTH--AQLLSRQG 571
Cdd:COG0396  160 KLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKelALELEEEG 235

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

344-570

1.02e-14

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 1.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHlTAEQLNSLISV 423
Cdd:PRK13537   8 IDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 VFQdvwlFDD-----TLLANLLIARPQATQQEVEEAARAAQCLEFiSRLPQGWLTPMGEmggqLSGGERQRISIARALLK 498
Cdd:PRK13537  85 VPQ----FDNldpdfTVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVN 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 499 DAPIVILDEPTAALDIDS-ELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGNIL-VMEEGEVVEQGTHAQLLSRQ 570
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQArHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLcVIEEGRKIAEGAPHALIESE 229

ABC_6TM_exporters

cd07346

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

35-321

1.34e-14

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: 74.51 E-value: 1.34e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  35 IALLLAALMQGIAFACLYP-----IVDALLRGEASPLLTWALVfsatAFAALALRWYGLGFeYRGHLA-----QATHELR 104
Cdd:cd07346    1 LLLALLLLLLATALGLALPlltklLIDDVIPAGDLSLLLWIAL----LLLLLALLRALLSY-LRRYLAarlgqRVVFDLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 105 LRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPMLVPF 184
Cdd:cd07346   76 RDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 185 YYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHRQSAGATMLIAGVVEL 264
Cdd:cd07346  156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 265 GLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRI 321
Cdd:cd07346  236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

357-570

1.36e-14

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 1.36e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTA-EQLNSLISVVFQDVWLFD--- 432
Cdd:PRK10895  15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrls 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 --DTLLANLLIARPQATQQEVEeaaRAAQCLE--FISRLPQgwltpmgEMGGQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:PRK10895  95 vyDNLMAVLQIRDDLSAEQRED---RANELMEefHIEHLRD-------SMGQSLSGGERRRVEIARALAANPKFILLDEP 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 509 TAALDIDSELAVQKAIDHLV-HNRTVIIIAHRL-STIAGAGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228

LPS_export_lptB

TIGR04406

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...

359-568

1.44e-14

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]

Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 73.46 E-value: 1.44e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQDVWLF-----D 432
Cdd:TIGR04406  15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYLPQEASIFrkltvE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  433 DTLLANLLIaRPQATQQEVEEaaRAAQCL-EF-ISRLPQgwltpmgEMGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:TIGR04406  95 ENIMAVLEI-RKDLDRAEREE--RLEALLeEFqISHLRD-------NKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  511 ALDIDSELAVQKAIDHLVH-NRTVIIIAHRL-STIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKErGIGVLITDHNVrETLDICDRAYIISDGKVLAEGTPAEIVA 224

PRK13651

cobalt transporter ATP-binding subunit; Provisional

360-568

1.46e-14

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 1.46e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTT----VSKLLMryadPQQGEISIGGVDIRHLT---------------------- 413
Cdd:PRK13651  22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehLNALLL----PDTGTIEWIFKDEKNKKktkekekvleklviqktrfkki 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 414 --AEQLNSLISVVFQ--DVWLFDDTLLANLLIArPQATQQEVEEA-ARAAQCLEFISrLPQGWL--TPMGemggqLSGGE 486
Cdd:PRK13651  98 kkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAkKRAAKYIELVG-LDESYLqrSPFE-----LSGGQ 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 487 RQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRL-STIAGAGNILVMEEGEVVEQGTHA 564
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDTY 250


                 ....
gi 515713280 565 QLLS 568
Cdd:PRK13651 251 DILS 254

3a01204

TIGR00955

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...

361-568

1.68e-14

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 1.68e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADP---QQGEISIGGVDIrhlTAEQLNSLISVVFQDVwLFDDTLLA 437
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPTLTV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  438 --NLLIA---RPQATQQEVEEAARAAQCLEFISRLP-QGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:TIGR00955 117 reHLMFQahlRMPRRVTKKEKRERVDEVLQALGLRKcANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  512 LDIDSELAVQKAIDHLVHN-RTVIIIAHR-LSTIAGA-GNILVMEEGEVVEQGTHAQLLS 568
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKgKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAVP 256

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

377-543

1.83e-14

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: 76.36 E-value: 1.83e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 377 VGASGAGKTTVSKLLMRYADPQQGEISiGGVDI----------RHLTAEQ-LNSLISVVFQDVWLFDDtllanllIARP- 444
Cdd:COG1245  372 VGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIsykpqyispdYDGTVEEfLRSANTDDFGSSYYKTE-------IIKPl 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 445 ---QATQQEVEEaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQ 521
Cdd:COG1245  444 gleKLLDKNVKD----------------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495

                        170       180
                 ....*....|....*....|....
gi 515713280 522 KAIDHLVHNR--TVIIIAHRLSTI 543
Cdd:COG1245  496 KAIRRFAENRgkTAMVVDHDIYLI 519

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

357-585

3.10e-14

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.10e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHlTAEQLNSLISVVFQdvwlFDD--- 433
Cdd:PRK13536  53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDNldl 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 434 --TLLANLLIARPQATQQEVEEAARAAQCLEFiSRLPQGWLTPMGEmggqLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:PRK13536 128 efTVRENLLVFGRYFGMSTREIEAVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 512 LDIDS-ELAVQKAIDHLVHNRTVIIIAHrlstiagagnilVMEEGE-------VVEQGTHAQllsrQGRYQALWQAQMAA 583
Cdd:PRK13536 203 LDPHArHLIWERLRSLLARGKTILLTTH------------FMEEAErlcdrlcVLEAGRKIA----EGRPHALIDEHIGC 266


                 ..
gi 515713280 584 RV 585
Cdd:PRK13536 267 QV 268

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

357-546

3.19e-14

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.50 E-value: 3.19e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdirhltaeqlNSLISVVFQDVWLfDDTLL 436
Cdd:NF040873   4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEV-PDSLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANL-------------LIARPQAT-QQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKDAPI 502
Cdd:NF040873  72 LTVrdlvamgrwarrgLWRRLTRDdRAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEADL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515713280 503 VILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLSTIAGA 546
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRA 185

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

377-543

4.23e-14

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 4.23e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 377 VGASGAGKTTVSKLLMRYADPQQGEISIGgVDI----------RHLTAEQLNSLISVVFQDVWLFDDTL----LANLLia 442
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIsykpqyikpdYDGTVEDLLRSITDDLGSSYYKSEIIkplqLERLL-- 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 443 rpqatQQEVEEaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQK 522
Cdd:PRK13409 448 -----DKNVKD----------------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494

                        170       180
                 ....*....|....*....|...
gi 515713280 523 AIDHLVHNR--TVIIIAHRLSTI 543
Cdd:PRK13409 495 AIRRIAEEReaTALVVDHDIYMI 517

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

376-562

4.43e-14

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: 72.44 E-value: 4.43e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 376 LVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI----RHLTAEQLNSLisvvfqdvwlfdDTLLANLLIARPQATQQEV 451
Cdd:cd03237   30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADYEGTV------------RDLLSSITKDFYTHPYFKT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 452 EeaarAAQCLEFISRLPQGWLTpmgemggqLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV--H 529
Cdd:cd03237   98 E----IAKPLQIEQILDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAenN 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515713280 530 NRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGT 562
Cdd:cd03237  166 EKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGV 198

COG4586

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

360-573

5.93e-14

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 5.93e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLL---MRyadPQQGEISIGGVD-----IRHLtaeqlnSLISVVF---QDV 428
Cdd:COG4586   37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgiLV---PTSGEVRVLGYVpfkrrKEFA------RRIGVVFgqrSQL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WlFD----DTLLANLLIARpqatqqeVEEAaraaqclEFISRLpqGWLTPMGEMGG-------QLSGGERQRISIARALL 497
Cdd:COG4586  108 W-WDlpaiDSFRLLKAIYR-------IPDA-------EYKKRL--DELVELLDLGElldtpvrQLSLGQRMRCELAAALL 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 498 KDAPIVILDEPTAALDIDSELAVQKAIDHLV--HNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLLSRQGRY 573
Cdd:COG4586  171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNreRGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEELKERFGPY 249

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

344-569

1.16e-13

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.68 E-value: 1.16e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLL--MRYADPQQGEI--------SIGGVDIRHLT 413
Cdd:TIGR03269   1 IEVKNLTKKFDGK--EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalceKCGYVERPSKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  414 AEQ-------------------------LNSLISVVFQDVWLF--DDTLLANLLIARPQATQQEVEEAARAAQCLEFISR 466
Cdd:TIGR03269  79 GEPcpvcggtlepeevdfwnlsdklrrrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  467 LPQgwltpMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLSTIA 544
Cdd:TIGR03269 159 SHR-----ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIE 233

                         250       260
                  ....*....|....*....|....*.
gi 515713280  545 G-AGNILVMEEGEVVEQGTHAQLLSR 569
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVAV 259

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

347-541

1.25e-13

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.25e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 347 DTICYRYDDSG--DPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLT----AEQLNSL 420
Cdd:PRK11629   9 DNLCKRYQEGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNQK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 ISVVFQDVWLFDD-TLLAN----LLI--ARPQATQQEVEEAArAAQCLEFISRlpqgwltpmgEMGGQLSGGERQRISIA 493
Cdd:PRK11629  89 LGFIYQFHHLLPDfTALENvampLLIgkKKPAEINSRALEML-AAVGLEHRAN----------HRPSELSGGERQRVAIA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 494 RALLKDAPIVILDEPTAALDI---DS------ELAVQKAIDHLV--HNrtvIIIAHRLS 541
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDArnaDSifqllgELNRLQGTAFLVvtHD---LQLAKRMS 213

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

360-561

2.32e-13

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: 69.23 E-value: 2.32e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdiRHLTAEQLNsLISVVFQDVWLFDDTLLANL 439
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARN-RIGYLPEERGLYPKMKVIDQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIARPQATQQEVEEAARaaQCLEFISRLpqgwltpmgEMGG-------QLSGGERQRISIARALLKDAPIVILDEPTAAL 512
Cdd:cd03269   91 LVYLAQLKGLKKEEARR--RIDEWLERL---------ELSEyankrveELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515713280 513 DIDSELAVQKAIDHLVHN-RTVIIIAHRLSTI-AGAGNILVMEEGEVVEQG 561
Cdd:cd03269  160 DPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

344-544

2.63e-13

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 2.63e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ-----QGEISIGGVDI--RHLTAEQ 416
Cdd:PRK14258   8 IKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 417 LNSLISVVFQDVWLFDDTLLANLLIA------RPQATQQEVEEAARAAQCL--EFISRLPQGWLtpmgemggQLSGGERQ 488
Cdd:PRK14258  86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLwdEIKHKIHKSAL--------DLSGGQQQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 489 RISIARALLKDAPIVILDEPTAALDIdselAVQKAIDHLVHNR------TVIIIAHRLSTIA 544
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDP----IASMKVESLIQSLrlrselTMVIVSHNLHQVS 215

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

481-540

4.12e-13

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 4.12e-13

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 481 QLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRL 540
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

482-565

7.15e-13

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: 67.21 E-value: 7.15e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 482 LSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN--RTVIIIAHRLSTIAGAGNILVMEEGEVVE 559
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151


                 ....*.
gi 515713280 560 QGTHAQ 565
Cdd:cd03222  152 YGIASQ 157

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

357-538

1.55e-12

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: 66.61 E-value: 1.55e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLL 436
Cdd:TIGR01189  12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  437 ANL-LIARPQATQQEVEEAARAAQCLEFISRLPqgwltpmgemGGQLSGGERQRISIARALLKDAPIVILDEPTAALDID 515
Cdd:TIGR01189  92 ENLhFWAAIHGGAQRTIEDALAAVGLTGFEDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161

                         170       180
                  ....*....|....*....|....
gi 515713280  516 S-ELAVQKAIDHLVHNRTVIIIAH 538
Cdd:TIGR01189 162 GvALLAGLLRAHLARGGIVLLTTH 185

PRK03695

vitamin B12-transporter ATPase; Provisional

358-568

1.83e-12

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.83e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 358 DPALNNLSLTFPAASMSALVGASGAGKTTvskLLMRYAD--PQQGEISIGGVDIRHLT-----------AEQLNSLISVv 424
Cdd:PRK03695   9 STRLGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSaaelarhraylSQQQTPPFAM- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 425 fqDVWLFDDTLLANLliARPQATQQEVEEAARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARALLKDAP--- 501
Cdd:PRK03695  85 --PVFQYLTLHQPDK--TRTEAVASALNEVAEALGLDDKLGR-----------SVNQLSGGEWQRVRLAAVVLQVWPdin 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 502 ----IVILDEPTAALDIdselAVQKAIDHLVH-----NRTVIIIAHRLS-TIAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK03695 150 pagqLLLLDEPMNSLDV----AQQAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222

PRK13549

xylose transporter ATP-binding subunit; Provisional

356-556

2.55e-12

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.55e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 356 SGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLL---MRYADpQQGEISIGGVDIR-HLTAEQLNSLISVVFQDVWLF 431
Cdd:PRK13549  16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvYPHGT-YEGEIIFEGEELQaSNIRDTERAGIAIIHQELALV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DD-TLLANLLIARPQATQQEVEEAARAAQCLEFISRL-----PQgwlTPMGEMGGqlsgGERQRISIARALLKDAPIVIL 505
Cdd:PRK13549  95 KElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLkldinPA---TPVGNLGL----GQQQLVEIAKALNKQARLLIL 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515713280 506 DEPTAALdIDSELAVQKAI--DHLVHNRTVIIIAHRLSTIAG-AGNILVMEEGE 556
Cdd:PRK13549 168 DEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

346-539

7.96e-12

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 7.96e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 346 FDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVF 425
Cdd:PRK13540   2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 426 QDVWLFDDTLLANLLI-ARPQATQQEVEEAARAAQcLEFISRLPQGWltpmgemggqLSGGERQRISIARALLKDAPIVI 504
Cdd:PRK13540  82 RSGINPYLTLRENCLYdIHFSPGAVGITELCRLFS-LEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515713280 505 LDEPTAALDIDSELAVQKAID-HLVHNRTVIIIAHR 539
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQeHRAKGGAVLLTSHQ 186

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

317-569

1.05e-11

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 1.05e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 317 ALQRIEQFMALPPLPVAERGEMPERYD-IRFDTICYRYDDSGDpALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYA 395
Cdd:PRK10522 295 AFNKLNKLALAPYKAEFPRPQAFPDWQtLELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 396 DPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLlanlliaRPQATQQEVEEAARAAQCLEFIS--RLPQGWLT 473
Cdd:PRK10522 374 QPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL-------GPEGKPANPALVEKWLERLKMAHklELEDGRIS 446

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 474 PMgemggQLSGGERQRISIARALLKDAPIVILDEPTAalDIDSE---------LAVQKAIDHlvhnrTVIIIAHRLSTIA 544
Cdd:PRK10522 447 NL-----KLSKGQKKRLALLLALAEERDILLLDEWAA--DQDPHfrrefyqvlLPLLQEMGK-----TIFAISHDDHYFI 514

                        250       260
                 ....*....|....*....|....*.
gi 515713280 545 GAGNILVMEEGEVVE-QGTHAQLLSR 569
Cdd:PRK10522 515 HADRLLEMRNGQLSElTGEERDAASR 540

ABC_6TM_AarD_CydD

cd18584

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...

34-221

1.14e-11

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: 65.89 E-value: 1.14e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  34 MIALLLAALMQGIAFACLYPIVDALLRGEA-SPLLTWALVFSATAFAALALRWYGlgfEYRGHLA--QATHELRLRLGEQ 110
Cdd:cd18584    3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGlAALLPLLLLLLAALLLRALLAWAQ---ERLAARAaaRVKAELRRRLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 111 LRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPmLVPFYYW--- 187
Cdd:cd18584   80 LLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAP-LIPLFMIlig 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515713280 188 --RRPAMRRQMQTLgeahQRLSGDIVEFAQGMMVLR 221
Cdd:cd18584  159 kaAQAASRRQWAAL----SRLSGHFLDRLRGLPTLK 190

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

363-540

1.50e-11

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: 62.76 E-value: 1.50e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 363 NLSLTFPAASMSALVGASGAGKTTVskllmryadpqqgeisiggvdirhltaeqLNSLISVVFQdvwlfddtllANLLIA 442
Cdd:cd03227   13 PNDVTFGEGSLTIITGPNGSGKSTI-----------------------------LDAIGLALGG----------AQSATR 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 443 RPQATQQEVEEAARAAqclEFISRLPQgwltpmgemggqLSGGERQRISIARAL----LKDAPIVILDEPTAALDIDSEL 518
Cdd:cd03227   54 RRSGVKAGCIVAAVSA---ELIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118

                        170       180
                 ....*....|....*....|...
gi 515713280 519 AVQKAI-DHLVHNRTVIIIAHRL 540
Cdd:cd03227  119 ALAEAIlEHLVKGAQVIVITHLP 141

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

361-540

1.98e-11

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.36 E-value: 1.98e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEIsiggvdirhLTAEQLNslISVVFQDVWLfDDTL---LA 437
Cdd:PRK09544  20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--IGYVPQKLYL-DTTLpltVN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLIARPQATQQEVEEA---ARAAQCLEFisrlpqgwltPMGemggQLSGGERQRISIARALLKDAPIVILDEPTAALDI 514
Cdd:PRK09544  88 RFLRLRPGTKKEDILPAlkrVQAGHLIDA----------PMQ----KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153

                        170       180
                 ....*....|....*....|....*...
gi 515713280 515 DSELAVQKAIDHLVH--NRTVIIIAHRL 540
Cdd:PRK09544 154 NGQVALYDLIDQLRRelDCAVLMVSHDL 181

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

377-561

1.98e-11

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 1.98e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 377 VGASGAGKTTVSKLLMRYADPQQGEISIGGvdirhltaEQLNSL------ISVVFQDVWLFDDTLLAN-------LLIAR 443
Cdd:PRK11000  35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGE--------KRMNDVppaergVGMVFQSYALYPHLSVAEnmsfglkLAGAK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 444 PQATQQEVEEAARAAQCLEFISRLPQGwltpmgemggqLSGGERQRISIARALLKDAPIVILDEPTAALdiDSELAVQKA 523
Cdd:PRK11000 107 KEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL--DAALRVQMR 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515713280 524 ID----HLVHNRTVIIIAH-RLSTIAGAGNILVMEEGEVVEQG 561
Cdd:PRK11000 174 IEisrlHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

344-558

2.11e-11

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 2.11e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  344 IRFDTICYRYDDSgdPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIG-GVDIRHL--TAEQLNSL 420
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGeTVKLAYVdqSRDALDPN 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  421 ISVvFQDVWLFDDTLLANlliarpqatqqEVEEAARAaqcleFISRLP-QGwlTPMGEMGGQLSGGERQRISIARALLKD 499
Cdd:TIGR03719 401 KTV-WEEISGGLDIIKLG-----------KREIPSRA-----YVGRFNfKG--SDQQKKVGQLSGGERNRVHLAKTLKSG 461

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280  500 APIVILDEPTAALDIDSELAVQKAIdhLVHNRTVIIIAH------RLSTiagagNILVME-EGEVV 558
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVVISHdrwfldRIAT-----HILAFEgDSHVE 520

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

480-542

2.76e-11

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: 66.35 E-value: 2.76e-11

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 480 GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLST 542
Cdd:COG1245  211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeEGKYVLVVEHDLAI 274

ABC_Carb_Monos_II

cd03215

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

356-557

2.94e-11

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: 62.45 E-value: 2.94e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 356 SGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQD---VWLF 431
Cdd:cd03215   11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDrkrEGLV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DD-TLLANLLIARpqatqqeveeaaraaqclefisrlpqgwltpmgemggQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:cd03215   91 LDlSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTR 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713280 511 ALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:cd03215  134 GVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182

ABCD_peroxisomal_ALDP

cd03223

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

482-539

3.45e-11

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: 61.79 E-value: 3.45e-11

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 482 LSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAV-QKAIDHLVhnrTVIIIAHR 539
Cdd:cd03223   92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLyQLLKELGI---TVISVGHR 147

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

361-538

3.54e-11

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: 63.25 E-value: 3.54e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLnslisVVFQDVWLFD-DTLLANL 439
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  440 LIA----RPQATQQEVEEAARaaQCLEFIsrlpqGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDID 515
Cdd:TIGR01184  76 ALAvdrvLPDLSKSERRAIVE--EHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148

                         170       180
                  ....*....|....*....|....*
gi 515713280  516 SELAVQKAIDHLV--HNRTVIIIAH 538
Cdd:TIGR01184 149 TRGNLQEELMQIWeeHRVTVLMVTH 173

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

359-566

3.90e-11

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.02 E-value: 3.90e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL---ISVVFQDVWLFDD-T 434
Cdd:PRK11831  21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQSGALFTDmN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 435 LLANllIARPQATQQEVEEA---ARAAQCLEFISRLPQGWLTPmgemgGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:PRK11831 101 VFDN--VAYPLREHTQLPAPllhSTVMMKLEAVGLRGAAKLMP-----SELSGGMARRAALARAIALEPDLIMFDEPFVG 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 512 LDIDSELAVQKAIDHLVH--NRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQL 566
Cdd:PRK11831 174 QDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

361-561

4.45e-11

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 4.45e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQ-----GEISIGGVDI--RHLTAEQLNSLISVVFQ------D 427
Cdd:PRK14267  20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQypnpfpH 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 VWLFDDTLLANLL--IARPQATQQEVEEAA--RAAQCLEFISRLpqgwltpmGEMGGQLSGGERQRISIARALLKDAPIV 503
Cdd:PRK14267 100 LTIYDNVAIGVKLngLVKSKKELDERVEWAlkKAALWDEVKDRL--------NDYPSNLSGGQRQRLVIARALAMKPKIL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 504 ILDEPTAALDIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQG 561
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDyVAFLYLGKLIEVG 230

livF

PRK11614

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

360-570

1.13e-10

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.13e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHL-TAEQLNSLISVVFQDVWLFDD-TLLA 437
Cdd:PRK11614  20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSRmTVEE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLIARPQATQQEVEEaaRAAQCLEFISRLPQGWLTPMGEMggqlSGGERQRISIARALLKDAPIVILDEPTAALdidSE 517
Cdd:PRK11614 100 NLAMGGFFAERDQFQE--RIKWVYELFPRLHERRIQRAGTM----SGGEQQMLAIGRALMSQPRLLLLDEPSLGL---AP 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 518 LAVQKAIDHLVHNR----TVIII---AHRLSTIAGAGniLVMEEGEVVEQGTHAQLLSRQ 570
Cdd:PRK11614 171 IIIQQIFDTIEQLReqgmTIFLVeqnANQALKLADRG--YVLENGHVVLEDTGDALLANE 228

PRK15112

peptide ABC transporter ATP-binding protein SapF;

360-568

1.22e-10

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 1.22e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVwlfddtllANL 439
Cdd:PRK15112  28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP--------STS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIARPQATQ---------QEVEEAARAAQcleFISRLPQGWLTP--MGEMGGQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:PRK15112 100 LNPRQRISQildfplrlnTDLEPEQREKQ---IIETLRQVGLLPdhASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 509 TAALD-------IDSELAVQKAidhlvHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK15112 177 LASLDmsmrsqlINLMLELQEK-----QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239

anch_rpt_ABC

TIGR03771

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...

375-570

1.59e-10

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]

Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 61.41 E-value: 1.59e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  375 ALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEqlnslISVVFQD---VWLFDDTLLANLLIARP------- 444
Cdd:TIGR03771  10 GLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-----IGYVPQRhefAWDFPISVAHTVMSGRTghigwlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  445 ---QATQQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKDAPIVILDEPTAALDIDS-ELAV 520
Cdd:TIGR03771  85 rpcVADFAAVRDALRRVGLTELADR-------PVGE----LSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTqELLT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515713280  521 QKAIDHLVHNRTVIIIAHRLSTIAGAGNILVMEEGEVVEQGTHAQLLSRQ 570
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPA 203

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

361-513

1.67e-10

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 1.67e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL----ISVVFQDVWLFDdTLL 436
Cdd:PRK10584  26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIP-TLN 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 437 ANLLIARPQATQQEVEEAARAaQCLEFISRLPQGwlTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALD 513
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRN-GAKALLEQLGLG--KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

360-561

1.83e-10

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: 60.03 E-value: 1.83e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKllmryadpqqgEIsiggvdirhLTAEQLNSLISvvfqdvwlFDDTLLANL 439
Cdd:cd03238   10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EG---------LYASGKARLIS--------FLPKFSRNK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIARPQatqqeveeaaraaqcLEFISRLPQGWLTPMGEMGgQLSGGERQRISIARALLKDAP--IVILDEPTAALDIDSE 517
Cdd:cd03238   62 LIFIDQ---------------LQFLIDVGLGYLTLGQKLS-TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515713280 518 LAVQKAIDHLVH-NRTVIIIAHRLSTIAGAGNILVM------EEGEVVEQG 561
Cdd:cd03238  126 NQLLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

352-539

2.05e-10

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 2.05e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEisiGGVDIRHLTAEQLNSLIsvvfQDVWLF 431
Cdd:COG2401   37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA---GCVDVPDNQFGREASLI----DAIGRK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DDTLLAnlliarpqatqqeveeaaraaqcLEFISRL----PQGWLTPMGEmggqLSGGERQRISIARALLKDAPIVILDE 507
Cdd:COG2401  110 GDFKDA-----------------------VELLNAVglsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDE 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515713280 508 PTAALDIDSELAVQKAIDHLV--HNRTVIIIAHR 539
Cdd:COG2401  163 FCSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196

PRK09984

phosphonate ABC transporter ATP-binding protein;

360-566

2.19e-10

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 2.19e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTV----SKLLMRYADPQQGEISIGGV---------DIRHLTAEQlnsliSVVFQ 426
Cdd:PRK09984  19 ALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGSHIELLGRTvqregrlarDIRKSRANT-----GYIFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 DVWLFDD-TLLANLLIARPQATqqeveeaARAAQCLEFISRL-PQGWLTPMGEMG---------GQLSGGERQRISIARA 495
Cdd:PRK09984  94 QFNLVNRlSVLENVLIGALGST-------PFWRTCFSWFTREqKQRALQALTRVGmvhfahqrvSTLSGGQQQRVAIARA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 496 LLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR--TVIIIAHRLS-TIAGAGNILVMEEGEVVEQGTHAQL 566
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

350-557

2.31e-10

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: 63.31 E-value: 2.31e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  350 CYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKT-TVSKLLMRYADPQQGEISIGG--VDIRHlTAEQLNSLISVVFQ 426
Cdd:TIGR02633 265 CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIRN-PAQAIRAGIAMVPE 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  427 D---------VWLFDDTLLANLliaRPQATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGqLSGGERQRISIARALL 497
Cdd:TIGR02633 344 DrkrhgivpiLGVGKNITLSVL---KSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLL 419

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280  498 KDAPIVILDEPTAALDIDSELAVQKAIDHLVHNR-TVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGlSDRVLVIGEGKL 481

sufC

TIGR01978

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...

359-561

2.65e-10

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]

Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 61.12 E-value: 2.65e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMryADPQ----QGEISIGGVDIRHLTAEQLNSL-ISVVFQ---DV-W 429
Cdd:TIGR01978  14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIA--GHPSyevtSGTILFKGQDLLELEPDERARAgLFLAFQypeEIpG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  430 LFDDTLLANLLIARPQATQQEV-----------EEAARAAQCLEFISR-LPQGWltpmgemggqlSGGERQRISIARALL 497
Cdd:TIGR01978  92 VSNLEFLRSALNARRSARGEEPldlldfekllkEKLALLDMDEEFLNRsVNEGF-----------SGGEKKRNEILQMAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280  498 KDAPIVILDEPTAALDIDSELAVQKAIDHL-VHNRTVIIIAH--RLSTIAGAGNILVMEEGEVVEQG 561
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLrEPDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

359-583

3.04e-10

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.87 E-value: 3.04e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADP----QQGEISIGGVDIrhLTAEQLNSLISVVFQD------- 427
Cdd:PRK10418  17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV--APCALRGRKIATIMQNprsafnp 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 VWLFDDTLLANLLIARPQATQQEVEEAARAAQcLEFISRLPQgwLTPMgemggQLSGGERQRISIARALLKDAPIVILDE 507
Cdd:PRK10418  95 LHTMHTHARETCLALGKPADDATLTAALEAVG-LENAARVLK--LYPF-----EMSGGMLQRMMIALALLCEAPFIIADE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 508 PTAALDIDSELAVQKAIDHLVHNRT--VIIIAHRLSTIAG-AGNILVMEEGEVVEQGTHAQLLSRQGR---------YQA 575
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHavtrslvsaHLA 246


                 ....*...
gi 515713280 576 LWQAQMAA 583
Cdd:PRK10418 247 LYGMELAS 254

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

363-547

3.30e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 3.30e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 363 NLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLisvvfqdVWL-----FDDTLLA 437
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL-------LYLghqpgIKTELTA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 --NLLIArpQATQQEV-EEAARAAqclefisrlpqgwLTPMGEMG------GQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:PRK13538  92 leNLRFY--QRLHGPGdDEALWEA-------------LAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 515713280 509 TAALDIDSELAVQKAID-HLVHNRTVIIIAHRLSTIAGAG 547
Cdd:PRK13538 157 FTAIDKQGVARLEALLAqHAEQGGMVILTTHQDLPVASDK 196

YhaQ

COG4152

ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...

360-572

4.20e-10

ABC-type uncharacterized transport system, ATPase component [General function prediction only];

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.28 E-value: 4.20e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQ---------LNSLISVvfQDVWL 430
Cdd:COG4152   16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeergLYPKMKV--GEQLV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FddtlLANLliarpqaTQQEVEEAARAAqcLEFISRLpqgwltpmgEMGG-------QLSGGERQRISIARALLKDAPIV 503
Cdd:COG4152   94 Y----LARL-------KGLSKAEAKRRA--DEWLERL---------GLGDrankkveELSKGNQQKVQLIAALLHDPELL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 504 ILDEPTAALD-IDSELaVQKAIDHLVHN-RTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLLSRQGR 572
Cdd:COG4152  152 ILDEPFSGLDpVNVEL-LKDVIRELAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR 222

PRK13549

xylose transporter ATP-binding subunit; Provisional

378-557

4.35e-10

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.35e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 378 GASGAGKT-TVSKLLMRYADPQQGEISIGG--VDIRHlTAEQLNSLISVVFQD------VWLFD---DTLLANLliaRPQ 445
Cdd:PRK13549 295 GLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDrkrdgiVPVMGvgkNITLAAL---DRF 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 446 ATQQEVEEAARAAQCLEFISRLPQGWLTPMGEMGgQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAID 525
Cdd:PRK13549 371 TGGSRIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515713280 526 HLVHNR-TVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:PRK13549 450 QLVQQGvAIIVISSELPEVLGlSDRVLVMHEGKL 483

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

347-579

4.46e-10

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.30 E-value: 4.46e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 347 DTICYRYDDSGDP--ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYAD-P---QQGEISIGGVDIRHLTAEQLNSL 420
Cdd:PRK11022   7 DKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 421 I----SVVFQD-VWLFDDTLLANLLIARPQATQQEVEEAARAAQCLEFISRLpqGWLTPMGEMG---GQLSGGERQRISI 492
Cdd:PRK11022  87 VgaevAMIFQDpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQV--GIPDPASRLDvypHQLSGGMSQRVMI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 493 ARALLKDAPIVILDEPTAALD-------IDSELAVQKAidhlvHNRTVIIIAHRLSTIA-GAGNILVMEEGEVVEQGTHA 564
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQK-----ENMALVLITHDLALVAeAAHKIIVMYAGQVVETGKAH 239

                        250
                 ....*....|....*..
gi 515713280 565 QLLS--RQGRYQALWQA 579
Cdd:PRK11022 240 DIFRapRHPYTQALLRA 256

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

375-567

5.86e-10

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 5.86e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 375 ALVGASGAGKTTVSKLLMRYADPQQGEISIGG-----VDIRHLTAEQLNSLI----SVVFQDVwlfDDTLL------ANL 439
Cdd:PRK11701  36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLrtewGFVHQHP---RDGLRmqvsagGNI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 ---LIA---------RPQATQ--QEVE-EAARaaqclefISRLPqgwltpmgemgGQLSGGERQRISIARALLKDAPIVI 504
Cdd:PRK11701 113 gerLMAvgarhygdiRATAGDwlERVEiDAAR-------IDDLP-----------TTFSGGMQQRLQIARNLVTHPRLVF 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515713280 505 LDEPTAALDIdselAVQ-KAID---HLVH--NRTVIIIAHRLStIAG--AGNILVMEEGEVVEQGTHAQLL 567
Cdd:PRK11701 175 MDEPTGGLDV----SVQaRLLDllrGLVRelGLAVVIVTHDLA-VARllAHRLLVMKQGRVVESGLTDQVL 240

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

357-543

7.46e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 7.46e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTA-EQLNSLISVVFQDVWLF-DDT 434
Cdd:PRK10982  10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkEALENGISMVHQELNLVlQRS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 435 LLANLLIARPQATQQEVEEAARAAQCLEFISRL-----PQgwltpmgEMGGQLSGGERQRISIARALLKDAPIVILDEPT 509
Cdd:PRK10982  90 VMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELdididPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515713280 510 AALdidselaVQKAIDHL------VHNR--TVIIIAHRLSTI 543
Cdd:PRK10982 163 SSL-------TEKEVNHLftiirkLKERgcGIVYISHKMEEI 197

ycf16

CHL00131

sulfate ABC transporter protein; Validated

361-571

8.57e-10

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 8.57e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ--QGEISIGGVDIRHLTAEQLNSL-ISVVFQdvWLFDDTLLA 437
Cdd:CHL00131  23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLgIFLAFQ--YPIEIPGVS 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 N---LLIARPQATQQEVEEAARAAQCLEFISR------LPQGWLTPMGEMGgqLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:CHL00131 101 NadfLRLAYNSKRKFQGLPELDPLEFLEIINEklklvgMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAILDET 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 509 TAALDIDSELAVQKAIDHLVH-NRTVIIIAH--RLSTIAGAGNILVMEEGEVVEQG--THAQLLSRQG 571
Cdd:CHL00131 179 DSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGdaELAKELEKKG 246

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

347-538

9.22e-10

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 9.22e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 347 DTICYRyddSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIR------------HLTA 414
Cdd:PRK13539   7 DLACVR---GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpdvaeachylgHRNA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 415 eqLNSLISVVfqdvwlfddtllANLLI-ARPQATQQEVEEAARAAQCLEFISRLPqgwltpmgemGGQLSGGERQRISIA 493
Cdd:PRK13539  84 --MKPALTVA------------ENLEFwAAFLGGEELDIAAALEAVGLAPLAHLP----------FGYLSAGQKRRVALA 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515713280 494 RALLKDAPIVILDEPTAALDIDSELAVQKAI-DHLVHNRTVIIIAH 538
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

361-517

9.31e-10

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: 58.66 E-value: 9.31e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVFQDVWLFDDTLLANLL 440
Cdd:cd03231   16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 441 IARPQATQQEVEEAaraaqclefisrLPQGWLTPMGEMG-GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSE 517
Cdd:cd03231   96 FWHADHSDEQVEEA------------LARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

376-568

1.25e-09

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.89 E-value: 1.25e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 376 LVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI-----------------------RHLTAEQlNslisvvfqdvwlfd 432
Cdd:COG1137   34 LLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarlgigylpqeasifRKLTVED-N-------------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 dtLLANLLIARPQATQQEveeaARAAQCL-EF-ISRLpqgwltpMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:COG1137   99 --ILAVLELRKLSKKERE----ERLEELLeEFgITHL-------RKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 511 ALDidsELAV---QKAIDHLV----------HN-RTVIIIAHRLStiagagnilVMEEGEVVEQGTHAQLLS 568
Cdd:COG1137  166 GVD---PIAVadiQKIIRHLKergigvlitdHNvRETLGICDRAY---------IISEGKVLAEGTPEEILN 225

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

360-558

1.48e-09

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.48e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLL--MRYADPQQGEISIGGVDI--RHLTAEQLNSlISVVFQDVWLFDD-T 434
Cdd:TIGR02633  16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgVYPHGTWDGEIYWSGSPLkaSNIRDTERAG-IVIIHQELTLVPElS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  435 LLANLL----IARPQATQQEVEEAARAAQCLEFIsRLPqgwLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTA 510
Cdd:TIGR02633  95 VAENIFlgneITLPGGRMAYNAMYLRAKNLLREL-QLD---ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515713280  511 AL-DIDSELAVQKAIDHLVHNRTVIIIAHRLSTIAGAGN-ILVMEEGEVV 558
Cdd:TIGR02633 171 SLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDtICVIRDGQHV 220

ABC_UvrA_II

cd03271

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...

474-562

1.62e-09

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: 58.78 E-value: 1.62e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 474 PMGEMGGQLSGGERQRISIARALLKDAP---IVILDEPTAAL---DIDSELAVqkaIDHLVHN-RTVIIIAHRLSTIAGA 546
Cdd:cd03271  162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEV---LQRLVDKgNTVVVIEHNLDVIKCA 238

                         90       100
                 ....*....|....*....|..
gi 515713280 547 GNILVM------EEGEVVEQGT 562
Cdd:cd03271  239 DWIIDLgpeggdGGGQVVASGT 260

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

481-541

1.80e-09

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 1.80e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 481 QLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLS 541
Cdd:cd03236  139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEHDLA 200

PRK11147

ABC transporter ATPase component; Reviewed

375-538

2.16e-09

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.16e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 375 ALVGASGAGKTTVSKLLMRYADPQQGEISIGgvdiRHLtaeqlnslisvvfqDVWLFDD---------TLLANLliarpQ 445
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKL--------------EVAYFDQhraeldpekTVMDNL-----A 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 446 ATQQEVEEAARAAQCLEFIsrlpQGWL-TPMGEMG--GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDS-ELavq 521
Cdd:PRK11147 406 EGKQEVMVNGRPRHVLGYL----QDFLfHPKRAMTpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlEL--- 478

                        170
                 ....*....|....*....
gi 515713280 522 kaIDHLVHNR--TVIIIAH 538
Cdd:PRK11147 479 --LEELLDSYqgTVLLVSH 495

PRK10762

D-ribose transporter ATP binding protein; Provisional

360-543

4.12e-09

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.12e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG--VDIRHLTAEQlNSLISVVFQDVWLFDD-TLL 436
Cdd:PRK10762  19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQ-EAGIGIIHQELNLIPQlTIA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 ANLLIARPQAT-------QQEVEEAARAAQCLEfisrLPQGWLTPMGEmggqLSGGERQRISIARALLKDAPIVILDEPT 509
Cdd:PRK10762  98 ENIFLGREFVNrfgridwKKMYAEADKLLARLN----LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515713280 510 AAL-DIDSElAVQKAIDHL-VHNRTVIIIAHRLSTI 543
Cdd:PRK10762 170 DALtDTETE-SLFRVIRELkSQGRGIVYISHRLKEI 204

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

344-571

5.19e-09

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 5.19e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   344 IRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIrhLTAeqlnslISV 423
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN------ISD 2009

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   424 VFQDVWL---FD--DTLLAN----LLIARPQAT-QQEVEEAARAAqclefISRLpqGWLTPMGEMGGQLSGGERQRISIA 493
Cdd:TIGR01257 2010 VHQNMGYcpqFDaiDDLLTGrehlYLYARLRGVpAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTA 2082

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   494 RALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

352-561

5.31e-09

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: 56.50 E-value: 5.31e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 352 RYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ---QGEISIGGVDIrHLTAEQLNSLISVVFQDV 428
Cdd:cd03233   14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-KEFAEKYPGEIIYVSEED 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WLFddtllanlliarPQATqqeVEEAaraaqcLEFISRLpQGwltpmGEMGGQLSGGERQRISIARALLKDAPIVILDEP 508
Cdd:cd03233   93 VHF------------PTLT---VRET------LDFALRC-KG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 509 TAALDIDSELAVQKAIDHLVHnrtviiiAHRLSTIAG---AGN--------ILVMEEGEVVEQG 561
Cdd:cd03233  146 TRGLDSSTALEILKCIRTMAD-------VLKTTTFVSlyqASDeiydlfdkVLVLYEGRQIYYG 202

GguA

NF040905

sugar ABC transporter ATP-binding protein;

360-559

1.61e-08

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 1.61e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLM------RYadpqQGEISIGGV-----DIRhlTAEQLNslISVVFQDV 428
Cdd:NF040905  16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSY----EGEILFDGEvcrfkDIR--DSEALG--IVIIHQEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 429 WLFDDTLLA-NLLIARPQATQQEV---EEAARAAQCLEFI--SRLPQgwlTPMGEMGGqlsgGERQRISIARALLKDAPI 502
Cdd:NF040905  88 ALIPYLSIAeNIFLGNERAKRGVIdwnETNRRARELLAKVglDESPD---TLVTDIGV----GKQQLVEIAKALSKDVKL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515713280 503 VILDEPTAAL-DIDSElavqKAIDHLVHNR----TVIIIAHRLSTIAG-AGNILVMEEGEVVE 559
Cdd:NF040905 161 LILDEPTAALnEEDSA----ALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219

AAA

smart00382

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

375-546

1.96e-08

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.53 E-value: 1.96e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   375 ALVGASGAGKTTVSKLLMRYADPQQGE-ISIGGVDIRHLTAEQLnslisvvfqdvwlfddtllanlliarpqatqqevee 453
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------------ 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   454 aaraaqclefisrlpqgWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV----- 528
Cdd:smart00382  50 -----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllk 112

                          170       180
                   ....*....|....*....|
gi 515713280   529 --HNRTVIIIAHRLSTIAGA 546
Cdd:smart00382 113 seKNLTVILTTNDEKDLGPA 132

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

451-562

2.37e-08

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: 57.33 E-value: 2.37e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  451 VEEAA-------RAAQCLEFISRLPQGWLtPMGEMGGQLSGGERQRISIARALLKDA---PIVILDEPTAAL---DIDSE 517
Cdd:TIGR00630 793 VEEAYeffeavpSISRKLQTLCDVGLGYI-RLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKL 871

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515713280  518 LAVqkaIDHLVHN-RTVIIIAHRLSTIAGAGNILVM------EEGEVVEQGT 562
Cdd:TIGR00630 872 LEV---LQRLVDKgNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGT 920

ABC_6TM_Rv0194_D1_like

cd18543

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

34-321

4.27e-08

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: 54.80 E-value: 4.27e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  34 MIALLLAALMqGIAFACLYPIV------DALLRGEASPLLTWALVFSATAFAALAL----RWYGlgfeyrGHLAQAT-HE 102
Cdd:cd18543    1 LILALLAALL-ATLAGLAIPLLtrraidGPIAHGDRSALWPLVLLLLALGVAEAVLsflrRYLA------GRLSLGVeHD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 103 LRLRLGEQLRRVPLERLQRGRAGEtnalLLGSVDENLNYVIAIANILLLTIVTPLTASLAT---LWIDWRLGLVMLLIFP 179
Cdd:cd18543   74 LRTDLFAHLQRLDGAFHDRWQSGQ----LLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLvvmLVLSPPLALVALASLP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 180 MLVPF-YYWRR---PAMRRQMQTLGEahqrLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHRQSAGAT 255
Cdd:cd18543  150 PLVLVaRRFRRryfPASRRAQDQAGD----LATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFW 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 256 MLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRI 321
Cdd:cd18543  226 PLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291

ugpC

PRK11650

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

355-513

4.47e-08

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 4.47e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 355 DSGDPALNNLSLTFPAASMSALVGASGAGKTTvskLLMRYADPQQ---GEISIGGVDIRHLtaEQLNSLISVVFQDVWLF 431
Cdd:PRK11650  14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKST---LLRMVAGLERitsGEIWIGGRVVNEL--EPADRDIAMVFQNYALY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 D-----DTLLANLLIAR-PQAT-QQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKDaPIVI 504
Cdd:PRK11650  89 PhmsvrENMAYGLKIRGmPKAEiEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRAIVRE-PAVF 156

                        170
                 ....*....|
gi 515713280 505 L-DEPTAALD 513
Cdd:PRK11650 157 LfDEPLSNLD 166

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

365-582

4.71e-08

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 4.71e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 365 SLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISvvfqDVWLFDDTllaNLLIARP 444
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVS----DEWQRNNT---DMLSPGE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 445 QAT--------QQEVEEAARAAQCLEF--ISRLpqgwltpMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDI 514
Cdd:PRK10938  96 DDTgrttaeiiQDEVKDPARCEQLAQQfgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 515 DSELAVQKAIDHLVHNR-TVIIIAHRLSTI-AGAGNILVMEEGEVVEQGTHAQLLSrqgryQALWqAQMA 582
Cdd:PRK10938 169 ASRQQLAELLASLHQSGiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ-----QALV-AQLA 232

PRK15093

peptide ABC transporter ATP-binding protein SapD;

343-568

6.84e-08

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 6.84e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 343 DIRFDTICYRYDDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLL--------------MRYADpqqgeisiggVD 408
Cdd:PRK15093   5 DIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDD----------ID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 409 IRHLTAEQLNSLI----SVVFQDVWLFDD---TLLANLLIARPQAT-----QQEVEEAARAAqcLEFISRLP-QGWLTPM 475
Cdd:PRK15093  75 LLRLSPRERRKLVghnvSMIFQEPQSCLDpseRVGRQLMQNIPGWTykgrwWQRFGWRKRRA--IELLHRVGiKDHKDAM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 476 GEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALdidsELAVQKAIDHLV------HNRTVIIIAHRLSTIAG-AGN 548
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAM----EPTTQAQIFRLLtrlnqnNNTTILLISHDLQMLSQwADK 228

                        250       260
                 ....*....|....*....|
gi 515713280 549 ILVMEEGEVVEQGTHAQLLS 568
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVT 248

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

360-561

1.09e-07

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: 52.92 E-value: 1.09e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdirhltaeqlnslisvvfQDVWLFD------- 432
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------------RVSSLLGlgggfnp 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 433 -----DTLLANLLIARpqATQQEVEEaaRAAQCLEFiSRLPQGWLTPMGEmggqLSGGERQRISIARALLKDAPIVILDE 507
Cdd:cd03220   98 eltgrENIYLNGRLLG--LSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDE 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 508 PTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAGAGN-ILVMEEGEVVEQG 561
Cdd:cd03220  169 VLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRLCDrALVLEKGKIRFDG 224

PRK10636

putative ABC transporter ATP-binding protein; Provisional

361-524

1.19e-07

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.19e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIG-GVDIRHLTAEQLNSLISvvfqdvwlfDDTLLANL 439
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRA---------DESPLQHL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIARPQATQQEVEEaaraaqclefisrlpqgWLTPMG-------EMGGQLSGGERQRISIARALLKDAPIVILDEPTAAL 512
Cdd:PRK10636 399 ARLAPQELEQKLRD-----------------YLGGFGfqgdkvtEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461

                        170
                 ....*....|..
gi 515713280 513 DIDSELAVQKAI 524
Cdd:PRK10636 462 DLDMRQALTEAL 473

MglA

COG1129

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

376-558

1.46e-07

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 1.46e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 376 LVGASGAGKTTVSKLLMRYADPQQGEISIGG--VDIRHlTAEQLNSLISVVFQD-----VWLfDDTLLANLLIARPQATQ 448
Cdd:COG1129  283 IAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRS-PRDAIRAGIAYVPEDrkgegLVL-DLSIRENITLASLDRLS 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 449 -----QEVEEAARAAqclEFISRL---PQGWLTPMGemggQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAV 520
Cdd:COG1129  361 rggllDRRRERALAE---EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEI 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713280 521 QKAIDHLVHN-RTVIII----------AHRlstiagagnILVMEEGEVV 558
Cdd:COG1129  434 YRLIRELAAEgKAVIVIsselpellglSDR---------ILVMREGRIV 473

ABC_6TM_exporter_like

cd18564

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

35-215

2.50e-07

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

Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.90 E-value: 2.50e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  35 IALLLAALMQGIAFACLYP-----IVDALLRGEASPLLTW-----------ALVFSATAFAALALRWYGLGF--EYRGHL 96
Cdd:cd18564    1 LALALLALLLETALRLLEPwplkvVIDDVLGDKPLPGLLGlapllgpdplaLLLLAAAALVGIALLRGLASYagTYLTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  97 A--QATHELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDenlnyviAIANiLLLTIVTPLTASLATL--------WI 166
Cdd:cd18564   81 VgqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVG-------AIQD-LLVSGVLPLLTNLLTLvgmlgvmfWL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713280 167 DWRLGLVMLLIFPMLVPFYYWrrpaMRRQMQTLGEAHQRLSGDIVEFAQ 215
Cdd:cd18564  153 DWQLALIALAVAPLLLLAARR----FSRRIKEASREQRRREGALASVAQ 197

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

344-555

2.76e-07

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: 51.09 E-value: 2.76e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 344 IRFDTICYRYDDSGDPA--LNNLSLTFPAASMSALVGASGAGKTTVSKLLM--RYADPQQGEISIGGVDIRhltaEQLNS 419
Cdd:cd03232    4 LTWKNLNYTVPVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD----KNFQR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 420 LISVVFQDvwlfdDTLLanlliarPQATqqeVEEAaraaqcLEFiSRLPQGwltpmgemggqLSGGERQRISIARALLKD 499
Cdd:cd03232   80 STGYVEQQ-----DVHS-------PNLT---VREA------LRF-SALLRG-----------LSVEQRKRLTIGVELAAK 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 500 APIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLS--TIAGAGNILVMEEG 555
Cdd:cd03232  127 PSILFLDEPTSGLDSQAAYNIVRFLKKLAdSGQAILCTIHQPSasIFEKFDRLLLLKRG 185

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

357-571

3.16e-07

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 3.16e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQ--QGEISIGGVDIRHLTAEQ-LNSLISVVFQ------- 426
Cdd:PRK09580  13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDrAGEGIFMAFQypveipg 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 427 -DVWLFDDTLLANLLIARPQAT------QQEVEEAARaaqclefISRLPQGWLTPMGEMGgqLSGGERQRISIARALLKD 499
Cdd:PRK09580  93 vSNQFFLQTALNAVRSYRGQEPldrfdfQDLMEEKIA-------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 500 APIVILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAH--RLSTIAGAGNILVMEEGEVVEQGTH--AQLLSRQG 571
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlVKQLEEQG 240

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

480-557

7.82e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 7.82e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVH-NRTVIIIAHRLSTIAGAGN-ILVMEEGEV 557
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkDKGIIIISSEMPELLGITDrILVMSNGLV 469

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

361-538

9.52e-07

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 9.52e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  361 LNNLSLTF-PAASMsALVGASGAGKTTVSKLLMRYADPQQGE------ISIG--------------------GV-DIRHL 412
Cdd:TIGR03719  21 LKDISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgIKVGylpqepqldptktvrenveeGVaEIKDA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  413 TAEqLNSlISVVFQDVwlfDDTLlaNLLIARpQATQQEVEEAA----------RAAQCLefisRLPQgWLTPMGEmggqL 482
Cdd:TIGR03719 100 LDR-FNE-ISAKYAEP---DADF--DKLAAE-QAELQEIIDAAdawdldsqleIAMDAL----RCPP-WDADVTK----L 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280  483 SGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKaidHLV-HNRTVIIIAH 538
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQeYPGTVVAVTH 216

uvrA

PRK00349

excinuclease ABC subunit UvrA;

480-562

1.38e-06

excinuclease ABC subunit UvrA;

Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 51.61 E-value: 1.38e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQ----LSGGERQRISIARALLKDA---PIVILDEPTAAL---DIDSELAVqkaIDHLVHN-RTVIIIAHRLSTIAGAGN 548
Cdd:PRK00349 825 GQpattLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRKLLEV---LHRLVDKgNTVVVIEHNLDVIKTADW 901

                         90       100
                 ....*....|....*....|
gi 515713280 549 ILVM------EEGEVVEQGT 562
Cdd:PRK00349 902 IIDLgpeggdGGGEIVATGT 921

PRK10762

D-ribose transporter ATP binding protein; Provisional

473-567

2.28e-06

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 2.28e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 473 TP-MGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIdselAVQKAIDHLVhNR------TVIIIAHRLSTIAG 545
Cdd:PRK10762 386 TPsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV----GAKKEIYQLI-NQfkaeglSIILVSSEMPEVLG 460

                         90       100
                 ....*....|....*....|....*...
gi 515713280 546 AGN-ILVMEEGEV-----VEQGTHAQLL 567
Cdd:PRK10762 461 MSDrILVMHEGRIsgeftREQATQEKLM 488

UvrA

COG0178

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];

480-562

2.95e-06

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 2.95e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQ----LSGGERQRISIARALLKDAP---IVILDEPTAAL---DIDSELAVqkaIDHLV---HnrTVIIIAHRLSTIAGA 546
Cdd:COG0178  821 GQpattLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLEV---LHRLVdkgN--TVVVIEHNLDVIKTA 895

                         90       100
                 ....*....|....*....|..
gi 515713280 547 GNILVM------EEGEVVEQGT 562
Cdd:COG0178  896 DWIIDLgpeggdGGGEIVAEGT 917

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

363-557

3.16e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 3.16e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 363 NLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHL-TAEQLNSliSVVF-----QDVWLFDDTLL 436
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLAR--GLVYlpedrQSSGLYLDAPL 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 437 A----NLLIARPQATQQEVEEAARaaqcLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAAL 512
Cdd:PRK15439 359 AwnvcALTHNRRGFWIKPARENAV----LERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515713280 513 DIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:PRK15439 435 DVSARNDIYQLIRSIAaQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

357-515

3.38e-06

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 3.38e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPAL-NNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGG------VD-IR-HLTAEQlnslisVVFQD 427
Cdd:PRK11819 335 GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvklayVDqSRdALDPNK------TVWEE 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 VWLFDDTLLANlliarpqatqqEVEEAARAaqcleFISRLpqgwltpmGEMG-------GQLSGGERQRISIARALLKDA 500
Cdd:PRK11819 409 ISGGLDIIKVG-----------NREIPSRA-----YVGRF--------NFKGgdqqkkvGVLSGGERNRLHLAKTLKQGG 464

                        170
                 ....*....|....*
gi 515713280 501 PIVILDEPTAALDID 515
Cdd:PRK11819 465 NVLLLDEPTNDLDVE 479

ABC_6TM_AarD_CydDC_like

cd18561

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...

54-266

3.92e-06

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: 48.82 E-value: 3.92e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  54 IVDALLRGEASPLLTWALVFSATAFAALALRWyglGFEYRGHLAQAT--HELRLRLGEQLRRVPLERLQRGRAGETNALL 131
Cdd:cd18561   23 LARIFAGGPWEDIMPPLAGIAGVIVLRAALLW---LRERVAHRAAQRvkQHLRRRLFAKLLKLGPGYLEGERTGELQTTV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 132 LGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLG---LVMLLIFPMLVPFYYWRrpaMRRQMQTLGEAHQRLSG 208
Cdd:cd18561  100 VDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVAlilLVFALLIPLSPALWDRL---AKDTGRRHWAAYGRLSA 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 209 DIVEFAQGMMVLRTCGSDGEKSRALLahfNALESLQSRTHRQSAgATMLIAGVVELGL 266
Cdd:cd18561  177 QFLDSLQGMTTLKAFGASKRRGNELA---ARAEDLRQATMKVLA-VSLLSSGIMGLAT 230

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

375-538

6.21e-06

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.

Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 6.21e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 375 ALVGASGAGKTTVSKLLmRYA-----DPQqgeiSIGGVDIRHLTAEQLNSL-ISVVFQDVwlfddtlLANLLIARpqatq 448
Cdd:cd03240   26 LIVGQNGAGKTTIIEAL-KYAltgelPPN----SKGGAHDPKLIREGEVRAqVKLAFENA-------NGKKYTIT----- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 449 qeveeaaRAAQCLEFISRLPQG---WLTPmgEMGGQLSGGERQ------RISIARALLKDAPIVILDEPTAALDIDS-EL 518
Cdd:cd03240   89 -------RSLAILENVIFCHQGesnWPLL--DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEE 159

                        170       180
                 ....*....|....*....|..
gi 515713280 519 AVQKAIDHLVH--NRTVIIIAH 538
Cdd:cd03240  160 SLAEIIEERKSqkNFQLIVITH 181

PLN03211

ABC transporter G-25; Provisional

375-568

8.38e-06

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 8.38e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 375 ALVGASGAGKTTvskLLMRYADPQQGEISIGGVDI--RHLTaEQLNSLISVVFQDVWLFD-----DTLLANLLIARPQA- 446
Cdd:PLN03211  98 AVLGPSGSGKST---LLNALAGRIQGNNFTGTILAnnRKPT-KQILKRTGFVTQDDILYPhltvrETLVFCSLLRLPKSl 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 447 TQQEVEEAARAAqclefISRLPqgwLTPMGE--MGGQ----LSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAV 520
Cdd:PLN03211 174 TKQEKILVAESV-----ISELG---LTKCENtiIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515713280 521 QKAIDHLVHN-RTVIIIAHRLST--IAGAGNILVMEEGEVVEQGTHAQLLS 568
Cdd:PLN03211 246 VLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

354-558

1.09e-05

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.09e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 354 DDSGDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSL-ISVVFQD----- 427
Cdd:COG3845  267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrg 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 428 ------VW------LFDDTLLANLLIARPQATQQEVEEAARaaqclEFISRLPQGWlTPMGemggQLSGGERQRISIARA 495
Cdd:COG3845  347 lvpdmsVAenlilgRYRRPPFSRGGFLDRKAIRAFAEELIE-----EFDVRTPGPD-TPAR----SLSGGNQQKVILARE 416

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 496 LLKDAPIVILDEPTAALDIdselavqKAIDHlVHNRtviIIAHRlstIAGAG----------------NILVMEEGEVV 558
Cdd:COG3845  417 LSRDPKLLIAAQPTRGLDV-------GAIEF-IHQR---LLELR---DAGAAvllisedldeilalsdRIAVMYEGRIV 481

PRK15064

ABC transporter ATP-binding protein; Provisional

353-571

1.95e-05

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.95e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 353 YDDsgDPALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISiggvdirhlTAEqlNSLISVVFQDVWL-F 431
Cdd:PRK15064 329 FDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK---------WSE--NANIGYYAQDHAYdF 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 432 DDTLlaNLLIARPQATQQE-VEEAARAAqclefISRLpqgwLTPMGEMGGQ---LSGGERQRISIARALLKDAPIVILDE 507
Cdd:PRK15064 396 ENDL--TLFDWMSQWRQEGdDEQAVRGT-----LGRL----LFSQDDIKKSvkvLSGGEKGRMLFGKLMMQKPNVLVMDE 464

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 508 PTAALDIDSELAVQKAIDHlvHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVE-QGTHAQLLSRQG 571
Cdd:PRK15064 465 PTNHMDMESIESLNMALEK--YEGTLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRSQG 528

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

361-568

2.12e-05

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 2.12e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTFPAASMSALVGASGAGKTTvskLLMRYADPQQGEISIGGVDIR---HLTAEQLNSLisvvfqdvwlfDDTLLA 437
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKST---LLKALAGDLTGGGAPRGARVTgdvTLNGEPLAAI-----------DAPRLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NLLIARPQATQQEVEEAARAaqcLEFISRLPQ----------------------GWLTPMGEMGGQLSGGERQRISIARA 495
Cdd:PRK13547  83 RLRAVLPQAAQPAFAFSARE---IVLLGRYPHarragalthrdgeiawqalalaGATALVGRDVTTLSGGELARVQFARV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 496 LLK---------DAPIVILDEPTAALDIDSELAVQKAIDHLVH--NRTVIIIAHRLSTIA-GAGNILVMEEGEVVEQGTH 563
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAP 239


                 ....*
gi 515713280 564 AQLLS 568
Cdd:PRK13547 240 ADVLT 244

ABC_6TM_exporter_like

cd18563

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

36-321

2.29e-05

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 46.73 E-value: 2.29e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  36 ALLLAALMQGIAFACLYP------IVDALLRGEASPLLTWALVFSATAFAALALRWYGLGFeYRGHL-----AQATHELR 104
Cdd:cd18563    1 LILGFLLMLLGTALGLVPpyltkiLIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGI-LRGRLlarlgERITADLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 105 LRLGEQLRRVPLERLQRGRAGEtnalLLGSV--D-ENLNYVIA------IANILLLTIVtpltaSLATLWIDWRLGLVML 175
Cdd:cd18563   80 RDLYEHLQRLSLSFFDKRQTGS----LMSRVtsDtDRLQDFLSdglpdfLTNILMIIGI-----GVVLFSLNWKLALLVL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 176 LIFPMLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGS-DGEKSRALLAHFNALESlQSRTHRQSAGA 254
Cdd:cd18563  151 IPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQeKREIKRFDEANQELLDA-NIRAEKLWATF 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 255 TMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISYTSVVELIASALQRI 321
Cdd:cd18563  230 FPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

480-568

2.33e-05

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 2.33e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQLSGGERQRISIARALLKDAPIVILDEPTAALDI--DSElavqkaIDHLVHN-----RTVIIIAHRLSTIAG-AGNILV 551
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgaKHE------IYNVIYElaaqgVAVLFVSSDLPEVLGvADRIVV 468

                         90       100
                 ....*....|....*....|..
gi 515713280 552 MEEGEVV-----EQGTHAQLLS 568
Cdd:PRK11288 469 MREGRIAgelarEQATERQALS 490

PRK00635

excinuclease ABC subunit A; Provisional

474-550

2.39e-05

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.39e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  474 PMGEMGGQLSGGERQRISIARALL---KDAPIVILDEPTAAL---DIDSELAVQKAIDHLVHnrTVIIIAHRLSTIAGAG 547
Cdd:PRK00635  802 PLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGH--TVVIIEHNMHVVKVAD 879


                  ...
gi 515713280  548 NIL 550
Cdd:PRK00635  880 YVL 882

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

452-568

2.52e-05

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 2.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  452 EEAARAAQCL-EFISRLP------QGWLTPmGEMGGQLSGGERQRISIARALLKDAPIV--ILDEPTAAL-DIDSElavq 521
Cdd:TIGR00630 453 EEKKIAEEVLkEIRERLGflidvgLDYLSL-SRAAGTLSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLhQRDNR---- 527

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280  522 KAIDHLVHNR----TVIIIAHRLSTIAGAGNILVM------EEGEVVEQGTHAQLLS 568
Cdd:TIGR00630 528 RLINTLKRLRdlgnTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILA 584

ABC_6TM_Sav1866_like

cd18554

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

92-321

3.35e-05

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: 46.26 E-value: 3.35e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  92 YRGHLAQAT-----HELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWI 166
Cdd:cd18554   65 YRQYFAQWIankilYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 167 DWRLGLVMLLIFP---MLVPFYYWR-RPAMRRQMQTLGEAHQRLSgdivEFAQGMMVLRTCGSDGEKSRALLAHFNALES 242
Cdd:cd18554  145 NPKLTFVSLVIFPfyiLAVKYFFGRlRKLTKERSQALAEVQGFLH----ERIQGMSVIKSFALEKHEQKQFDKRNGHFLT 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 243 LQSRTHRQSAGATMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFI-SYTSVVELIASaLQRI 321
Cdd:cd18554  221 RALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVnSFTTLTQSFAS-MDRV 299

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

461-561

4.16e-05

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 4.16e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 461 LEFISRLPQGWLTpMGEMGGQLSGGERQRISIARAL---LKDApIVILDEPTAAL---DIdselavQKAIDHLVHNR--- 531
Cdd:cd03270  118 LGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLhprDN------DRLIETLKRLRdlg 189

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515713280 532 -TVIIIAHRLSTIAGAGNILVM------EEGEVVEQG 561
Cdd:cd03270  190 nTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226

ABC_6TM_Rv0194_D2_like

cd18546

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

34-222

4.57e-05

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: 45.56 E-value: 4.57e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  34 MIALLLAALMQGIAFACL--YPIVDALLRGEASPLLTWALVFSATAFAALALRWygLGFEYRGHLAQA-THELRLRLGEQ 110
Cdd:cd18546    4 ALLLVVVDTAASLAGPLLvrYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQR--AQTRLTGRTGERlLYDLRLRVFAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 111 LRRVPLERLQRGRAGETNALLLGSVDenlnyviAIANIL-------LLTIVTPLTASLATLWIDWRLGLVMLLIFPMLVP 183
Cdd:cd18546   82 LQRLSLDFHERETSGRIMTRMTSDID-------ALSELLqtglvqlVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515713280 184 FYYWRRpamRRQMQTLGEAHQRLSGDIVEFAQGMMVLRT 222
Cdd:cd18546  155 ATRWFR---RRSSRAYRRARERIAAVNADLQETLAGIRV 190

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

361-538

5.00e-05

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 5.00e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 361 LNNLSLTF-PAASMsALVGASGAGKTTVSKLLMRYADPQQGE------ISIG--------------------GV-DIRHL 412
Cdd:PRK11819  23 LKDISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVGylpqepqldpektvrenveeGVaEVKAA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 413 TAEqLNSlISVVFQDVWLFDDTLLANlliarpQATQQEVEEAA----------RAAQCLefisRLPqgwltPMGEMGGQL 482
Cdd:PRK11819 102 LDR-FNE-IYAAYAEPDADFDALAAE------QGELQEIIDAAdawdldsqleIAMDAL----RCP-----PWDAKVTKL 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 483 SGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKaidHLV-HNRTVIIIAH 538
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ---FLHdYPGTVVAVTH 218

PRK01156

chromosome segregation protein; Provisional

482-538

1.24e-04

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.24e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713280 482 LSGGERQ------RISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRT----VIIIAH 538
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISH 868

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

461-539

1.27e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.27e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   461 LEFISRLPQGWLTPMGemggQLSGGERQRISIA--RALL--KDAPIVILDEPTAALDidseLAVQKAIDHLVHNRT---- 532
Cdd:pfam02463 1061 IEISARPPGKGVKNLD----LLSGGEKTLVALAliFAIQkyKPAPFYLLDEIDAALD----DQNVSRVANLLKELSknaq 1132


                   ....*..
gi 515713280   533 VIIIAHR 539
Cdd:pfam02463 1133 FIVISLR 1139

PRK13543

heme ABC exporter ATP-binding protein CcmA;

378-515

1.60e-04

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.30 E-value: 1.60e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 378 GASGAGKTTVSKLLMRYADPQQGEISIGGVDIRhlTAEQLN-----SLISVVFQDVWLFDDTLLANLLIARpqatqqeve 452
Cdd:PRK13543  44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRfmaylGHLPGLKADLSTLENLHFLCGLHGR--------- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713280 453 eaaRAAQclefisrLPQGWLTPMGEMG------GQLSGGERQRISIARALLKDAPIVILDEPTAALDID 515
Cdd:PRK13543 113 ---RAKQ-------MPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171

PLN03140

ABC transporter G family member; Provisional

325-541

1.89e-04

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  325 MALPPLPVAergemperydIRFDTICYRYD------DSGDPA-----LNNLSLTFPAASMSALVGASGAGKTTVSKLLM- 392
Cdd:PLN03140  859 MVLPFTPLA----------MSFDDVNYFVDmpaemkEQGVTEdrlqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAg 928

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  393 -RYADPQQGEISIGGVDIRHLT-------AEQlNSLIS--VVFQDVWLFDdtllANLLIARPQATQQ------EVEEAAR 456
Cdd:PLN03140  929 rKTGGYIEGDIRISGFPKKQETfarisgyCEQ-NDIHSpqVTVRESLIYS----AFLRLPKEVSKEEkmmfvdEVMELVE 1003

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  457 AAQCLEFISRLPqgwltpmGEMGgqLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVII 535
Cdd:PLN03140 1004 LDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVVC 1074


                  ....*.
gi 515713280  536 IAHRLS 541
Cdd:PLN03140 1075 TIHQPS 1080

ABC_6TM_MsbA_like

cd18552

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

33-258

2.36e-04

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: 43.56 E-value: 2.36e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  33 SMIALLLAALMQGIAFACLYPIVDALLRGEASPLLTW--ALVFSATAFAALALRWYGLGFEYRGHlaQATHELRLRLGEQ 110
Cdd:cd18552    4 AILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLvpLAIIGLFLLRGLASYLQTYLMAYVGQ--RVVRDLRNDLFDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 111 LRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILL---LTIVTpLTASLatLWIDWRLGLVMLLIFP-MLVPFYY 186
Cdd:cd18552   82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdpLTVIG-LLGVL--FYLDWKLTLIALVVLPlAALPIRR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 187 WRRP---AMRRQMQTLGEAHQRLSgdivEFAQGMMVLRT-CGSDGEKSRAlLAHFNALESLQSRTHRQSAGATMLI 258
Cdd:cd18552  159 IGKRlrkISRRSQESMGDLTSVLQ----ETLSGIRVVKAfGAEDYEIKRF-RKANERLRRLSMKIARARALSSPLM 229

UvrA

COG0178

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];

482-573

2.60e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.60e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 482 LSGGERQRISIARAL---LKDApIVILDEPTAAL---DIDselavqKAIDHLVHNR----TVIIIAHRLSTIA------- 544
Cdd:COG0178  486 LSGGEAQRIRLATQIgsgLVGV-LYVLDEPSIGLhqrDND------RLIETLKRLRdlgnTVIVVEHDEDTIRaadyiid 558

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515713280 545 ---GAGnilvmEE-GEVVEQGTHAQLL----SRQGRY 573
Cdd:COG0178  559 igpGAG-----EHgGEVVAQGTPEEILknpdSLTGQY 590

ABC_6TM_CydC

cd18585

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ...

100-261

2.99e-04

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD 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. 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: 350029 [Multi-domain] Cd Length: 290 Bit Score: 43.24 E-value: 2.99e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 100 THELRLRLGEQLRR------VPL--ERLQRGRAGETNALLLGSVD--ENLnYVIAIANILLLTIVTPLTaSLATLWIDWR 169
Cdd:cd18585   59 SHDATFRLLSNLRVwfyrklEPLapARLQKYRSGDLLNRIVADIDtlDNL-YLRVLSPPVVALLVILAT-ILFLAFFSPA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 170 LGLVMLLIFPM---LVP--FYYWRRPAMRRQMQTLGEahqrLSGDIVEFAQGMMVLRTCGSDGEKSRALLAHFNALESLQ 244
Cdd:cd18585  137 LALILLAGLLLagvVIPllFYRLGKKIGQQLVQLRAE----LRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQ 212

                        170       180
                 ....*....|....*....|
gi 515713280 245 SRTHRQSA---GATMLIAGV 261
Cdd:cd18585  213 RRLARLSGlsqALMILLSGL 232

PLN03073

ABC transporter F family; Provisional

481-538

3.01e-04

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.01e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515713280 481 QLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIdhLVHNRTVIIIAH 538
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399

PLN03073

ABC transporter F family; Provisional

357-557

4.03e-04

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 4.03e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 357 GDPAL-NNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQG------EISIGGVDIRHLTAEQLNSlisvvfqdvw 429
Cdd:PLN03073 520 GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGtvfrsaKVRMAVFSQHHVDGLDLSS---------- 589

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 430 lfddTLLANLLIARPQATQQEVeeaaraaqclefisRLPQGWLTPMGEMGGQ----LSGGERQRISIARALLKDAPIVIL 505
Cdd:PLN03073 590 ----NPLLYMMRCFPGVPEQKL--------------RAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLL 651

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515713280 506 DEPTAALDIDselAVQKAIDHLV-HNRTVIIIAHRLSTIAGAGNIL-VMEEGEV 557
Cdd:PLN03073 652 DEPSNHLDLD---AVEALIQGLVlFQGGVLMVSHDEHLISGSVDELwVVSEGKV 702

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

480-559

4.39e-04

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 4.39e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHN-RTVIIIAHRLSTI-AGAGNILVMEEGEV 557
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIiTVCDRIAVFCEGRL 487


                 ..
gi 515713280 558 VE 559
Cdd:PRK09700 488 TQ 489

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

360-562

4.86e-04

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 41.99 E-value: 4.86e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGvdirhltaeQLNSLISV--VFQDvwlfDDTLLA 437
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSALLELgaGFHP----ELTGRE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 438 NL-LIAR-----PQATQQEVEEAARAAQCLEFISrlpqgwlTPMgemgGQLSGGERQRISIARALLKDAPIVILDEPTAA 511
Cdd:COG1134  108 NIyLNGRllglsRKEIDEKFDEIVEFAELGDFID-------QPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 512 LDIDselAVQKAIDHL----VHNRTVIIIAHRLSTIAG-AGNILVMEEGEVVEQGT 562
Cdd:COG1134  177 GDAA---FQKKCLARIrelrESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229

ABC_SMC_barmotin

cd03278

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...

482-557

5.47e-04

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).

Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 5.47e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 482 LSGGERQRISIAR--ALL--KDAPIVILDEPTAALDiDSELA-VQKAIDHLVHNRTVIIIAHRLSTIAGAGNIL--VMEE 554
Cdd:cd03278  114 LSGGEKALTALALlfAIFrvRPSPFCVLDEVDAALD-DANVErFARLLKEFSKETQFIVITHRKGTMEAADRLYgvTMQE 192


                 ...
gi 515713280 555 GEV 557
Cdd:cd03278  193 SGV 195

PRK15064

ABC transporter ATP-binding protein; Provisional

359-538

5.90e-04

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 5.90e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 359 PALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIG-GVDIRHLTAEQL----NSLISVVFQ---DVWL 430
Cdd:PRK15064  15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQFafeeFTVLDTVIMghtELWE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 431 FD---DTLLANlliarPQATQqevEEAARAAQcLEfisrlpqgwlTPMGEMGG--------------------------Q 481
Cdd:PRK15064  95 VKqerDRIYAL-----PEMSE---EDGMKVAD-LE----------VKFAEMDGytaearagelllgvgipeeqhyglmsE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713280 482 LSGGERQRISIARALLKDAPIVILDEPTAALDIDSelavqkaIDHLVH-----NRTVIIIAH 538
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT-------IRWLEDvlnerNSTMIIISH 210

40850658_otr

NF000106

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

455-571

7.64e-04

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 7.64e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 455 ARAAQCLEFISRLPQGwltpmGEMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLVHNRTVI 534
Cdd:NF000106 123 ARADELLERFSLTEAA-----GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 515713280 535 IIAHRLSTIAG--AGNILVMEEGEVVEQGTHAQLLSRQG 571
Cdd:NF000106 198 LLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

482-541

7.68e-04

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: 42.43 E-value: 7.68e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  482 LSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLvhNRTVIIIAHRLS 541
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

466-544

7.85e-04

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 7.85e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 466 RLPQGWLTPMGeMGGQ--------LSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVII- 535
Cdd:PRK10938 379 KLAQQWLDILG-IDKRtadapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLf 457

                         90       100
                 ....*....|....*....|
gi 515713280 536 -----------IAHRLSTIA 544
Cdd:PRK10938 458 vshhaedapacITHRLEFVP 477

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

360-571

9.31e-04

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 9.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDI---RHLTAEQ-------------LNSLISV 423
Cdd:NF033858  16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadaRHRRAVCpriaympqglgknLYPTLSV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 424 vFQDVWLFddtllANLLIARPQATQQEVEEAARAAQCLEFISRlpqgwltPMGemggQLSGGERQRISIARALLKDAPIV 503
Cdd:NF033858  96 -FENLDFF-----GRLFGQDAAERRRRIDELLRATGLAPFADR-------PAG----KLSGGMKQKLGLCCALIHDPDLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 504 ILDEPTAALDIDS-----ELavqkaIDHLVHNR---TVIII------AHRLSTIAgagnilVMEEGEVVEQGTHAQLLSR 569
Cdd:NF033858 159 ILDEPTTGVDPLSrrqfwEL-----IDRIRAERpgmSVLVAtaymeeAERFDWLV------AMDAGRVLATGTPAELLAR 227


                 ..
gi 515713280 570 QG 571
Cdd:NF033858 228 TG 229

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

360-543

1.13e-03

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.13e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 360 ALNNLSLTFPAASMSALVGASGAGKTTVSKLLMRYADPQQGEISIGGVDIRHLTAEQLNSLISVVfqdvwlfDDTLLANL 439
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-------ENIELKGL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 440 LIArpqATQQEVEEAarAAQCLEFisrlpqgwlTPMGEMGGQ----LSGGERQRISIARALLKDAPIVILDEptaALDID 515
Cdd:PRK13545 112 MMG---LTKEKIKEI--IPEIIEF---------ADIGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDE---ALSVG 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 515713280 516 SELAVQKAIDHL----VHNRTVIIIAHRLSTI 543
Cdd:PRK13545 175 DQTFTKKCLDKMnefkEQGKTIFFISHSLSQV 206

ABC_membrane

pfam00664

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

34-212

1.31e-03

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: 41.09 E-value: 1.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   34 MIALLLAALMQGIA-------FACLYPIVDALLRGEASPLLTWALVFSATAFAALALRWygLGFEYRGHLAQ-ATHELRL 105
Cdd:pfam00664   1 LILAILLAILSGAIspafplvLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSF--LQSYLLNHTGErLSRRLRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  106 RLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPMLVPFY 185
Cdd:pfam00664  79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158

                         170       180
                  ....*....|....*....|....*..
gi 515713280  186 YWRRPAMRRQMQTLGEAHQRLSGDIVE 212
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEE 185

PRK10636

putative ABC transporter ATP-binding protein; Provisional

483-538

1.58e-03

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 1.58e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515713280 483 SGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHlvHNRTVIIIAH 538
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS--YQGTLILISH 204

ABC_6TM_TmrB_like

cd18541

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

35-222

1.58e-03

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: 40.86 E-value: 1.58e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  35 IALLLAALMQgiafacLYP------IVDALLRGEASPlltWALVFSATAFAALALRWYGLGFEYRGHLAQA----THELR 104
Cdd:cd18541    6 LFLILVDLLQ------LLIpriigrAIDALTAGTLTA---SQLLRYALLILLLALLIGIFRFLWRYLIFGAsrriEYDLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 105 LRLGEQLRRVPLERLQRGRAGETNALL---LGSVDENLNY-VIAIANILLLTIVTPLtaslATLWIDWRLGLVMLLIFPM 180
Cdd:cd18541   77 NDLFAHLLTLSPSFYQKNRTGDLMARAtndLNAVRMALGPgILYLVDALFLGVLVLV----MMFTISPKLTLIALLPLPL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515713280 181 LVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRT 222
Cdd:cd18541  153 LALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKA 194

PRK11147

ABC transporter ATPase component; Reviewed

482-516

1.92e-03

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 1.92e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515713280 482 LSGGERQRISIARALLKDAPIVILDEPTAALDIDS 516
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191

GguA

NF040905

sugar ABC transporter ATP-binding protein;

480-558

2.72e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.72e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 480 GQLSGGERQRISIARALLKDAPIVILDEPTAALDIDSELAVQKAIDHLV-HNRTVIIIAHRLSTIAG-AGNILVMEEGEV 557
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELPELLGmCDRIYVMNEGRI 482


                 .
gi 515713280 558 V 558
Cdd:NF040905 483 T 483

ABC_6TM_exporter_like

cd18550

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

35-321

3.41e-03

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 39.77 E-value: 3.41e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280  35 IALLLAALMQGIAFACLYPIV------DALLRGEASpLLTWALVFSATAFAALALrwYGLGFEYR-GHLAQA-THELRLR 106
Cdd:cd18550    1 LALVLLLILLSALLGLLPPLLlreiidDALPQGDLG-LLVLLALGMVAVAVASAL--LGVVQTYLsARIGQGvMYDLRVQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 107 LGEQLRRVPLERLQRGRAGETNALLlgsvdenLNYVIAIANIL---LLTIVTPLTASLATL----WIDWRLGLVMLLIfp 179
Cdd:cd18550   78 LYAHLQRMSLAFFTRTRTGEIQSRL-------NNDVGGAQSVVtgtLTSVVSNVVTLVATLvamlALDWRLALLSLVL-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 180 mlVPFYYW--------RRPAMRRQMQTLGEahqrLSGDIVEF--AQGMMVLRTCGSDGEKSRALLAHFNALESLQSRTHR 249
Cdd:cd18550  149 --LPLFVLptrrvgrrRRKLTREQQEKLAE----LNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQAL 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 250 QSAGATMLIAGVVELGLQVVVLAGVVWVVTGTLNLAFLIAAAAMIMRFSEPMAMFISytSVVELIASA--LQRI 321
Cdd:cd18550  223 AGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLN--IQVDLMTSLalFERI 294

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

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

102-182

4.33e-03

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: 39.39 E-value: 4.33e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280 102 ELRLRLGEQLRRVPLERLQRGRAGETNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPML 181
Cdd:cd18576   70 DLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVV 149


                 .
gi 515713280 182 V 182
Cdd:cd18576  150 V 150

ABC_SMC_head

cd03239

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...

472-540

4.65e-03

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.

Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.44 E-value: 4.65e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 472 LTPMGEMGGQLSGGERQRISIARAL----LKDAPIVILDEPTAALDIDSELAVQKAI-DHLVHNRTVIIIAHRL 540
Cdd:cd03239   85 LVLQGKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIkEMAKHTSQFIVITLKK 158

ABC_SMC2_euk

cd03273

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...

469-531

4.96e-03

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).

Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 39.20 E-value: 4.96e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515713280 469 QGWLTPMGEMGG-------QLSGGERQRI--SIARALL--KDAPIVILDEPTAALDidseLAVQKAIDHLVHNR 531
Cdd:cd03273  147 QGRITKVLNMGGvwkesltELSGGQRSLValSLILALLlfKPAPMYILDEVDAALD----LSHTQNIGRMIKTH 216

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

370-561

6.79e-03

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 6.79e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   370 AASMSALVGASGAGKTTVSKLLM----RYADPQQGEISIGGVD----IRHLTAEQL-NSLISVVFQDVWLFDdTLLANLL 440
Cdd:TIGR00956   86 PGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITpeeiKKHYRGDVVyNAETDVHFPHLTVGE-TLDFAAR 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   441 IARPQATQQEVEEAARAAQCLEFISR---LPQGWLTPMG-EMGGQLSGGERQRISIARALLKDAPIVILDEPTAALDIDS 516
Cdd:TIGR00956  165 CKTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 515713280   517 ELAVQKAIDHLVH--NRTVIIIAHRLSTIAGA--GNILVMEEGEVVEQG 561
Cdd:TIGR00956  245 ALEFIRALKTSANilDTTPLVAIYQCSQDAYElfDKVIVLYEGYQIYFG 293

SMC_prok_B

TIGR02168

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

481-554

8.53e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 8.53e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713280   481 QLSGGERQRISIARA----LLKDAPIVILDEPTAALDidsELAVQ---KAIDHLVHNRTVIIIAHRLSTIAGAGNIL--V 551
Cdd:TIGR02168 1089 LLSGGEKALTALALLfaifKVKPAPFCILDEVDAPLD---DANVErfaNLLKEFSKNTQFIVITHNKGTMEVADQLYgvT 1165


                   ...
gi 515713280   552 MEE 554
Cdd:TIGR02168 1166 MQE 1168

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