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Conserved domains on  [gi|162312131|ref|NP_588371|]
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vacuolar phytochelatin and glutathione S-conjugate ABC family transmembrane transporter Hmt1 [Schizosaccharomyces pombe]

Protein Classification

ABCB family ABC transporter ATP-binding protein/permease( domain architecture ID 11474391)

ABCB family ABC transporter ATP-binding protein/permease ontains both the ATPase catalytic subunit and transmembrane (TM) component of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates; such as mitochondrial iron-sulfur clusters transporter ATM1

CATH:  3.40.50.300|1.20.1560.10
EC:  7.-.-.-
Gene Ontology:  GO:0140359|GO:0042626|GO:0005524|GO:0016887
PubMed:  24638992|25750732
SCOP:  4003976
TCDB:  3.A.1.210

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 229-828 0e+00

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: 681.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 229 STSKKPSDKSWAEYFRSFSTLLPYLWPTKDYRLQFQIFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILF 308
Cdd:COG5265    2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 309 VIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTAL---TKG-SSLNTFaeqVVFQ 384
Cdd:COG5265   82 LAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIergTKGiEFLLRF---LLFN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 385 IGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRE--SYAVqnDAIMNFETVKNFDA 462
Cdd:COG5265  159 ILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEanTRAV--DSLLNYETVKYFGN 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 463 DDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFG 542
Cdd:COG5265  237 EAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 543 TLYRSLQNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGG 622
Cdd:COG5265  317 FVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAG 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 623 KSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDR 702
Cdd:COG5265  397 KSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDF 476

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 703 ILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTI 782
Cdd:COG5265  477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 162312131 783 TNADLILCISNGRIVETGTHEELIKRdGGAYKKMWFQQAMGKTSAE 828
Cdd:COG5265  557 VDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEE 601
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 229-828 0e+00

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: 681.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 229 STSKKPSDKSWAEYFRSFSTLLPYLWPTKDYRLQFQIFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILF 308
Cdd:COG5265    2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 309 VIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTAL---TKG-SSLNTFaeqVVFQ 384
Cdd:COG5265   82 LAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIergTKGiEFLLRF---LLFN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 385 IGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRE--SYAVqnDAIMNFETVKNFDA 462
Cdd:COG5265  159 ILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEanTRAV--DSLLNYETVKYFGN 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 463 DDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFG 542
Cdd:COG5265  237 EAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 543 TLYRSLQNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGG 622
Cdd:COG5265  317 FVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAG 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 623 KSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDR 702
Cdd:COG5265  397 KSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDF 476

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 703 ILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTI 782
Cdd:COG5265  477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 162312131 783 TNADLILCISNGRIVETGTHEELIKRdGGAYKKMWFQQAMGKTSAE 828
Cdd:COG5265  557 VDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEE 601
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 584-820 2.26e-154

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: 450.53  E-value: 2.26e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVV 663
Cdd:cd03253    1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIIL 743
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 744 LDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRdGGAYKKMWFQQ 820
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWKAQ 236
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
339-810 9.84e-112

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 353.11  E-value: 9.84e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 339 AISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSS------LNTFAEQVVFQIGPVLLdLGVAmvyFFIKFDIYFTLIVL 412
Cdd:PRK13657  90 AVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDalfglwLEFMREHLATLVALVVL-LPLA---LFMNWRLSLVLVVL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 413 imtlcyCYVTVKITSW---RTEARRKMVNSWRESYAVQ-NDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSL 488
Cdd:PRK13657 166 ------GIVYTLITTLvmrKTKDGQAAVEEHYHDLFAHvSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWW 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 489 NFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGD---FVILLTYMIQ-LQQPLNFFGTLYRSlqnsiidTERLLEIFE- 563
Cdd:PRK13657 240 ALASVLNRAASTITMLAILVLGAALVQKGQLRVGEvvaFVGFATLLIGrLDQVVAFINQVFMA-------APKLEEFFEv 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 564 --EKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSI 641
Cdd:PRK13657 313 edAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 642 TIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKL 721
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 722 SGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGT 801
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552


                 ....*....
gi 162312131 802 HEELIKRDG 810
Cdd:PRK13657 553 FDELVARGG 561
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 242-810 3.10e-106

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: 338.23  E-value: 3.10e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  242 YFRSFSTLLPYLWptkdyrlqfqIFICIVLLFLGRAVN------ILAPrqlgVLTEKLTKHSEKIPWSdVILFVIYRFLQ 315
Cdd:TIGR02203   2 FRRLWSYVRPYKA----------GLVLAGVAMILVAATestlaaLLKP----LLDDGFGGRDRSVLWW-VPLVVIGLAVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  316 gnMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKGS----SLNTFAEQVVFQIGPVLLD 391
Cdd:TIGR02203  67 --RGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvaSAATDAFIVLVRETLTVIG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  392 LGVAMVYFfikfDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYG 471
Cdd:TIGR02203 145 LFIVLLYY----SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  472 HAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNS 551
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRG 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  552 IIDTERLLEIFEEKPTVVEKPNAPDlKVTqGKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRIL 630
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKDTGTRAIE-RAR-GDVEFRNVTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  631 LRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPS-ATNEEIYAAAKAAQIHDRILQFPDG 709
Cdd:TIGR02203 379 PRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLG 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  710 YNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLIL 789
Cdd:TIGR02203 459 LDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIV 538

                         570       580
                  ....*....|....*....|.
gi 162312131  790 CISNGRIVETGTHEELIKRDG 810
Cdd:TIGR02203 539 VMDDGRIVERGTHNELLARNG 559
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 265-538 9.66e-48

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: 170.90  E-value: 9.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKA 344
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  345 LRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAMVYFFIkFDIYFTLIVLIMTLCYCYVTV 423
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDtSKIRDGLGEKLGLLFQSLATIVGGIIVMFY-YGWKLTLVLLAVLPLYILVSA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  424 KITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSL 503
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 162312131  504 AIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPL 538
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
595-786 5.39e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 85.75  E-value: 5.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 595 PRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDqdirnvtlsslRSSIGVVPQDSTLfNDTI 674
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEV-PDSL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 lynikyakPsATNEEIYA-------------AAKAAQIHDRILQfpdgynsRVGERGL------KLSGGEKQRVAVARAI 735
Cdd:NF040873  71 --------P-LTVRDLVAmgrwarrglwrrlTRDDRAAVDDALE-------RVGLADLagrqlgELSGGQRQRALLAQGL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNAD 786
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRAD 186
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 609-797 1.76e-11

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: 62.78  E-value: 1.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   609 PGKVIALVGESGGGKSTIMRILLRFFDVNSGS-ITIDDQDIRNVTLSSLRssigvvpqdstlfndtilynikyakpsatn 687
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   688 eeiyaaakaaqihdrilqfpdgyNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAA----- 762
Cdd:smart00382  51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 162312131   763 -LNRLASGRTAIVIAHRLSTITNADLILCISNGRIV 797
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
GguA NF040905
sugar ABC transporter ATP-binding protein;
600-799 1.68e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 64.43  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNS--GSITIDDQDIRnvtLSSLRSS--IGVV---------PQD 666
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCR---FKDIRDSeaLGIViihqelaliPYL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 StlfndtILYNIKYAKPSATNEEI---YAAAKAAQIHDRI-LQfpDGYNSRVGERGLklsgGEKQRVAVARAILKDPSII 742
Cdd:NF040905  94 S------IAENIFLGNERAKRGVIdwnETNRRARELLAKVgLD--ESPDTLVTDIGV----GKQQLVEIAKALSKDVKLL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 743 LLDEATSALDtntERQIQAALNRL----ASGRTAIVIAHRLSTITN-ADLILCISNGRIVET 799
Cdd:NF040905 162 ILDEPTAALN---EEDSAALLDLLlelkAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
GguA NF040905
sugar ABC transporter ATP-binding protein;
594-797 8.87e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 594 DPRKPVLSDINFVAQPGKVIALVGESGGGKSTI-MRILLRFFDVN-SGSITIDDQ--DIRNVTlSSLRSSIGVVPQDST- 668
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKevDVSTVS-DAIDAGLAYVTEDRKg 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 669 ---LFNDTILYNIKYAKPSA--------TNEEIYAAAkaaqihdrilQFPDGYNSR---VGERGLKLSGGEKQRVAVARA 734
Cdd:NF040905 349 yglNLIDDIKRNITLANLGKvsrrgvidENEEIKVAE----------EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSKW 418

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRL-STITNADLILCISNGRIV 797
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELpELLGMCDRIYVMNEGRIT 483
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
692-811 1.30e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.11  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 692 AAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGR 770
Cdd:NF000106 121 ARARADELLERF-----SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGA 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 162312131 771 TAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRDGG 811
Cdd:NF000106 196 TVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGG 237
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 229-828 0e+00

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: 681.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 229 STSKKPSDKSWAEYFRSFSTLLPYLWPTKDYRLQFQIFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILF 308
Cdd:COG5265    2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 309 VIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTAL---TKG-SSLNTFaeqVVFQ 384
Cdd:COG5265   82 LAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIergTKGiEFLLRF---LLFN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 385 IGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRE--SYAVqnDAIMNFETVKNFDA 462
Cdd:COG5265  159 ILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEanTRAV--DSLLNYETVKYFGN 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 463 DDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFG 542
Cdd:COG5265  237 EAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 543 TLYRSLQNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGG 622
Cdd:COG5265  317 FVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAG 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 623 KSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDR 702
Cdd:COG5265  397 KSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDF 476

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 703 ILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTI 782
Cdd:COG5265  477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 162312131 783 TNADLILCISNGRIVETGTHEELIKRdGGAYKKMWFQQAMGKTSAE 828
Cdd:COG5265  557 VDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEE 601
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
240-823 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 547.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 240 AEYFRSFSTLLPYLWPtkdYRLQFqiFICIVLLFLGRAVNILAPRQLGVLTEKLTKHS--EKIPWSDVILFVIYrFLQGn 317
Cdd:COG1132    3 KSPRKLLRRLLRYLRP---YRGLL--ILALLLLLLSALLELLLPLLLGRIIDALLAGGdlSALLLLLLLLLGLA-LLRA- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 318 mgVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAM 396
Cdd:COG1132   76 --LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDvDAVEQFLAHGLPQLVRSVVTLIGAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 397 VYFFIkFDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDI 476
Cdd:COG1132  154 VVLFV-IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 477 YLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTE 556
Cdd:COG1132  233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 557 RLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDV 636
Cdd:COG1132  313 RIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 637 NSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGE 716
Cdd:COG1132  393 TSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 717 RGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRI 796
Cdd:COG1132  473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552

                        570       580
                 ....*....|....*....|....*..
gi 162312131 797 VETGTHEELIKRdGGAYKKMWFQQAMG 823
Cdd:COG1132  553 VEQGTHEELLAR-GGLYARLYRLQFGE 578
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 584-820 2.26e-154

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: 450.53  E-value: 2.26e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVV 663
Cdd:cd03253    1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIIL 743
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 744 LDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRdGGAYKKMWFQQ 820
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWKAQ 236
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
 268-558 2.38e-143

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.


Pssm-ID: 350027 [Multi-domain]  Cd Length: 290  Bit Score: 424.25  E-value: 2.38e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 268 CIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQgNMGVIGSLRSFLWVPVSQYAYRAISTKALRH 347
Cdd:cd18583    1 CFLCLLAERVLNVLVPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQ-SGGGLGLLRSWLWIPVEQYSYRALSTAAFNH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 348 VLNLSYDFHLNKRAGEVLTALTKGSSLNTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKITS 427
Cdd:cd18583   80 VMNLSMDFHDSKKSGEVLKAIEQGSSINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 428 WRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIAC 507
Cdd:cd18583  160 WRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLILTLGLLAGC 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162312131 508 LLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18583  240 FLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 244-821 2.44e-137

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: 424.25  E-value: 2.44e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 244 RSFSTLLPYLWPTKdyRLQFQIFICIVL---------LFLGRAVNILAPRQ----LGVLtekltkhsekipwsdVILFVI 310
Cdd:COG2274  142 FGLRWFLRLLRRYR--RLLLQVLLASLLinllalatpLFTQVVIDRVLPNQdlstLWVL---------------AIGLLL 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 311 YRFLQGnmgVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALtkgSSLNTFAEQVVFQIGPVLL 390
Cdd:COG2274  205 ALLFEG---LLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF---RDVESIREFLTGSLLTALL 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 391 DLGVAMVYFFIKF--DIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENE 468
Cdd:COG2274  279 DLLFVLIFLIVLFfySPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 469 RYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSL 548
Cdd:COG2274  359 RWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRF 438

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 549 QNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIM 627
Cdd:COG2274  439 QDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 628 RILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFP 707
Cdd:COG2274  519 KLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALP 598

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 708 DGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADL 787
Cdd:COG2274  599 MGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678

                        570       580       590
                 ....*....|....*....|....*....|....
gi 162312131 788 ILCISNGRIVETGTHEELIKRDgGAYKKMWFQQA 821
Cdd:COG2274  679 IIVLDKGRIVEDGTHEELLARK-GLYAELVQQQL 711
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
 268-558 4.73e-117

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.


Pssm-ID: 350004 [Multi-domain]  Cd Length: 292  Bit Score: 356.53  E-value: 4.73e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 268 CIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALRH 347
Cdd:cd18560    1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 348 VLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKIT 426
Cdd:cd18560   81 LHSLSLDWHLSKKTGEVVRIMDRGtESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVFTIKVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 427 SWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIA 506
Cdd:cd18560  161 EWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 507 CLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18560  241 LLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 584-820 2.71e-116

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: 352.23  E-value: 2.71e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRK--PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIG 661
Cdd:cd03249    1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSI 741
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDgGAYKKMWFQQ 820
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKAQ 238
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 584-817 1.94e-115

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: 349.99  E-value: 1.94e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRK-PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGV 662
Cdd:cd03251    1 VEFKNVTFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSII 742
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 743 LLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRdGGAYKKMW 817
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
339-810 9.84e-112

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 353.11  E-value: 9.84e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 339 AISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSS------LNTFAEQVVFQIGPVLLdLGVAmvyFFIKFDIYFTLIVL 412
Cdd:PRK13657  90 AVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDalfglwLEFMREHLATLVALVVL-LPLA---LFMNWRLSLVLVVL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 413 imtlcyCYVTVKITSW---RTEARRKMVNSWRESYAVQ-NDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSL 488
Cdd:PRK13657 166 ------GIVYTLITTLvmrKTKDGQAAVEEHYHDLFAHvSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWW 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 489 NFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGD---FVILLTYMIQ-LQQPLNFFGTLYRSlqnsiidTERLLEIFE- 563
Cdd:PRK13657 240 ALASVLNRAASTITMLAILVLGAALVQKGQLRVGEvvaFVGFATLLIGrLDQVVAFINQVFMA-------APKLEEFFEv 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 564 --EKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSI 641
Cdd:PRK13657 313 edAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 642 TIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKL 721
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 722 SGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGT 801
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552


                 ....*....
gi 162312131 802 HEELIKRDG 810
Cdd:PRK13657 553 FDELVARGG 561
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 582-810 1.39e-106

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: 326.87  E-value: 1.39e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIG 661
Cdd:cd03254    1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSI 741
Cdd:cd03254   81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDG 810
Cdd:cd03254  161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 242-810 3.10e-106

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: 338.23  E-value: 3.10e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  242 YFRSFSTLLPYLWptkdyrlqfqIFICIVLLFLGRAVN------ILAPrqlgVLTEKLTKHSEKIPWSdVILFVIYRFLQ 315
Cdd:TIGR02203   2 FRRLWSYVRPYKA----------GLVLAGVAMILVAATestlaaLLKP----LLDDGFGGRDRSVLWW-VPLVVIGLAVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  316 gnMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKGS----SLNTFAEQVVFQIGPVLLD 391
Cdd:TIGR02203  67 --RGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvaSAATDAFIVLVRETLTVIG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  392 LGVAMVYFfikfDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYG 471
Cdd:TIGR02203 145 LFIVLLYY----SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  472 HAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNS 551
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRG 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  552 IIDTERLLEIFEEKPTVVEKPNAPDlKVTqGKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRIL 630
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKDTGTRAIE-RAR-GDVEFRNVTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  631 LRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPS-ATNEEIYAAAKAAQIHDRILQFPDG 709
Cdd:TIGR02203 379 PRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLG 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  710 YNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLIL 789
Cdd:TIGR02203 459 LDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIV 538

                         570       580
                  ....*....|....*....|.
gi 162312131  790 CISNGRIVETGTHEELIKRDG 810
Cdd:TIGR02203 539 VMDDGRIVERGTHNELLARNG 559
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 347-816 3.39e-104

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: 333.21  E-value: 3.39e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  347 HVLNLSYDFHLNKRAGEVLTALTK---------GSSLNTFAEQVVFQIGPVLLdlgvaMVYFFIKFDIYFTLIVLIMTLC 417
Cdd:TIGR02204 100 HLISLSPSFFDKNRSGEVVSRLTTdttllqsviGSSLSMALRNALMCIGGLIM-----MFITSPKLTSLVLLAVPLVLLP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  418 YCYVTVKITSWRTEARRKMVNSwrESYAvqNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKvlfSLNFLNIVQGG 497
Cdd:TIGR02204 175 ILLFGRRVRKLSRESQDRIADA--GSYA--GETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQ---RIRTRALLTAI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  498 IFTFSL-AIACLL--SAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERLLEIFEEKPTVVEKPNA 574
Cdd:TIGR02204 248 VIVLVFgAIVGVLwvGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHP 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  575 PDLKV-TQGKVIFSHVSFAY--DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV 651
Cdd:TIGR02204 328 KTLPVpLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  652 TLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAV 731
Cdd:TIGR02204 408 DPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAI 487

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  732 ARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRdGG 811
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK-GG 566


                  ....*
gi 162312131  812 AYKKM 816
Cdd:TIGR02204 567 LYARL 571
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 449-810 5.23e-103

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: 329.41  E-value: 5.23e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 449 DAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLfSLNFLNIvqgGI--FTFSLAIAclLSAyrVTFGFNTVGD--- 523
Cdd:COG4988  202 DRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVL-RVAFLSS---AVleFFASLSIA--LVA--VYIGFRLLGGslt 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 524 -----FVILLT---YmiqlqQPLNFFGTLYRSLQNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDP 595
Cdd:COG4988  274 lfaalFVLLLApefF-----LPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPG 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTIL 675
Cdd:COG4988  349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIR 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNT 755
Cdd:COG4988  429 ENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 756 ERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDG 810
Cdd:COG4988  509 EAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
457-820 2.46e-92

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 301.94  E-value: 2.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 457 VKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLN-IVQggiFTFSLAIACLLsaYRVTF----GFNTVGDFVILLTYM 531
Cdd:PRK11176 217 VLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDpIIQ---LIASLALAFVL--YAASFpsvmDTLTAGTITVVFSSM 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 532 IQLQQPLNFFGTLYRSLQNSIIDTERLLEIFEEKPtvvEKPNAP-DLKVTQGKVIFSHVSFAYDPR-KPVLSDINFVAQP 609
Cdd:PRK11176 292 IALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ---EKDEGKrVIERAKGDIEFRNVTFTYPGKeVPALRNINFKIPA 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYA-KPSATNE 688
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSRE 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 689 EIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS 768
Cdd:PRK11176 449 QIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK 528

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 769 GRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDgGAYK---KMWFQQ 820
Cdd:PRK11176 529 NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN-GVYAqlhKMQFGQ 582
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 556-817 6.14e-92

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: 300.53  E-value: 6.14e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 556 ERLLEIFEEKPTVVEkPNAPDLKVTQGKVIFSHVSFAYDP-RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFF 634
Cdd:COG4987  307 RRLNELLDAPPAVTE-PAEPAPAPGGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 635 DVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRV 714
Cdd:COG4987  386 DPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWL 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 715 GERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNG 794
Cdd:COG4987  466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDG 545

                        250       260
                 ....*....|....*....|...
gi 162312131 795 RIVETGTHEELIKRDgGAYKKMW 817
Cdd:COG4987  546 RIVEQGTHEELLAQN-GRYRQLY 567
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
 268-556 1.09e-90

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 287.99  E-value: 1.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 268 CIVLLFLGRAVNILAPRQLGV----LTEKLTKHSEKIPWSDVILFVIYRFLQG----NMGVIGSLRSFLWVPVSQYAYRA 339
Cdd:cd18581    1 CLLLLAAGRVVNVLVPILYKKivdsLTPDSADSPLAFPWALILLYVFLKFLQGggsgSVGLLSNLRSFLWIPVQQFTTRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 340 ISTKALRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCY 418
Cdd:cd18581   81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGtSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 419 CYVTVKITSWRTEARRKM--VNSWRESYAVqnDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQG 496
Cdd:cd18581  161 LILTIIITEWRTKFRREMnkLDNEKRAKAV--DSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQN 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 497 GIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTE 556
Cdd:cd18581  239 LIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDME 298
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 584-820 3.90e-81

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: 260.50  E-value: 3.90e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKP-VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGV 662
Cdd:cd03252    1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSII 742
Cdd:cd03252   81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 743 LLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRdGGAYKKMWFQQ 820
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 338-816 6.45e-79

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 269.28  E-value: 6.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  338 RAISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSSL--NTFAEQVvfQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMT 415
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTmsRSLSLNV--NVLLRNLVMLLGLLGFMLWLSPRLTMVTLINL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  416 LCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLK-QERKVLFSLNFL--- 491
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQlNKRKALAYAGYLwtt 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  492 NIVQGGIFTFSLAIAcllsAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERLLEIFEEKPTVvek 571
Cdd:TIGR00958 392 SVLGMLIQVLVLYYG----GQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNI--- 464

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  572 PNAPDLKVT--QGKVIFSHVSFAY--DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQD 647
Cdd:TIGR00958 465 PLTGTLAPLnlEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP 544

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  648 IRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQ 727
Cdd:TIGR00958 545 LVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQ 624

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  728 RVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRlaSGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIK 807
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702


                  ....*....
gi 162312131  808 rDGGAYKKM 816
Cdd:TIGR00958 703 -DQGCYKHL 710
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 338-816 5.45e-77

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 264.11  E-value: 5.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  338 RAISTKALRHVLNLSYDFHLNKRAGEVLTALtkgSSLNTFAEQVVFQIGPVLLDLGVAMVYFFIKF--DIYFTLIVLIMT 415
Cdd:TIGR03796 227 VGMSARFLWHILRLPVRFFAQRHAGDIASRV---QLNDQVAEFLSGQLATTALDAVMLVFYALLMLlyDPVLTLIGIAFA 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  416 LCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKnfdADDFENERYGHAVDIY---LKQERKVLFSLNFLN 492
Cdd:TIGR03796 304 AINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLK---ASGLESDFFSRWAGYQaklLNAQQELGVLTQILG 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  493 IVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL-------LEIFEEK 565
Cdd:TIGR03796 381 VLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLddvlrnpVDPLLEE 460

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  566 PTVVEKPNAPDLKVtQGKVIFSHVSFAYDP-RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITID 644
Cdd:TIGR03796 461 PEGSAATSEPPRRL-SGYVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  645 DQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGG 724
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  725 EKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRlaSGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEE 804
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697

                         490
                  ....*....|..
gi 162312131  805 LIKRdGGAYKKM 816
Cdd:TIGR03796 698 LWAV-GGAYARL 708
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 584-795 1.10e-76

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: 245.76  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGV 662
Cdd:cd03228    1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFNDTILYNIkyakpsatneeiyaaakaaqihdrilqfpdgynsrvgerglkLSGGEKQRVAVARAILKDPSII 742
Cdd:cd03228   81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162312131 743 LLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGR 795
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 268-558 3.73e-74

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350026 [Multi-domain]  Cd Length: 292  Bit Score: 243.56  E-value: 3.73e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 268 CIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALRH 347
Cdd:cd18582    1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 348 VLNLSYDFHLNKRAGEVLTALTKGS-SLNTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKIT 426
Cdd:cd18582   81 LHSLSLRFHLSRKTGALSRAIERGTrGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAFTIKVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 427 SWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIA 506
Cdd:cd18582  161 EWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 507 CLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18582  241 MLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 402-814 1.81e-72

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: 248.65  E-value: 1.81e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  402 KFDIYFTLIVLIMTLCYCYVTvKITSWRTEARRKMVNSWRES-YAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQ 480
Cdd:TIGR01192 153 AMDWRLSIVLMVLGILYILIA-KLVMQRTKNGQAAVEHHYHNvFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  481 ERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTY---MI-QLQQplnffgtlYRSLQNSIIDTE 556
Cdd:TIGR01192 232 QYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFanlLIgRLDQ--------MSGFITQIFEAR 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  557 RLLEIF---EEKPTVVEKP-NAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLR 632
Cdd:TIGR01192 304 AKLEDFfdlEDSVFQREEPaDAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQR 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  633 FFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNS 712
Cdd:TIGR01192 384 VYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDT 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  713 RVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCIS 792
Cdd:TIGR01192 464 LVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLD 543

                         410       420
                  ....*....|....*....|..
gi 162312131  793 NGRIVETGTHEELIKRDGGAYK 814
Cdd:TIGR01192 544 QGRLIEKGSFQELIQKDGRFYK 565
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 582-800 6.41e-69

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: 227.09  E-value: 6.41e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPRK-PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSI 660
Cdd:cd03245    1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPS 740
Cdd:cd03245   81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETG 800
Cdd:cd03245  161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 582-801 4.80e-67

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: 221.98  E-value: 4.80e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSI 660
Cdd:cd03244    1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFNDTILYNIKyakP--SATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKD 738
Cdd:cd03244   81 SIIPQDPVLFSGTIRSNLD---PfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGT 801
Cdd:cd03244  158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 338-789 8.27e-67

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: 231.41  E-value: 8.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  338 RAISTKALRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQ-----IGPVLLdlgVAMVYFFikfDIYFTLIV 411
Cdd:TIGR02857  77 SQLRERLLEAVAALGPRWLQGRPSGELATLALEGvEALDGYFARYLPQlvlavIVPLAI---LAAVFPQ---DWISGLIL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  412 LImTLCYCYVTVKITSWRTEARRkmvnswRESYAVQN-------DAIMNFETVKNFDADDFENERYGHAVDIYLKQERKV 484
Cdd:TIGR02857 151 LL-TAPLIPIFMILIGWAAQAAA------RKQWAALSrlsghflDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRV 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  485 LfSLNFLNivqGGIFTFSLAIACLLSAyrVTFGFNTV--------GDFVILLT---YmiqlqQPLNFFGTLYRSLQNSII 553
Cdd:TIGR02857 224 L-RIAFLS---SAVLELFATLSVALVA--VYIGFRLLagdldlatGLFVLLLApefY-----LPLRQLGAQYHARADGVA 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  554 DTERLLEIFEEKPtVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRF 633
Cdd:TIGR02857 293 AAEALFAVLDAAP-RPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  634 FDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSR 713
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTP 451

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131  714 VGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLIL 789
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 581-796 5.76e-66

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 219.26  E-value: 5.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 581 QGKVIFSHVSFAYdPRKP---VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLR 657
Cdd:cd03248    9 KGIVKFQNVTFAY-PTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 658 SSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILK 737
Cdd:cd03248   88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRI 796
Cdd:cd03248  168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
557-820 6.92e-66

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 229.98  E-value: 6.92e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 557 RLLEIFEEKPTVVEkpNAPDLKVTQGKVIFSHVSFAY-DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFD 635
Cdd:PRK10789 289 RIRAMLAEAPVVKD--GSEPVPEGRGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 636 VNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVG 715
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVG 446

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 716 ERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGR 795
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGH 526

                        250       260
                 ....*....|....*....|....*.
gi 162312131 796 IVETGTHEELIKRDGGaYKKMW-FQQ 820
Cdd:PRK10789 527 IAQRGNHDQLAQQSGW-YRDMYrYQQ 551
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 556-814 3.85e-64

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 225.47  E-value: 3.85e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 556 ERLLEIFEEKPTVvEKPNAPDLKVTQGKVIFSHVSFAYDPRK-PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFF 634
Cdd:PRK11160 312 RRINEITEQKPEV-TFPTTSTAAADQVSLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 635 DVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIhDRILQFPDGYNSRV 714
Cdd:PRK11160 391 DPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWL 469

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 715 GERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNG 794
Cdd:PRK11160 470 GEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNG 549

                        250       260
                 ....*....|....*....|
gi 162312131 795 RIVETGTHEELIKRDGGAYK 814
Cdd:PRK11160 550 QIIEQGTHQELLAQQGRYYQ 569
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 231-810 4.17e-64

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: 228.47  E-value: 4.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  231 SKKPSDKSWAEYFRSFSTLLPYLwpTKDYRLQFQIFICIVLLFLgraVNILAPRQLGVLTEKLTKHSEK--IPWSDVILF 308
Cdd:TIGR01193 129 SPTPEYKPIKEKENSLLKFIPLI--TRQKKLIVNIVIAAIIVTL---ISIAGSYYLQKIIDTYIPHKMMgtLGIISIGLI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  309 VIYRFLQgnmgVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSSLntfAEQVVFQIGPV 388
Cdd:TIGR01193 204 IAYIIQQ----ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSI---IDALASTILSL 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  389 LLDLG-VAMVYFFIKFDiYFTLIVLIMTLCYCYVTVKITSWRTeaRRKMVNSWRESYAVQNDAIMN----FETVKNFDAD 463
Cdd:TIGR01193 277 FLDMWiLVIVGLFLVRQ-NMLLFLLSLLSIPVYAVIIILFKRT--FNKLNHDAMQANAVLNSSIIEdlngIETIKSLTSE 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  464 DFENERYGHAVDIYLKQErkvlFSLNFLNIVQGGIFT---FSLAIACL-LSAYRVTFGFNTVGD---FVILLTYMIQlqq 536
Cdd:TIGR01193 354 AERYSKIDSEFGDYLNKS----FKYQKADQGQQAIKAvtkLILNVVILwTGAYLVMRGKLTLGQlitFNALLSYFLT--- 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  537 PLNFFGTLYRSLQNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALV 616
Cdd:TIGR01193 427 PLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIV 506

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  617 GESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYN-IKYAKPSATNEEIYAAAK 695
Cdd:TIGR01193 507 GMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENlLLGAKENVSQDEIWAACE 586

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  696 AAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASgRTAIVI 775
Cdd:TIGR01193 587 IAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFV 665

                         570       580       590
                  ....*....|....*....|....*....|....*
gi 162312131  776 AHRLSTITNADLILCISNGRIVETGTHEELIKRDG 810
Cdd:TIGR01193 666 AHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 556-808 8.66e-64

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: 224.24  E-value: 8.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 556 ERLLEIFEEKPTVVEKPnAPdlkvtQGKVIFSHVSFAYdP--RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRF 633
Cdd:COG4618  309 NELLAAVPAEPERMPLP-RP-----KGRLSVENLTVVP-PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 634 FDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIkyAK-PSATNEEIYAAAKAAQIHDRILQFPDGYNS 712
Cdd:COG4618  382 WPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDT 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 713 RVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLILCI 791
Cdd:COG4618  460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVL 539

                        250
                 ....*....|....*..
gi 162312131 792 SNGRIVETGTHEELIKR 808
Cdd:COG4618  540 RDGRVQAFGPRDEVLAR 556
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
501-821 2.70e-59

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 212.27  E-value: 2.70e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 501 FSLAIAC-LLsayrVTFGFNTVGDFVI-----LLTYMIQLQQPLNFFGTLYRSLQNSIIDTERlleIFEEKPTVVEKPNA 574
Cdd:PRK10790 259 FSALILCgLL----MLFGFSASGTIEVgvlyaFISYLGRLNEPLIELTTQQSMLQQAVVAGER---VFELMDGPRQQYGN 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 575 PDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLS 654
Cdd:PRK10790 332 DDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 655 SLRSSIGVVPQDSTLFNDTILYNIKYAKPsATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARA 734
Cdd:PRK10790 412 VLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDGGAYK 814
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQ 570


                 ....*..
gi 162312131 815 KMWFQQA 821
Cdd:PRK10790 571 MYQLQLA 577
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 546-779 1.15e-56

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 203.36  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  546 RSLQNSIIDTERLLEIFEEKPTV--VEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGK 623
Cdd:TIGR02868 295 QQLTRVRAAAERIVEVLDAAGPVaeGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  624 STIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRI 703
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWL 454

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131  704 LQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRL 779
Cdd:TIGR02868 455 RALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 536-816 5.71e-53

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 194.29  E-value: 5.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 536 QPLNFFGTLYRSLQNSIIDTERLLEIFE---EKPTVVEKPNAPDLKVT---QGKVIFSHVSfaydprKPVLSDINFVAQP 609
Cdd:PRK11174 302 QPLRDLGTFYHAKAQAVGAAESLVTFLEtplAHPQQGEKELASNDPVTieaEDLEILSPDG------KTLAGPLNFTLPA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILLRFFDVNsGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEE 689
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQ 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 690 IYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASG 769
Cdd:PRK11174 455 LQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR 534

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 162312131 770 RTAIVIAHRLSTITNADLILCISNGRIVETGTHEELiKRDGGAYKKM 816
Cdd:PRK11174 535 QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL-SQAGGLFATL 580
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 389-815 7.54e-52

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 197.17  E-value: 7.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  389 LLDLG-VAMVYFFIKFDIYFtLIVLIMTLCYC-----------YVTVKITSWRT------EARRKMVNSWRESYAVQND- 449
Cdd:PTZ00265  937 LLKTGlVNNIVIFTHFIVLF-LVSMVMSFYFCpivaavltgtyFIFMRVFAIRArltankDVEKKEINQPGTVFAYNSDd 1015

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  450 ------------AIMNFETVKNFDADDFENERYGHAVDIYLK-QERKVLFSLNFLNIVQGGIFtFSLAIACLLSAYRVTF 516
Cdd:PTZ00265 1016 eifkdpsfliqeAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKgQKRKTLVNSMLWGFSQSAQL-FINSFAYWFGSFLIRR 1094

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  517 GFNTVGDFV-ILLTYMiqlqqplnFFGTLYRSLQNSIIDTERLLEIFEEK-PTVVEKPNA----------PDLKVTQGKV 584
Cdd:PTZ00265 1095 GTILVDDFMkSLFTFL--------FTGSYAGKLMSLKGDSENAKLSFEKYyPLIIRKSNIdvrdnggiriKNKNDIKGKI 1166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  585 IFSHVSFAY--DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDV-------------------------- 636
Cdd:PTZ00265 1167 EIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgde 1246

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  637 ----------------------------NSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNE 688
Cdd:PTZ00265 1247 eqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATRE 1326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  689 EIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL-- 766
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkd 1406

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 162312131  767 ASGRTAIVIAHRLSTITNADLILCISN----GRIVET-GTHEELIKRDGGAYKK 815
Cdd:PTZ00265 1407 KADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVYKK 1460
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 580-801 7.61e-50

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: 174.52  E-value: 7.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 580 TQGKVIFSHVSFAYDPRKP-VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRS 658
Cdd:cd03369    3 EHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 659 SIGVVPQDSTLFNDTILYNI----KYakpsaTNEEIYAAAkaaqihdrilqfpdgynsRVGERGLKLSGGEKQRVAVARA 734
Cdd:cd03369   83 SLTIIPQDPTLFSGTIRSNLdpfdEY-----SDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARA 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGT 801
Cdd:cd03369  140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 218-827 5.46e-49

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 188.31  E-value: 5.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  218 SASTSNFGTLKSTSKKPSDKSWAEYFRSFST-----LLPY-LWPTKDYRLQFQIFICIVL------LFLGRAVNILAPRQ 285
Cdd:PTZ00265   12 NSGGGNLSIKDEVEKELNKKGTFELYKKIKTqkipfFLPFkCLPASHRKLLGVSFVCATIsggtlpFFVSVFGVIMKNMN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  286 LGvltekltkhsEKIpwSDVILFVIYrflqgnMGVIGSLRSFlwvpVSQYAYRAISTKALRhVLNLSY---------DFH 356
Cdd:PTZ00265   92 LG----------ENV--NDIIFSLVL------IGIFQFILSF----ISSFCMDVVTTKILK-TLKLEFlksvfyqdgQFH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  357 LNKrAGEVLTaltkgSSLNTFAEQVVFQIGPVLLDLgVAMVYFFIKFDIYFTLIVLIMTLCY-C-----YVTVKITSWRT 430
Cdd:PTZ00265  149 DNN-PGSKLT-----SDLDFYLEQVNAGIGTKFITI-FTYASAFLGLYIWSLFKNARLTLCItCvfpliYICGVICNKKV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  431 EARRK---MVNSwrESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYlkqeRKVLFSLNFLNIVQGGIFTfslaiAC 507
Cdd:PTZ00265  222 KINKKtslLYNN--NTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLY----SKYILKANFMESLHIGMIN-----GF 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  508 LLSAYRVTFGFNTVgdfvILLTYMIQlQQPLNFF----------GTLYRSLQNSII------------DTERLLEIFEEK 565
Cdd:PTZ00265  291 ILASYAFGFWYGTR----IIISDLSN-QQPNNDFhggsvisillGVLISMFMLTIIlpniteymksleATNSLYEIINRK 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  566 PTVVEKPNAPDLKVTQgKVIFSHVSFAYDPRKPV--LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITI 643
Cdd:PTZ00265  366 PLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  644 DD-QDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYA----------------------------------------- 681
Cdd:PTZ00265  445 NDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlnd 524

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  682 --KPSATNE--------------EIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLD 745
Cdd:PTZ00265  525 msNTTDSNEliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  746 EATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITNADLILCISN------------------------------ 793
Cdd:PTZ00265  605 EATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNrergstvdvdiigedptkdnkennnknnkd 684

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|.
gi 162312131  794 -----------------GRIVETGTHEELIKRDGGAYKKMWFQQAMGKTSA 827
Cdd:PTZ00265  685 dnnnnnnnnnnkinnagSYIIEQGTHDALMKNKNGIYYTMINNQKVSSKKS 735
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 265-538 9.66e-48

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: 170.90  E-value: 9.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKA 344
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  345 LRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAMVYFFIkFDIYFTLIVLIMTLCYCYVTV 423
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDtSKIRDGLGEKLGLLFQSLATIVGGIIVMFY-YGWKLTLVLLAVLPLYILVSA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  424 KITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSL 503
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 162312131  504 AIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPL 538
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 589-796 1.39e-47

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: 166.62  E-value: 1.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAY-DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDS 667
Cdd:cd03246    6 VSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 TLFNDTILYNIkyakpsatneeiyaaakaaqihdrilqfpdgynsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEA 747
Cdd:cd03246   86 ELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312131 748 TSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLILCISNGRI 796
Cdd:cd03246  124 NSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
PLN03232 PLN03232
ABC transporter C family member; Provisional
 196-816 1.57e-43

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 171.31  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  196 TEESNVNENAISQNPSTVQLGVS----ASTSNFGTLKSTSKKPSDK-----SWAEYFRsFSTLLPYLWptkdyrlqfQIF 266
Cdd:PLN03232  846 TQEVNTNDENILKLGPTVTIDVSernlGSTKQGKRGRSVLVKQEERetgiiSWNVLMR-YNKAVGGLW---------VVM 915

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  267 ICIVLLFLGRAVNILAPRQLGVLTEKLTKHSekipWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALR 346
Cdd:PLN03232  916 ILLVCYLTTEVLRVSSSTWLSIWTDQSTPKS----YSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  347 HVLNLSYDFHLNKRAGEVLTALTK---------GSSLNTFAEQVvFQIGPVLLDLGVAMVyffikfdIYFTLIVLIMTLC 417
Cdd:PLN03232  992 SILRAPMLFFHTNPTGRVINRFSKdigdidrnvANLMNMFMNQL-WQLLSTFALIGTVST-------ISLWAIMPLLILF 1063

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  418 Y-CYVTVKITSwrTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNI--- 493
Cdd:PLN03232 1064 YaAYLYYQSTS--REVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIrle 1141

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  494 VQGGIFTFSLAIACLLSAYRVT--FGF-NTVGdfvILLTYMIQLQQPLNffGTLYRS--LQNSIIDTERL---LEIFEEK 565
Cdd:PLN03232 1142 TLGGVMIWLTATFAVLRNGNAEnqAGFaSTMG---LLLSYTLNITTLLS--GVLRQAskAENSLNSVERVgnyIDLPSEA 1216

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  566 PTVVEKPNAPDLKVTQGKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITID 644
Cdd:PLN03232 1217 TAIIENNRPVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMID 1296

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  645 DQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKyakP-SATNE-EIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLS 722
Cdd:PLN03232 1297 DCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID---PfSEHNDaDLWEALERAHIKDVIDRNPFGLDAEVSEGGENFS 1373

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  723 GGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTH 802
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSP 1453

                         650
                  ....*....|....
gi 162312131  803 EELIKRDGGAYKKM 816
Cdd:PLN03232 1454 QELLSRDTSAFFRM 1467
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 584-795 1.60e-43

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: 156.48  E-value: 1.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPR----KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIddqdirnvtlsslRSS 659
Cdd:cd03250    1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDSTLFNDTILYNIKYAKPsaTNEEIYAAA-KAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKD 738
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFGKP--FDEERYEKViKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 739 PSIILLDEATSALDTNTERQI--QAALNRLASGRTAIVIAHRLSTITNADLILCISNGR 795
Cdd:cd03250  146 ADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 586-808 2.68e-43

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: 156.72  E-value: 2.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ 665
Cdd:COG1122    3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 --DSTLFNDTI-------LYNIKYAKpsatnEEIYAAAKAAqihdriLQfpdgynsRVGERGLK------LSGGEKQRVA 730
Cdd:COG1122   83 npDDQLFAPTVeedvafgPENLGLPR-----EEIRERVEEA------LE-------LVGLEHLAdrppheLSGGQKQRVA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTIT-NADLILCISNGRIVETGTHEELIKR 808
Cdd:COG1122  145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSD 224
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 586-800 2.93e-43

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: 154.78  E-value: 2.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSSIGVVP 664
Cdd:cd03247    3 INNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 665 QDSTLFNDTILYNIkyakpsatneeiyaaakaaqihdrilqfpdgynsrvgerGLKLSGGEKQRVAVARAILKDPSIILL 744
Cdd:cd03247   82 QRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 745 DEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETG 800
Cdd:cd03247  123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
586-796 5.63e-43

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 154.97  E-value: 5.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ 665
Cdd:COG4619    3 LEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFNDTILYNI----KYAKPSATNEEIYAAAKAAQIHDRILqfpdgyNSRVGErglkLSGGEKQRVAVARAILKDPSI 741
Cdd:COG4619   82 EPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPDV 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAH------RLstitnADLILCISNGRI 796
Cdd:COG4619  152 LLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 566-815 7.93e-43

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: 163.54  E-value: 7.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 566 PTVVEKPNAPDLKVTQGKVIFS--HVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSG 639
Cdd:COG1123  241 PRLGAARGRAAPAAAAAEPLLEvrNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 640 SITIDDQDIRNVT---LSSLRSSIGVVPQD--STLF-NDTILYNIkyAKPSatneEIYAAAKAAQIHDRILQF------- 706
Cdd:COG1123  321 SILFDGKDLTKLSrrsLRELRRRVQMVFQDpySSLNpRMTVGDII--AEPL----RLHGLLSRAERRERVAELlervglp 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 707 PDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITN 784
Cdd:COG1123  395 PDLADRYPHE----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRY 470

                        250       260       270
                 ....*....|....*....|....*....|..
gi 162312131 785 -ADLILCISNGRIVETGTHEELIKRDGGAYKK 815
Cdd:COG1123  471 iADRVAVMYDGRIVEDGPTEEVFANPQHPYTR 502
PLN03130 PLN03130
ABC transporter C family member; Provisional
 526-828 6.89e-42

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 166.07  E-value: 6.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  526 ILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL---LEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPR-KPVLS 601
Cdd:PLN03130 1177 LLLSYALNITSLLTAVLRLASLAENSLNAVERVgtyIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPElPPVLH 1256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIkya 681
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL--- 1333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  682 kpSATNE----EIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTER 757
Cdd:PLN03130 1334 --DPFNEhndaDLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131  758 QIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDGGAYKKMwfQQAMGKTSAE 828
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM--VQSTGAANAQ 1480
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 587-808 7.85e-42

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: 153.03  E-value: 7.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDP---RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVV 663
Cdd:COG1124    5 RNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTL-FN-----DTILynikyAKP------SATNEEIYAAAKAAQIHDRIL-QFPDgynsrvgerglKLSGGEKQRVA 730
Cdd:COG1124   85 FQDPYAsLHprhtvDRIL-----AEPlrihglPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIK 807
Cdd:COG1124  149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLreERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228


                 .
gi 162312131 808 R 808
Cdd:COG1124  229 G 229
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
586-798 8.68e-42

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 152.50  E-value: 8.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAY---DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRI---LLRffdVNSGSITIDDQDIRNVT---LSSL 656
Cdd:COG1136    7 LRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSereLARL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 657 R-SSIGVVPQDSTLFND-TILYNIKYA------KPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQR 728
Cdd:COG1136   84 RrRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 729 VAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITNADLILCISNGRIVE 798
Cdd:COG1136  153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 586-800 3.17e-41

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: 150.73  E-value: 3.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRK---PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSS 659
Cdd:cd03257    4 VKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDS-----------TLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRIL-QFPDgynsrvgerglKLSGGEKQ 727
Cdd:cd03257   84 IQMVFQDPmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnRYPH-----------ELSGGQRQ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 728 RVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03257  153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 584-809 4.92e-41

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 151.01  E-value: 4.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVtlsslRSSIGVV 663
Cdd:COG1121    7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTL---F----NDTILYNIKYAKP------SATNEEIYAAAKAAQIHDRIlqfpdgyNSRVGErglkLSGGEKQRVA 730
Cdd:COG1121   81 PQRAEVdwdFpitvRDVVLMGRYGRRGlfrrpsRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQRVL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTI-TNADLILCIsNGRIVETGTHEELIKR 808
Cdd:COG1121  150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEVLTP 228


                 .
gi 162312131 809 D 809
Cdd:COG1121  229 E 229
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
588-808 8.64e-41

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 149.83  E-value: 8.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGVVPQDS 667
Cdd:COG1131    5 GLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 TLFND-TILYNIKYA------KPSATNEEIYAAAKAAQIHDRIlqfpdgyNSRVGerglKLSGGEKQRVAVARAILKDPS 740
Cdd:COG1131   83 ALYPDlTVRENLRFFarlyglPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALLHDPE 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRLASGRTAIVIA-HRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:COG1131  152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 586-795 9.30e-41

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 148.77  E-value: 9.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVP 664
Cdd:cd03225    2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 665 Q--DSTLFNDTI-------LYNIKYAKpsatnEEIYAAAKAAqihdriLQfpdgynsRVGERGLK------LSGGEKQRV 729
Cdd:cd03225   82 QnpDDQFFGPTVeeevafgLENLGLPE-----EEIEERVEEA------LE-------LVGLEGLRdrspftLSGGQKQRV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 730 AVARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGR 795
Cdd:cd03225  144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 600-749 1.02e-40

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: 146.64  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFND-TILYNI 678
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131  679 KYAKPSATNEEIYAAAKAAQIHDRiLQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 407-813 1.27e-40

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: 162.04  E-value: 1.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   407 FTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDaddfENERYGHAVDIYLKQERKVLF 486
Cdd:TIGR00957 1107 AAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE----EQERFIHQSDLKVDENQKAYY 1182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   487 ----SLNFLNI----VQGGIFTFSlAIACLLSAYRVTFGFntVGdfvILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:TIGR00957 1183 psivANRWLAVrlecVGNCIVLFA-ALFAVISRHSLSAGL--VG---LSVSYSLQVTFYLNWLVRMSSEMETNIVAVERL 1256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   559 LEIFE---EKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFF 634
Cdd:TIGR00957 1257 KEYSEtekEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN 1336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   635 DVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKyAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRV 714
Cdd:TIGR00957 1337 ESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHEC 1415

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   715 GERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNG 794
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1495

                          410
                   ....*....|....*....
gi 162312131   795 RIVETGTHEELIKRDGGAY 813
Cdd:TIGR00957 1496 EVAEFGAPSNLLQQRGIFY 1514
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 586-796 1.62e-40

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: 148.41  E-value: 1.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAY---DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRN---VTLSSLR-S 658
Cdd:cd03255    3 LKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlseKELAAFRrR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 659 SIGVVPQDSTLFND-TILYNIKYAKPSATNEEIYAAAKAAQIHDRiLQFPDGYNSRVGErglkLSGGEKQRVAVARAILK 737
Cdd:cd03255   83 HIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELLER-VGLGDRLNHYPSE----LSGGQQQRVAIARALAN 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITNADLILCISNGRI 796
Cdd:cd03255  158 DPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 584-800 1.97e-40

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: 148.05  E-value: 1.97e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSslRSSIGVV 663
Cdd:cd03259    1 LELKGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLF-----NDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQfpdgyNSRVGErglkLSGGEKQRVAVARAILKD 738
Cdd:cd03259   78 FQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL-----NRYPHE----LSGGQQQRVALARALARE 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLS-TITNADLILCISNGRIVETG 800
Cdd:cd03259  149 PSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
586-798 4.01e-40

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 147.51  E-value: 4.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGV 662
Cdd:COG2884    4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRIGV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFND-TILYNIKYA------KPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAI 735
Cdd:COG2884   84 VFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIARAL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIA-HRLSTITNADL-ILCISNGRIVE 798
Cdd:COG2884  153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 586-795 5.00e-40

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: 144.69  E-value: 5.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYdPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ 665
Cdd:cd00267    2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 dstlfndtilynikyakpsatneeiyaaakaaqihdrilqfpdgynsrvgerglkLSGGEKQRVAVARAILKDPSIILLD 745
Cdd:cd00267   81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 746 EATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITNA-DLILCISNGR 795
Cdd:cd00267  106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 582-813 8.62e-39

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


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 145.05  E-value: 8.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSI 660
Cdd:cd03288   18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFNDTILYNIKYAKpSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPS 740
Cdd:cd03288   98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDGGAY 813
Cdd:cd03288  177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 588-806 1.06e-38

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


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 144.42  E-value: 1.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDS 667
Cdd:COG1120    6 NLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 TL-FN----DTIL-----YNIKYAKPSATNEEI-YAAAKAAQIH---DRilqfpdgynsRVGErglkLSGGEKQRVAVAR 733
Cdd:COG1120   85 PApFGltvrELVAlgrypHLGLFGRPSAEDREAvEEALERTGLEhlaDR----------PVDE----LSGGERQRVLIAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLstitN-----ADLILCISNGRIVETGTHEELI 806
Cdd:COG1120  151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHDL----NlaaryADRLVLLKDGRIVAQGPPEEVL 226
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 586-800 7.99e-38

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: 140.75  E-value: 7.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVtlsslRSSIGVVPQ 665
Cdd:cd03235    2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTL---FNDTI-------LYNIKYAKPSATNEEiyaAAKAAQIHDR--ILQFPDgynSRVGErglkLSGGEKQRVAVAR 733
Cdd:cd03235   76 RRSIdrdFPISVrdvvlmgLYGHKGLFRRLSKAD---KAKVDEALERvgLSELAD---RQIGE----LSGGQQQRVLLAR 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCIsNGRIVETG 800
Cdd:cd03235  146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 586-808 2.21e-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: 147.36  E-value: 2.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDP-RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN---SGSITIDDQDIRNVTLSSLRSSIG 661
Cdd:COG1123    7 VRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQD--STLFNDTILYNIKYA------KPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVAR 733
Cdd:COG1123   87 MVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAM 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:COG1123  156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 586-808 5.50e-37

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: 139.36  E-value: 5.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ 665
Cdd:cd03295    3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLF-NDTILYNI-------KYAKPsatneeiyaaakaaQIHDRILQF-------PDGYNSRVGErglKLSGGEKQRVA 730
Cdd:cd03295   83 QIGLFpHMTVEENIalvpkllKWPKE--------------KIRERADELlalvgldPAEFADRYPH---ELSGGQQQRVG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRL-STITNADLILCISNGRIVETGTHEELIK 807
Cdd:cd03295  146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225


                 .
gi 162312131 808 R 808
Cdd:cd03295  226 S 226
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 586-809 6.90e-37

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: 138.79  E-value: 6.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGV 662
Cdd:cd03261    3 LRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFND-TILYNI------KYAKPSATNEEIyAAAK--AAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVAR 733
Cdd:cd03261   82 LFQSGALFDSlTVFENVafplreHTRLSEEEIREI-VLEKleAVGLRGAEDLYPA-----------ELSGGMKKRVALAR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTI-TNADLILCISNGRIVETGTHEELIKRD 809
Cdd:cd03261  150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRASD 228
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 586-809 7.33e-37

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 138.57  E-value: 7.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGV 662
Cdd:COG1127    8 VRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFND-TILYNIKYA---KPSATNEEIYAAAKAAqihdriLQfpdgynsRVGERGLK------LSGGEKQRVAVA 732
Cdd:COG1127   87 LFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEK------LE-------LVGLPGAAdkmpseLSGGMRKRVALA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 733 RAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTI-TNADLILCISNGRIVETGTHEELIKRD 809
Cdd:COG1127  154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLASD 233
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 586-805 7.50e-37

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: 138.08  E-value: 7.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN-----SGSITIDDQDIR--NVTLSSLRS 658
Cdd:cd03260    3 LRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYdlDVDVLELRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 659 SIGVVPQDSTLFNDTILYNIKYA------KPSATNEEI-YAAAKAAQIHDRilqfpdgynsrVGER--GLKLSGGEKQRV 729
Cdd:cd03260   82 RVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDE-----------VKDRlhALGLSGGQQQRL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 730 AVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:cd03260  151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 586-805 1.06e-35

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: 135.39  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGV 662
Cdd:cd03256    3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFND-TILYNIKYAKPSATN-----------EEIYAAAKAAqihDRiLQFPDGYNSRVGErglkLSGGEKQRVA 730
Cdd:cd03256   83 IFQQFNLIERlSVLENVLSGRLGRRStwrslfglfpkEEKQRALAAL---ER-VGLLDKAYQRADQ----LSGGQQQRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTIT-NADLILCISNGRIVETGTHEEL 805
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 584-808 3.82e-35

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: 133.48  E-value: 3.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRK---PVLSDINFVAQPGKVIALVGESGGGKSTIMRiLLRFFDV-NSGSITIDDQDI---RNVTLSSL 656
Cdd:cd03258    2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTDLtllSGKELRKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 657 RSSIGVVPQDSTLFND-TILYNIKYAKpsatneEIyAAAKAAQIHDRILQFPD--GYNSRVGERGLKLSGGEKQRVAVAR 733
Cdd:cd03258   81 RRRIGMIFQHFNLLSSrTVFENVALPL------EI-AGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIAR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:cd03258  154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 587-796 4.85e-35

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: 130.98  E-value: 4.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGVVPQD 666
Cdd:cd03230    4 RNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFndtilynikyakPSATNEEIyaaakaaqihdrilqfpdgynsrvgergLKLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:cd03230   82 PSLY------------ENLTVREN----------------------------LKLSGGMKQRLALAQALLHDPELLILDE 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 747 ATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILCISNGRI 796
Cdd:cd03230  122 PTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 586-805 1.95e-34

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 135.23  E-value: 1.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI-------RNvtlsslrs 658
Cdd:COG3842    8 LENVSKRYGD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN-------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 659 sIGVVPQDSTLF-NDTILYNI----KYAKPSAtnEEIyaAAKAAQIHDRI-LqfpDGY-NSRVGErglkLSGGEKQRVAV 731
Cdd:COG3842   79 -VGMVFQDYALFpHLTVAENVafglRMRGVPK--AEI--RARVAELLELVgL---EGLaDRYPHQ----LSGGQQQRVAL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 732 ARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLS---TItnADLILCISNGRIVETGTHEEL 805
Cdd:COG3842  147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 584-795 2.46e-34

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 129.23  E-value: 2.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYdPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR--NVTLSSLRSSIG 661
Cdd:cd03229    1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLF-NDTILYNIKYAkpsatneeiyaaakaaqihdrilqfpdgynsrvgerglkLSGGEKQRVAVARAILKDPS 740
Cdd:cd03229   80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLS-TITNADLILCISNGR 795
Cdd:cd03229  121 VLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDeAARLADRVVVLRDGK 178
PTZ00243 PTZ00243
ABC transporter; Provisional
 567-816 2.91e-34

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 141.84  E-value: 2.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  567 TVVEKP-----NAPDLkVTQGKVIFSHVSFAYDPRKP-VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGS 640
Cdd:PTZ00243 1288 TVVIEPasptsAAPHP-VQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGE 1366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  641 ITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKyakP--SATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERG 718
Cdd:PTZ00243 1367 IRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD---PflEASSAEVWAALELVGLRERVASESEGIDSRVLEGG 1443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  719 LKLSGGEKQRVAVARAILKDPS-IILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIV 797
Cdd:PTZ00243 1444 SNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVA 1523

                         250
                  ....*....|....*....
gi 162312131  798 ETGTHEELIKRDGGAYKKM 816
Cdd:PTZ00243 1524 EMGSPRELVMNRQSIFHSM 1542
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 584-799 4.15e-34

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: 130.28  E-value: 4.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAY---DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVtlsslRSSI 660
Cdd:cd03293    1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFN-DTILYNIKYAkpsatnEEIyAAAKAAQIHDRILQFPDgynsRVGERGLK------LSGGEKQRVAVAR 733
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALG------LEL-QGVPKAEARERAEELLE----LVGLSGFEnayphqLSGGMRQRVALAR 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLS-TITNADLILCISN--GRIVET 799
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 587-800 4.65e-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: 128.71  E-value: 4.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQd 666
Cdd:cd03214    3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 stlfndtilynikyakpsatneeIYAAAKAAQIHDRilqfpdGYNSrvgerglkLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:cd03214   81 -----------------------ALELLGLAHLADR------PFNE--------LSGGERQRVLLARALAQEPPILLLDE 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 747 ATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLstitN-----ADLILCISNGRIVETG 800
Cdd:cd03214  124 PTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDL----NlaaryADRVILLKDGRIVAQG 180
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 584-806 5.24e-34

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 130.50  E-value: 5.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI--RNVTLSSLRSSIG 661
Cdd:COG1126    2 IEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLFND-TILYNIKYA------KPSATNEEIyaaAKAA----QIHDRILQFPDgynsrvgerglKLSGGEKQRVA 730
Cdd:COG1126   81 MVFQQFNLFPHlTVLENVTLApikvkkMSKAEAEER---AMELlervGLADKADAYPA-----------QLSGGQQQRVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLS---TItnADLILCISNGRIVETGTHEELI 806
Cdd:COG1126  147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAkEGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFF 224
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 586-807 6.90e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 131.27  E-value: 6.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDP-RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVP 664
Cdd:PRK13632  10 VENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 665 QD-------STLFNDTI--LYNIKYaKPSATNEEIYAAAKAAQIHDRILQFPdgynsrvgergLKLSGGEKQRVAVARAI 735
Cdd:PRK13632  90 QNpdnqfigATVEDDIAfgLENKKV-PPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRLASGR--TAIVIAHRLSTITNADLILCISNGRIVETGTHEELIK 807
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 588-796 1.36e-33

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: 128.42  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRN--VTLSSLRSSIGVVPQ 665
Cdd:cd03262    5 NLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLF-NDTILYNIKYA------KPSATNEEI-YAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILK 737
Cdd:cd03262   84 QFNLFpHLTVLENITLApikvkgMSKAEAEERaLELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAM 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRI 796
Cdd:cd03262  153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 592-805 1.60e-31

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 122.93  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 592 AYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvtLSS---LRSSIGVVPQDST 668
Cdd:cd03224    8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG--LPPherARAGIGYVPEGRR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 669 LFND-TILYNIK---YAKPSATNEEIYaaakaaqihDRILQ-FPdgynsRVGER----GLKLSGGEKQRVAVARAILKDP 739
Cdd:cd03224   86 IFPElTVEENLLlgaYARRRAKRKARL---------ERVYElFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRP 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 740 SIILLDEATSALDTNTERQIQAALNRLASGRTAIVI----AHRLSTItnADLILCISNGRIVETGTHEEL 805
Cdd:cd03224  152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 599-808 1.94e-31

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: 122.83  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvtLSSLRSSIGVVPQDSTLF-NDTILYN 677
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFpHMTVYKN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 678 IKYAKPSATNEEIyaaakaaQIHDRILQFPD--GYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNT 755
Cdd:cd03299   92 IAYGLKKRKVDKK-------EIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 756 ERQIQAALNRL--ASGRTAIVIAHRLSTI-TNADLILCISNGRIVETGTHEELIKR 808
Cdd:cd03299  165 KEKLREELKKIrkEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 580-799 4.13e-31

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 122.89  E-value: 4.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 580 TQGKVIFSHVSFAYDPRK---PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRnvtlsSL 656
Cdd:COG1116    4 AAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 657 RSSIGVVPQDSTLFN-DTILYNIKYAKPSATneeiyaaAKAAQIHDRILQFPDgynsRVGergLK---------LSGGEK 726
Cdd:COG1116   79 GPDRGVVFQEPALLPwLTVLDNVALGLELRG-------VPKAERRERARELLE----LVG---LAgfedayphqLSGGMR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 727 QRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAH------RLstitnADLILCISN--GRI 796
Cdd:COG1116  145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRI 219


                 ...
gi 162312131 797 VET 799
Cdd:COG1116  220 VEE 222
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 602-806 1.00e-30

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: 121.98  E-value: 1.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRS-SIGVVPQDSTLF-NDTILY 676
Cdd:cd03294   42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLpHRTVLE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 NIKYA-----KPSATNEEiyAAAKAAQ---IHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:cd03294  122 NVAFGlevqgVPRAEREE--RAAEALElvgLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 749 SALDTNTERQIQAALNRLAS--GRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEELI 806
Cdd:cd03294  189 SALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 584-797 1.32e-30

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: 119.19  E-value: 1.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRIL--LRFFDVNSGSITIDDqdiRNVTLSSLRSSIG 661
Cdd:cd03213    9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLF-NDTILYNIKYAkpsatneeiyaaakaAQIhdrilqfpdgynsrvgeRGLklSGGEKQRVAVARAILKDPS 740
Cdd:cd03213   86 YVPQDDILHpTLTVRETLMFA---------------AKL-----------------RGL--SGGERKRVSIALELVSNPS 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLST--ITNADLILCISNGRIV 797
Cdd:cd03213  132 LLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
PLN03130 PLN03130
ABC transporter C family member; Provisional
 534-822 1.82e-30

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 129.86  E-value: 1.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  534 LQQPLNFFGTLYRSLQNSIIDTERLLEIF--EEK---PTVVEKPNAPDLKVTQGkvifshvSFAYDPR--KPVLSDINFV 606
Cdd:PLN03130  567 LRFPLFMLPNLITQAVNANVSLKRLEELLlaEERvllPNPPLEPGLPAISIKNG-------YFSWDSKaeRPTLSNINLD 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  607 AQPGKVIALVGESGGGK-STIMRILLRFFDVNSGSITIddqdirnvtlsslRSSIGVVPQDSTLFNDTILYNIKYAKPSA 685
Cdd:PLN03130  640 VPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFGSPFD 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  686 TNEEIYAAAKAAQIHDRILqFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQI-QAALN 764
Cdd:PLN03130  707 PERYERAIDVTALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIK 785

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131  765 RLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKrDGgaykkMWFQQAM 822
Cdd:PLN03130  786 DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG-----PLFQKLM 837
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 586-810 1.94e-30

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: 119.43  E-value: 1.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV---TLSSLRSSIGV 662
Cdd:cd03292    3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFNDTILYN-------IKYAKPSATNEEIYAAAKAAQIHDRILQFPDGynsrvgerglkLSGGEKQRVAVARAI 735
Cdd:cd03292   83 VFQDFRLLPDRNVYEnvafaleVTGVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAhrlstiTNADlilcisngRIVETGTHEELIKRDG 810
Cdd:cd03292  152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA------THAK--------ELVDTTRHRVIALERG 212
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 479-810 2.11e-30

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: 129.68  E-value: 2.11e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   479 KQERKVLFSLNFLNIVqgGIFTFS----LAIACLLSAYrVTFGFNTVGD----FVILLTYMIqLQQPLNFFGTLYRSLQN 550
Cdd:TIGR00957  527 QEELKVLKKSAYLHAV--GTFTWVctpfLVALITFAVY-VTVDENNILDaekaFVSLALFNI-LRFPLNILPMVISSIVQ 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   551 SIIDTERLlEIF----EEKPTVVEKPNapdLKVTQGKVIFSH-VSFAY---DPrkPVLSDINFVAQPGKVIALVGESGGG 622
Cdd:TIGR00957  603 ASVSLKRL-RIFlsheELEPDSIERRT---IKPGEGNSITVHnATFTWardLP--PTLNGITFSIPEGALVAVVGQVGCG 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   623 KSTIMRILLRFFDVNSGSITIddqdirnvtlsslRSSIGVVPQDSTLFNDTILYNIKYAKPsaTNEEIYAAA-KAAQIHD 701
Cdd:TIGR00957  677 KSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQVlEACALLP 741

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   702 RILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAAL---NRLASGRTAIVIAHR 778
Cdd:TIGR00957  742 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHG 821

                          330       340       350
                   ....*....|....*....|....*....|..
gi 162312131   779 LSTITNADLILCISNGRIVETGTHEELIKRDG 810
Cdd:TIGR00957  822 ISYLPQVDVIIVMSGGKISEMGSYQELLQRDG 853
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
586-808 2.12e-30

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 122.88  E-value: 2.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRK---PVLSDINFVAQPGKVIALVGESGGGKSTimriLLRFfdVN------SGSITIDDQDIrnVTLSS- 655
Cdd:COG1135    4 LENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRC--INllerptSGSVLVDGVDL--TALSEr 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 656 ----LRSSIGVVPQDSTLFND-TILYNIKYAKpsatneEIyAAAKAAQIHDRI---LQFpdgynsrVGERGLK------L 721
Cdd:COG1135   76 elraARRKIGMIFQHFNLLSSrTVAENVALPL------EI-AGVPKAEIRKRVaelLEL-------VGLSDKAdaypsqL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 722 SGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVE 798
Cdd:COG1135  142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221

                        250
                 ....*....|
gi 162312131 799 TGTHEELIKR 808
Cdd:COG1135  222 QGPVLDVFAN 231
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 586-808 4.51e-30

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 119.84  E-value: 4.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  586 FSHVSFAYDPR-KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV-TLSSLRSSIGVV 663
Cdd:TIGR04520   3 VENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKVGMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  664 PQDstlfndtilynikyakP-----SATNEEIYA------AAKAAQIHDRIlqfpDGYNSRVGERGLK------LSGGEK 726
Cdd:TIGR04520  83 FQN----------------PdnqfvGATVEDDVAfglenlGVPREEMRKRV----DEALKLVGMEDFRdrephlLSGGQK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  727 QRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITNADLILCISNGRIVETGTHEE 804
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222


                  ....
gi 162312131  805 LIKR 808
Cdd:TIGR04520 223 IFSQ 226
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 588-808 5.52e-30

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: 121.31  E-value: 5.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRK-PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN---SGSITIDDQDIRNVTLSSLRS----S 659
Cdd:COG0444    8 KVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDS-TLFN------DTILYNIKYAKPsATNEEIYAAAKaaqihdRILQfpdgynsRVG----ERGLK-----LSG 723
Cdd:COG0444   88 IQMIFQDPmTSLNpvmtvgDQIAEPLRIHGG-LSKAEARERAI------ELLE-------RVGlpdpERRLDrypheLSG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 724 GEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:COG0444  154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEG 233


                 ....*...
gi 162312131 801 THEELIKR 808
Cdd:COG0444  234 PVEELFEN 241
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 584-805 9.51e-30

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: 117.61  E-value: 9.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAY-DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGV 662
Cdd:cd03263    1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFND-TILYNIK-YAKPSATNEEIYAAAKAAQIhdRILQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPS 740
Cdd:cd03263   80 CPQFDALFDElTVREHLRfYARLKGLPKSEIKEEVELLL--RVLGLTDKANKRART----LSGGMKRKLSLAIALIGGPS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:cd03263  154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 588-805 1.60e-29

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 118.22  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN-----SGSITIDDQDI--RNVTLSSLRSSI 660
Cdd:COG1117   16 NLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVELRRRV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFNDTILYNIKYA------KPSATNEEIYAAA--KAA---QIHDRiLQfpdgynsrvgERGLKLSGGEKQRV 729
Cdd:COG1117   95 GMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlrKAAlwdEVKDR-LK----------KSALGLSGGQQQRL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 730 AVARAILKDPSIILLDEATSALD-TNTERqIQAALNRLASGRTaIVI-------AHRLStitnaDLILCISNGRIVETGT 801
Cdd:COG1117  164 CIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYT-IVIvthnmqqAARVS-----DYTAFFYLGELVEFGP 236


                 ....
gi 162312131 802 HEEL 805
Cdd:COG1117  237 TEQI 240
PLN03232 PLN03232
ABC transporter C family member; Provisional
 534-816 6.34e-29

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 124.70  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  534 LQQPLNFFGTLYRSLQNSIIDTERLLEIF--EEK---PTVVEKPNAPDLKVTQGkvifshvSFAYDPR--KPVLSDINFV 606
Cdd:PLN03232  567 LRSPLNMLPNLLSQVVNANVSLQRIEELLlsEERilaQNPPLQPGAPAISIKNG-------YFSWDSKtsKPTLSDINLE 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  607 AQPGKVIALVGESGGGKSTIMRILL-RFFDVNSGSITIddqdirnvtlsslRSSIGVVPQDSTLFNDTILYNIKYAKPSA 685
Cdd:PLN03232  640 IPVGSLVAIVGGTGEGKTSLISAMLgELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFE 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  686 TNEEIYAAAKAAQIHDRILqFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQI-QAALN 764
Cdd:PLN03232  707 SERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMK 785

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 162312131  765 RLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKrDGGAYKKM 816
Cdd:PLN03232  786 DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SGSLFKKL 836
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 582-805 7.83e-29

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 118.64  E-value: 7.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI-------RNvtls 654
Cdd:COG3839    2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 655 slrssIGVVPQDSTLF-------NdtILYNIKYAKPSAT--NEEIYAAAKAAQIHDrILqfpdgyNSRVGErglkLSGGE 725
Cdd:COG3839   77 -----IAMVFQSYALYphmtvyeN--IAFPLKLRKVPKAeiDRRVREAAELLGLED-LL------DRKPKQ----LSGGQ 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 726 KQRVAVARAILKDPSIILLDEATSALD----TNTERQIQAALNRLasGRTAIVIAHRLS---TItnADLILCISNGRIVE 798
Cdd:COG3839  139 RQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL--GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQ 214


                 ....*..
gi 162312131 799 TGTHEEL 805
Cdd:COG3839  215 VGTPEEL 221
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 584-805 8.15e-29

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 115.41  E-value: 8.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvtLSSLRSSIGVV 663
Cdd:cd03300    1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLFND-TILYNIKYA------KPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAIL 736
Cdd:cd03300   78 FQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEEL 805
Cdd:cd03300  147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 588-808 8.18e-29

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 118.33  E-value: 8.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRIL--LRFFDvnSGSITIDDQDIrNVTLSSLRSSIGVVPQ 665
Cdd:COG1118    7 NISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETPD--SGRIVLNGRDL-FTNLPPRERRVGFVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLF-NDTILYNIKYA----KPSAtneeiyaaakaAQIHDRILQFPDgynsRVGERGLK------LSGGEKQRVAVARA 734
Cdd:COG1118   83 HYALFpHMTVAENIAFGlrvrPPSK-----------AEIRARVEELLE----LVQLEGLAdrypsqLSGGQRQRVALARA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAH------RLstitnADLILCISNGRIVETGTHEELI 806
Cdd:COG1118  148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVY 222


                 ..
gi 162312131 807 KR 808
Cdd:COG1118  223 DR 224
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 588-797 8.79e-29

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: 114.28  E-value: 8.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvtlSSLRSSIGVVPQDS 667
Cdd:cd03226    4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 T--LFNDTILYNIKYAKP--SATNEEIYAAAKAAQIHDRILQFPdgynsrvgergLKLSGGEKQRVAVARAILKDPSIIL 743
Cdd:cd03226   81 DyqLFTDSVREELLLGLKelDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLI 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 744 LDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILCISNGRIV 797
Cdd:cd03226  150 FDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 584-800 3.19e-28

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: 113.06  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYdPRKPVLSDINFVAQPGkVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGVV 663
Cdd:cd03264    1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLFndtilynikyakPSATNEEI--YAAA----KAAQIHDRILQFPD--GYNSRVGERGLKLSGGEKQRVAVARAI 735
Cdd:cd03264   78 PQEFGVY------------PNFTVREFldYIAWlkgiPSKEVKARVDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQAL 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03264  146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
588-809 3.31e-28

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 115.11  E-value: 3.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAY-DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQD 666
Cdd:PRK13635  10 HISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 -------STLFNDTI--LYNIKYAKpsatnEEIYAAAKAAQIHDRILQFPDGYNSRvgerglkLSGGEKQRVAVARAILK 737
Cdd:PRK13635  90 pdnqfvgATVQDDVAfgLENIGVPR-----EEMVERVDQALRQVGMEDFLNREPHR-------LSGGQKQRVAIAGVLAL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRD 809
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 584-805 1.34e-26

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: 108.97  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYdPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSslRSSIGVV 663
Cdd:cd03296    3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLFND-TILYNIKY---AKPSATNEEiyAAAKAAQIHD--RILQFpDGYNSRVGErglKLSGGEKQRVAVARAILK 737
Cdd:cd03296   80 FQHYALFRHmTVFDNVAFglrVKPRSERPP--EAEIRAKVHEllKLVQL-DWLADRYPA---QLSGGQRQRVALARALAV 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEEL 805
Cdd:cd03296  154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
598-807 1.35e-26

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 114.73  E-value: 1.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT-LSSLRSSIGVVPQDSTLFND-TIL 675
Cdd:COG1129   18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNIKYAKPSATN-----EEIYAaaKAAQIHDRI-LQF-PDgynSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:COG1129   98 ENIFLGREPRRGglidwRAMRR--RARELLARLgLDIdPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 749 SALdtnTERQIQ---AALNRLASGRTAIV-IAHRLSTITN-ADLILCISNGRIVETG-----THEELIK 807
Cdd:COG1129  169 ASL---TEREVErlfRIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 598-799 1.37e-26

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: 106.74  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLS-SLRSSIGVVPQdstlfndtily 676
Cdd:cd03216   14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIAMVYQ----------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 nikyakpsatneeiyaaakaaqihdrilqfpdgynsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTE 756
Cdd:cd03216   83 --------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 162312131 757 RQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVET 799
Cdd:cd03216  119 ERLFKVIRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 596-804 1.68e-26

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 109.48  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTL-Fndti 674
Cdd:PRK13548  14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsF---- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 lynikyakpSATNEEIYA---------AAKAAQIHDRILQfpdgynsRVGERGLK------LSGGEKQRVAVARAIL--- 736
Cdd:PRK13548  90 ---------PFTVEEVVAmgraphglsRAEDDALVAAALA-------QVDLAHLAgrdypqLSGGEQQRVQLARVLAqlw 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 737 ---KDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLstitN-----ADLILCISNGRIVETGTHEE 804
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDL----NlaaryADRIVLLHQGRLVADGTPAE 227
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 591-794 4.85e-26

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: 107.03  E-value: 4.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 591 FAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSI----TIDDQDIRNVTLSSLRSSIGVVPQD 666
Cdd:cd03290    8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFNDTILYNIKYAKPsaTNEEIY-AAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLD 745
Cdd:cd03290   88 PWLLNATVEENITFGSP--FNKQRYkAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 746 EATSALDTN-TERQIQAALNRLASG--RTAIVIAHRLSTITNADLILCISNG 794
Cdd:cd03290  166 DPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 598-809 5.02e-26

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: 107.38  E-value: 5.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSL-RSSIGVVPQDSTLFND-TIL 675
Cdd:COG0410   17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNIK---YAKPSAtneeiyaaAKAAQIHDRILQ-FPdgynsRVGER----GLKLSGGEKQRVAVARAILKDPSIILLDEA 747
Cdd:COG0410   97 ENLLlgaYARRDR--------AEVRADLERVYElFP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 748 TSALDTNTERQIQAALNRLASGRTAIVI----AHRLSTItnADLILCISNGRIVETGTHEELIKRD 809
Cdd:COG0410  164 SLGLAPLIVEEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADP 227
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 599-822 7.66e-26

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 108.02  E-value: 7.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNsGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNI 678
Cdd:cd03289   19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 679 K-YAKPSatNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTER 757
Cdd:cd03289   98 DpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 758 QIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKrdggayKKMWFQQAM 822
Cdd:cd03289  176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN------EKSHFKQAI 234
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
587-806 8.17e-26

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 107.51  E-value: 8.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQD 666
Cdd:COG4559    5 ENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STL---FndtilynikyakpsaTNEEIYA---------AAKAAQIHDRILQfpdgynsRVGERGLK------LSGGEKQR 728
Cdd:COG4559   84 SSLafpF---------------TVEEVVAlgraphgssAAQDRQIVREALA-------LVGLAHLAgrsyqtLSGGEQQR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 729 VAVARAIL-------KDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLstitN-----ADLILCISNGR 795
Cdd:COG4559  142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARrGGGVVAVLHDL----NlaaqyADRILLLHQGR 217

                        250
                 ....*....|.
gi 162312131 796 IVETGTHEELI 806
Cdd:COG4559  218 LVAQGTPEEVL 228
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 568-823 8.46e-26

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: 114.62  E-value: 8.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   568 VVEKPNAPDLKVTQGKVIFSHVSFAY-DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNsGSITIDDQ 646
Cdd:TIGR01271 1202 VIENPHAQKCWPSGGQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGV 1280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   647 DIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIK-YAKPSatNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGE 725
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGH 1358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   726 KQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEEL 805
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438

                          250
                   ....*....|....*...
gi 162312131   806 IKrdggayKKMWFQQAMG 823
Cdd:TIGR01271 1439 LN------ETSLFKQAMS 1450
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 586-788 9.18e-26

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: 105.64  E-value: 9.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSSIGVVPQ 665
Cdd:COG4133    5 AENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFND-TILYNIKYA----KPSATNEEIYAAAKAAQIHDRIlqfpdgyNSRVGerglKLSGGEKQRVAVARAILKDPS 740
Cdd:COG4133   83 ADGLKPElTVRENLRFWaalyGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAP 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 162312131 741 IILLDEATSALDTNTERQIQAALNR-LASGRTAIVIAHRLSTITNADLI 788
Cdd:COG4133  152 LWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 602-800 1.02e-25

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: 105.84  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAqPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ---DIR-NVTLSSLRSSIGVVPQDSTLF-NDTILY 676
Cdd:cd03297   16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFpHLNVRE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 NIKYAKPSATNEEIyaAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTE 756
Cdd:cd03297   95 NLAFGLKRKRNRED--RISVDELLDLL-----GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162312131 757 RQIQAALNRLAS--GRTAIVIAHRLSTI-TNADLILCISNGRIVETG 800
Cdd:cd03297  168 LQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 584-800 1.36e-25

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: 105.41  E-value: 1.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVtlSSLRSSIGVV 663
Cdd:cd03301    1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLF-NDTILYNIKY------AKPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAIL 736
Cdd:cd03301   78 FQNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAH-RLSTITNADLILCISNGRIVETG 800
Cdd:cd03301  147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLqqRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 599-801 1.47e-25

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: 105.98  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRS-SIGVVPQDSTLF-NDT 673
Cdd:COG4181   27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLRArHVGFVFQSFQLLpTLT 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 674 ILYNIkyAKP----SATNeeiyAAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:COG4181  107 ALENV--MLPlelaGRRD----ARARARALLERV-----GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 750 ALDTNTERQIQA---ALNRlASGRTAIVIAHRLSTITNADLILCISNGRIVETGT 801
Cdd:COG4181  176 NLDAATGEQIIDllfELNR-ERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
cbiO PRK13640
energy-coupling factor transporter ATPase;
584-808 2.99e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 106.42  E-value: 2.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAY-DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRI---LLRFFDVNSGSITIDDQDIRNVTLSSLRSS 659
Cdd:PRK13640   6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQ--DSTLFNDTILYNIKYA---KPSATNEEIYAAAKA-AQIHdrILQFPDGYNSrvgerglKLSGGEKQRVAVAR 733
Cdd:PRK13640  86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVlADVG--MLDYIDSEPA-------NLSGGQKQRVAIAG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 594-800 4.21e-25

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: 103.99  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 594 DPRKPV--LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSlRSSIGVVPQDSTLFN 671
Cdd:cd03266   13 DVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRLGFVSDSTGLYD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 D-TILYNIKYakpsatneeiYAA---AKAAQIHDRI------LQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSI 741
Cdd:cd03266   92 RlTARENLEY----------FAGlygLKGDELTARLeeladrLGMEELLDRRVGG----FSTGMRQKVAIARALVHDPPV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03266  158 LLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 586-801 4.73e-25

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 107.19  E-value: 4.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYD-PRKPV--LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI---RNVTLSSLRSS 659
Cdd:PRK11153   4 LKNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKARRQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDstlFN----DTILYNIkyAKPSatneEIyAAAKAAQIHDRILQFPDgynsRVGERGLK------LSGGEKQRV 729
Cdd:PRK11153  84 IGMIFQH---FNllssRTVFDNV--ALPL----EL-AGTPKAEIKARVTELLE----LVGLSDKAdrypaqLSGGQKQRV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 730 AVARAILKDPSIILLDEATSALDTNTERQIQAAL---NRLAsGRTAIVIAHRLSTITN-ADLILCISNGRIVETGT 801
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLkdiNREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
584-806 5.13e-25

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 104.40  E-value: 5.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR--NVTLSSLRSSIG 661
Cdd:PRK09493   2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLFND-TILYNIKYAkP----SATNEEiyAAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAIL 736
Cdd:PRK09493  81 MVFQQFYLFPHlTALENVMFG-PlrvrGASKEE--AEKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
598-803 5.63e-25

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 104.32  E-value: 5.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILlRFFDV-NSGSITIDD------QDIRNVTLSSLRSSIGVVPQDSTLF 670
Cdd:COG4161   16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLETpDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQYNLW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 -NDTILYNIKYA--KPSATNEEIyAAAKAAQIHDRiLQFPDgYNSRVGergLKLSGGEKQRVAVARAILKDPSIILLDEA 747
Cdd:COG4161   95 pHLTVMENLIEApcKVLGLSKEQ-AREKAMKLLAR-LRLTD-KADRFP---LHLSGGQQQRVAIARALMMEPQVLLFDEP 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 748 TSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHE 803
Cdd:COG4161  169 TAALDPEITAQVVEIIRELSqTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 584-807 7.22e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 104.83  E-value: 7.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKP-VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGV 662
Cdd:PRK13648   8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQ--DSTLFNDTILYNIKYA--KPSATNEEIYaaakaaQIHDRILQFPDGYNSRVGERGlKLSGGEKQRVAVARAILKD 738
Cdd:PRK13648  88 VFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMH------RRVSEALKQVDMLERADYEPN-ALSGGQKQRVAIAGVLALN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRLASGR--TAIVIAHRLSTITNADLILCISNGRIVETGTHEELIK 807
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 593-788 7.51e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 104.47  E-value: 7.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 593 YDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN-----SGSITIDDQDI--RNVTLSSLRSSIGVVPQ 665
Cdd:PRK14239  14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFNDTILYNIKYA------KPSAT-NEEIYAAAKAAQIHDRIlqfpdgyNSRVGERGLKLSGGEKQRVAVARAILKD 738
Cdd:PRK14239  94 QPNPFPMSIYENVVYGlrlkgiKDKQVlDEAVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATS 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAH------RLSTIT----NADLI 788
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRsmqqasRISDRTgfflDGDLI 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 600-808 8.31e-25

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 106.35  E-value: 8.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGVVPQDStlfndtily 676
Cdd:COG4608   34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--------- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 nikYA--KPSATNEEIYAA-------AKAAQIHDRILQFPDgynsRVGergLK----------LSGGEKQRVAVARAILK 737
Cdd:COG4608  105 ---YAslNPRMTVGDIIAEplrihglASKAERRERVAELLE----LVG---LRpehadrypheFSGGQRQRIGIARALAL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 738 DPSIILLDEATSALDTNTERQIqaaLNRLAS-----GRTAIVIAHRLSTITNadlilcISN-------GRIVETGTHEEL 805
Cdd:COG4608  175 NPKLIVCDEPVSALDVSIQAQV---LNLLEDlqdelGLTYLFISHDLSVVRH------ISDrvavmylGKIVEIAPRDEL 245


                 ...
gi 162312131 806 IKR 808
Cdd:COG4608  246 YAR 248
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 599-803 1.13e-24

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 103.56  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITI-----------DDQDIRnvtlsSLRSSIGVVPQDS 667
Cdd:PRK11124  17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR-----ELRRNVGMVFQQY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 TLF-NDTILYNIKYA--KPSATNEEIyAAAKAAQIHDRI--LQFPDGYNsrvgergLKLSGGEKQRVAVARAILKDPSII 742
Cdd:PRK11124  92 NLWpHLTVQQNLIEApcRVLGLSKDQ-ALARAEKLLERLrlKPYADRFP-------LHLSGGQQQRVAIARALMMEPQVL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 743 LLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHE 803
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAeTGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 597-800 1.49e-24

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: 102.30  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvtLSSLRSSIGVVpqdstlfndtILY 676
Cdd:cd03268   13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL----------IEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 NIKYAKPSAtNEEIYAAAKAAQI----HDRILQfpdgynsRVGERGL------KLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:cd03268   81 PGFYPNLTA-RENLRLLARLLGIrkkrIDEVLD-------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 747 ATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03268  153 PTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 598-777 1.82e-24

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: 102.51  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDiRNVTLSSL---------RSSIG------- 661
Cdd:COG4778   25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLAQAspreilalrRRTIGyvsqflr 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLfnDTIlynikyAKP--SATNEEIYAAAKAAQIHDRiLQFPdgynsrvgERGLKL-----SGGEKQRVAVARA 734
Cdd:COG4778  104 VIPRVSAL--DVV------AEPllERGVDREEARARARELLAR-LNLP--------ERLWDLppatfSGGEQQRVNIARG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 162312131 735 ILKDPSIILLDEATSALD-TNTERQIQAALNRLASGRTAIVIAH 777
Cdd:COG4778  167 FIADPPLLLLDEPTASLDaANRAVVVELIEEAKARGTAIIGIFH 210
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 602-808 2.24e-24

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: 105.57  E-value: 2.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRI---LLRffdVNSGSITIDD---QDI-RNVTLSSLRSSIGVVPQDSTLFN--- 671
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPhls 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 --DTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:COG4148   94 vrGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 750 ALDTNTERQIQAALNRLASgRTAIVI---AH------RLstitnADLILCISNGRIVETGTHEELIKR 808
Cdd:COG4148  163 ALDLARKAEILPYLERLRD-ELDIPIlyvSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSR 224
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 584-805 2.72e-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: 103.78  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPrkpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITiddqdirnvtlSSLRssIGVV 663
Cdd:cd03291   40 LFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HSGR--ISFS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLFNDTILYNIKYAkpSATNEEIY-AAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSII 742
Cdd:cd03291  104 SQFSWIMPGTIKENIIFG--VSYDEYRYkSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 743 LLDEATSALDTNTERQI-QAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEEL 805
Cdd:cd03291  182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 265-558 6.64e-24

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: 102.63  E-value: 6.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAPRQLGVLTEKLT--KHSEKIPWSDVILFVIYrFLQGnmgVIGSLRSFLWVPVSQYAYRAIST 342
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVIpaGDLSLLLWIALLLLLLA-LLRA---LLSYLRRYLAARLGQRVVFDLRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 343 KALRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAMVYFFIkFDIYFTLIVLIMTLCYCYV 421
Cdd:cd07346   77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDvDAVQNLVSSGLLQLLSDVLTLIGALVILFY-LNWKLTLVALLLLPLYVLI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 422 TVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTF 501
Cdd:cd07346  156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 502 SLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd07346  236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
cbiO PRK13641
energy-coupling factor transporter ATPase;
586-807 6.93e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 102.60  E-value: 6.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPV----LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR----NVTLSSLR 657
Cdd:PRK13641   5 FENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 658 SSIGVVPQ--DSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRIlqfpdGYNSRVGERG-LKLSGGEKQRVAVARA 734
Cdd:PRK13641  85 KKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV-----GLSEDLISKSpFELSGGQMRRVAIAGV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQI-QAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIK 807
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
cbiO PRK13637
energy-coupling factor transporter ATPase;
589-807 8.00e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 102.43  E-value: 8.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI--RNVTLSSLRSSIGV 662
Cdd:PRK13637   8 LTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQ--DSTLFNDTILYNIKYAkPS---ATNEEIYAAAKAAQihdRILQFP-DGYNSRvgeRGLKLSGGEKQRVAVARAIL 736
Cdd:PRK13637  88 VFQypEYQLFEETIEKDIAFG-PInlgLSEEEIENRVKRAM---NIVGLDyEDYKDK---SPFELSGGQKRRVAIAGVVA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIK 807
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
603-809 1.00e-23

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 100.60  E-value: 1.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 603 INFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIrnvtlssLRSSIGVVP-----QDSTLFND-TILY 676
Cdd:COG3840   18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-------TALPPAERPvsmlfQENNLFPHlTVAQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 NIKYAKPSATNeeiYAAAKAAQIHDrILQfpdgynsRVGERGLK------LSGGEKQRVAVARAILKDPSIILLDEATSA 750
Cdd:COG3840   91 NIGLGLRPGLK---LTAEQRAQVEQ-ALE-------RVGLAGLLdrlpgqLSGGQRQRVALARCLVRKRPILLLDEPFSA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 751 LDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRD 809
Cdd:COG3840  160 LDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
cbiO PRK13646
energy-coupling factor transporter ATPase;
583-809 1.29e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 101.78  E-value: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 583 KVIFSHVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT----LS 654
Cdd:PRK13646   2 TIRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 655 SLRSSIGVVPQ--DSTLFNDTILYNIKYAkPSATNEEIYAAAKAAqiHDRILQFpdGYNSRVGERG-LKLSGGEKQRVAV 731
Cdd:PRK13646  82 PVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 732 ARAILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236


                 .
gi 162312131 809 D 809
Cdd:PRK13646 237 K 237
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 599-805 1.33e-23

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 100.59  E-value: 1.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI--------RNVTLSSLRSSIGVVPQDSTLF 670
Cdd:PRK11264  18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 -NDTILYNIkYAKPSATNEEIYAAAKAaqiHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:PRK11264  98 pHRTVLENI-IEGPVIVKGEPKEEATA---RARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 750 ALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
571-804 1.43e-23

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 103.49  E-value: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 571 KPNAPDLKVTQGKVI-FSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR 649
Cdd:PRK09452   1 SKKLNKQPSSLSPLVeLRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 650 NVtlSSLRSSIGVVPQDSTLFN-----DTILYNIKYAKPSatNEEIyaaakAAQIHD--RILQFPDGYNSRVgergLKLS 722
Cdd:PRK09452  80 HV--PAENRHVNTVFQSYALFPhmtvfENVAFGLRMQKTP--AAEI-----TPRVMEalRMVQLEEFAQRKP----HQLS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 723 GGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAH-RLSTITNADLILCISNGRIVET 799
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQD 226


                 ....*
gi 162312131 800 GTHEE 804
Cdd:PRK09452 227 GTPRE 231
PTZ00243 PTZ00243
ABC transporter; Provisional
 563-804 1.78e-23

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 107.17  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  563 EEKPTVVEKPNAPDLKVTQgkvifshvSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSIT 642
Cdd:PTZ00243  648 EATPTSERSAKTPKMKTDD--------FFELEP-KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW 718

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  643 IDdqdirnvtlsslrSSIGVVPQDSTLFNDTILYNIKYAKPSATnEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLS 722
Cdd:PTZ00243  719 AE-------------RSIAYVPQQAWIMNATVRGNILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLS 784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  723 GGEKQRVAVARAILKDPSIILLDEATSALDTNT-ERQIQAA-LNRLAsGRTAIVIAHRLSTITNADLILCISNGRIVETG 800
Cdd:PTZ00243  785 GGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECfLGALA-GKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863


                  ....
gi 162312131  801 THEE 804
Cdd:PTZ00243  864 SSAD 867
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 584-808 2.31e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 101.25  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI----RNVTLSS 655
Cdd:PRK13634   3 ITFQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 656 LRSSIGVVPQ--DSTLFNDTILYNIKYAkPS---ATNEEiyAAAKAAQIHDRIlqfpdGYNSRVGERG-LKLSGGEKQRV 729
Cdd:PRK13634  83 LRKKVGIVFQfpEHQLFEETVEKDICFG-PMnfgVSEED--AKQKAREMIELV-----GLPEELLARSpFELSGGQMRRV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 730 AVARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIF 234


                 ..
gi 162312131 807 KR 808
Cdd:PRK13634 235 AD 236
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 602-808 2.65e-23

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 104.77  E-value: 2.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDvNSGSITIDDQDIRNVT---LSSLRSSIGVVPQD--STLfndtily 676
Cdd:COG4172  304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfGSL------- 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 nikyaKPSATNEEIYA--------AAKAAQIHDRILQFpdgynsrVGERGLK----------LSGGEKQRVAVARAILKD 738
Cdd:COG4172  376 -----SPRMTVGQIIAeglrvhgpGLSAAERRARVAEA-------LEEVGLDpaarhrypheFSGGQRQRIAIARALILE 443

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTI-TNADLILCISNGRIVETGTHEELIKR 808
Cdd:COG4172  444 PKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQVFDA 516
cbiO PRK13650
energy-coupling factor transporter ATPase;
588-808 5.22e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 99.81  E-value: 5.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDP--RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ 665
Cdd:PRK13650   9 NLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 --DSTLFNDTILYNIKYA---KPSATNEEIYAAAKAAQIHDrILQFPDGYNSRvgerglkLSGGEKQRVAVARAILKDPS 740
Cdd:PRK13650  89 npDNQFVGATVEDDVAFGlenKGIPHEEMKERVNEALELVG-MQDFKEREPAR-------LSGGQKQRVAIAGAVAMRPK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 741 IILLDEATSALD-------TNTERQIqaalnRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK13650 161 IIILDEATSMLDpegrlelIKTIKGI-----RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 588-816 1.21e-22

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: 102.84  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFA-YDPRKPVLSDINFVAQPGKVIALVGESGGGKS----TIMRILLRFFDVNSGSITIDDQDIRNVTLSSLR----S 658
Cdd:COG4172   13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 659 SIGVVPQD-STLFNDtiLYNIkyakpsatnEE-------IYAAAKAAQIHDRILQFPDgynsRVG----ERGLK-----L 721
Cdd:COG4172   93 RIAMIFQEpMTSLNP--LHTI---------GKqiaevlrLHRGLSGAAARARALELLE----RVGipdpERRLDayphqL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 722 SGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIV-IAHRLSTITN-ADLILCISNGRIVE 798
Cdd:COG4172  158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLlITHDLGVVRRfADRVAVMRQGEIVE 237

                        250
                 ....*....|....*...
gi 162312131 799 TGTHEELIKRDGGAYKKM 816
Cdd:COG4172  238 QGPTAELFAAPQHPYTRK 255
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 598-809 1.56e-22

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 101.07  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTL-FNDTILY 676
Cdd:PRK09536  17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 NI---------KYAKPSATN----EEIYAAAKAAQIHDRILQfpdgynsrvgerglKLSGGEKQRVAVARAILKDPSIIL 743
Cdd:PRK09536  97 VVemgrtphrsRFDTWTETDraavERAMERTGVAQFADRPVT--------------SLSGGERQRVLLARALAQATPVLL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 744 LDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRD 809
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 610-800 1.64e-22

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: 96.41  E-value: 1.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIrnVTLSSLRSSIGVVPQDSTLFND-TILYNIKYAK-PS--- 684
Cdd:cd03298   24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNLFAHlTVEQNVGLGLsPGlkl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 685 --ATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAA 762
Cdd:cd03298  102 taEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 162312131 763 LNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03298  171 VLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 586-796 1.90e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 102.07  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIdDQDIRnvtlsslrssIGVVPQ 665
Cdd:COG0488    1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR----------IGYLPQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFND-TIL----------------YNIKYAKPSATNEEIyaaAKAAQIHDRILQFpDGYN--SRVGE--RGLK---- 720
Cdd:COG0488   69 EPPLDDDlTVLdtvldgdaelraleaeLEELEAKLAEPDEDL---ERLAELQEEFEAL-GGWEaeARAEEilSGLGfpee 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 --------LSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASgrTAIVIAH-R--LSTITNAdlIL 789
Cdd:COG0488  145 dldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSHdRyfLDRVATR--IL 220


                 ....*..
gi 162312131 790 CISNGRI 796
Cdd:COG0488  221 ELDRGKL 227
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 600-808 2.78e-22

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 98.88  E-value: 2.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRN---VTLSSLRSSIGVVPQD--STLfN--- 671
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNpyGSL-Nprk 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 --DTILynikyAKPSATNEEIYAAAKAAQIHDRIlqfpdgynSRVGergLK----------LSGGEKQRVAVARAILKDP 739
Cdd:PRK11308 110 kvGQIL-----EEPLLINTSLSAAERREKALAMM--------AKVG---LRpehydryphmFSGGQRQRIAIARALMLDP 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 740 SIILLDEATSALDTNTERQIqaaLNRLAS-----GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQV---LNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
587-799 3.98e-22

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 96.85  E-value: 3.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDP---RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRnvTLSSLRssiGVV 663
Cdd:COG4525    7 RHVSVRYPGggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADR---GVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLF-----NDTILYNIKYAKpsatneeiYAAAKAAQIHDRILQfpdgynsRVGERGL------KLSGGEKQRVAVA 732
Cdd:COG4525   82 FQKDALLpwlnvLDNVAFGLRLRG--------VPKAERRARAEELLA-------LVGLADFarrriwQLSGGMRQRVGIA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 733 RAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHR------LSTitnaDLILCISN-GRIVET 799
Cdd:COG4525  147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSveealfLAT----RLVVMSPGpGRIVER 218
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 598-805 4.52e-22

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: 102.68  E-value: 4.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLrffdvnsGSITIDDQDIRNvtlsslRSSIGVVPQDSTLFNDTILYN 677
Cdd:TIGR01271  440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELEPSEGKIKH------SGRISFSPQTSWIMPGTIKDN 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   678 IKYAkpSATNEEIYAAA-KAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTE 756
Cdd:TIGR01271  507 IIFG--LSYDEYRYTSViKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 162312131   757 RQI-QAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEEL 805
Cdd:TIGR01271  585 KEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 602-808 1.25e-21

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 97.49  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDD---QDIR-NVTLSSLRSSIGVVPQDSTLF-----ND 672
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRkGIFLPPEKRRIGYVFQEARLFphlsvRG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  673 TILYNIKYAKPSATNEEiyaaakaaqiHDRILQFPdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALD 752
Cdd:TIGR02142  95 NLRYGMKRARPSERRIS----------FERVIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131  753 TNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 589-809 1.36e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 95.64  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ--D 666
Cdd:PRK13652   9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFNDTILYNIKYAKPS-ATNEEIYAAAKAAQIHdrILQFPDgYNSRVGERglkLSGGEKQRVAVARAILKDPSIILLD 745
Cdd:PRK13652  89 DQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALH--MLGLEE-LRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 746 EATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRD 809
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
586-801 1.88e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 95.20  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR----NVTLSSLR 657
Cdd:PRK13649   5 LQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 658 SSIGVVPQ--DSTLFNDTILYNIKYAKP----SATNEEIYAAAKAAQIhdrilqfpdGYNSRVGERG-LKLSGGEKQRVA 730
Cdd:PRK13649  85 KKVGLVFQfpESQLFEETVLKDVAFGPQnfgvSQEEAEALAREKLALV---------GISESLFEKNpFELSGGQMRRVA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGT 801
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
587-799 2.09e-21

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 94.38  E-value: 2.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYdPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDdqdirNVTLSSLRSSIGVVPQD 666
Cdd:PRK11248   5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAERGVVFQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLF-----NDTILYNIKYAKPSATNEEIYAAAKAAQIHdrilqfPDGYNSRvgeRGLKLSGGEKQRVAVARAILKDPSI 741
Cdd:PRK11248  79 EGLLpwrnvQDNVAFGLQLAGVEKMQRLEIAHQMLKKVG------LEGAEKR---YIWQLSGGQRQRVGIARALAANPQL 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRL--STITNADLILCISN-GRIVET 799
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIeeAVFMATELVLLSPGpGRVVER 212
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 596-806 2.26e-21

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 93.76  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSS-LRSSIGVVPQDSTLFND-T 673
Cdd:cd03218   12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 674 ILYNIkyakpSATNEEIYAAAKaaQIHDRILQFPDGYN--SRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:cd03218   92 VEENI-----LAVLEIRGLSKK--EREEKLEELLEEFHitHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 752 DTNTERQIQAALNRLASGRTAIVIA-HRLS-TITNADLILCISNGRIVETGTHEELI 806
Cdd:cd03218  165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 584-803 2.65e-21

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 94.03  E-value: 2.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQdirnvtlssLRssIGVV 663
Cdd:PRK09544   5 VSLENVSVSFGQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQ----DSTLfnDTILYNIKYAKPSATNEEIYAAAK---AAQIHDRILQfpdgynsrvgerglKLSGGEKQRVAVARAIL 736
Cdd:PRK09544  73 PQklylDTTL--PLTVNRFLRLRPGTKKEDILPALKrvqAGHLIDAPMQ--------------KLSGGETQRVLLARALL 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTI-TNADLILCIsNGRIVETGTHE 803
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCL-NHHICCSGTPE 205
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
600-819 3.27e-21

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 97.03  E-value: 3.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLR-----------SSIGVVPQDST 668
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 669 LFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 749 SALDTNTERQIQAALNRLASG--RTAIVIAHRL-STITNADLILCISNGRIVETGTHEELIKRDGGAYKKMWFQ 819
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 467-794 3.30e-21

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 98.34  E-value: 3.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 467 NERYGHAVDIYLKQERKVLFslnfLNIVQGGIFTFSLAIACLLSAYR-----VTFG--FNTVGDFVilltymiQLQQPLN 539
Cdd:COG4178  248 RRRFDAVIANWRRLIRRQRN----LTFFTTGYGQLAVIFPILVAAPRyfageITLGglMQAASAFG-------QVQGALS 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 540 FFGTLYRSLQN--SIIDteRLLEIFE--EKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIAL 615
Cdd:COG4178  317 WFVDNYQSLAEwrATVD--RLAGFEEalEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLI 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 616 VGESGGGKSTIMRILLRFFDVNSGSITI-DDQDI-----RN-VTLSSLRSSIgVVPQDSTLFNDtilynikyakpsatnE 688
Cdd:COG4178  395 TGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqRPyLPLGTLREAL-LYPATAEAFSD---------------A 458

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 689 EIYAAAKAAQIHDRILQFPDGYN-SRVgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA 767
Cdd:COG4178  459 ELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL 532

                        330       340
                 ....*....|....*....|....*..
gi 162312131 768 SGRTAIVIAHRLSTITNADLILCISNG 794
Cdd:COG4178  533 PGTTVISVGHRSTLAAFHDRVLELTGD 559
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
586-797 4.36e-21

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 92.63  E-value: 4.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI---RNVTLSSLRSSIGV 662
Cdd:PRK10908   4 FEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDSTLFNDTILYNiKYAKP----SATNEEIY----AAAKAAQIHDRILQFPdgynsrvgergLKLSGGEKQRVAVARA 734
Cdd:PRK10908  84 IFQDHHLLMDRTVYD-NVAIPliiaGASGDDIRrrvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQ---AALNRLasGRTAIVIAHRLSTITNADL-ILCISNGRIV 797
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILrlfEEFNRV--GVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 588-786 7.35e-21

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 92.08  E-value: 7.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDS 667
Cdd:PRK10247  12 NVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 TLFNDTILYNIKYA---KPSATNEEIYAAAKAA-QIHDRILQfpdgynSRVGErglkLSGGEKQRVAVARAILKDPSIIL 743
Cdd:PRK10247  91 TLFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERfALPDTILT------KNIAE----LSGGEKQRISLIRNLQFMPKVLL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 162312131 744 LDEATSALDTNTERQIQAALNRLASGRTAIVI--AHRLSTITNAD 786
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHAD 205
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
596-805 7.93e-21

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 94.77  E-value: 7.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRssIGVVPQDSTLFND-TI 674
Cdd:PRK10851  14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 LYNIKYA--------KPSAtnEEIyaAAKAAQIHDrILQFP---DGYNSrvgerglKLSGGEKQRVAVARAILKDPSIIL 743
Cdd:PRK10851  92 FDNIAFGltvlprreRPNA--AAI--KAKVTQLLE-MVQLAhlaDRYPA-------QLSGGQKQRVALARALAVEPQILL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 744 LDEATSALDTNTERQIQAALNRLAS--GRTAIVIAH-RLSTITNADLILCISNGRIVETGTHEEL 805
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 596-799 8.06e-21

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: 92.95  E-value: 8.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSS---LRSSIGVVPQDStlfnd 672
Cdd:TIGR02769  23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDS----- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  673 tilynIKYAKPSATNEEI-------YAAAKAAQIHDRILQFPD--GYNSRVGER-GLKLSGGEKQRVAVARAILKDPSII 742
Cdd:TIGR02769  98 -----PSAVNPRMTVRQIigeplrhLTSLDESEQKARIAELLDmvGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLI 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  743 LLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVET 799
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 587-805 8.71e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 94.15  E-value: 8.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMR-----ILLRFFDVNSGSITIDDQDIRNVTLSS-- 655
Cdd:PRK13631  25 KNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpy 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 656 ---------LRSSIGVVPQ--DSTLFNDTILYNIKYAkPSATNEEIYAAAKAAQIHDRILQFPDGYNSRvgeRGLKLSGG 724
Cdd:PRK13631 105 skkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLER---SPFGLSGG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 725 EKQRVAVARAILKDPSIILLDEATSALDTNTERQ-IQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTH 802
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260


                 ...
gi 162312131 803 EEL 805
Cdd:PRK13631 261 YEI 263
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 597-814 1.05e-20

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 93.25  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRnvtlSSLRSSIGVVPQDSTLfndtily 676
Cdd:COG4152   14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPEERGL------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 nikYAKPSATNEEIYAAA----KAAQIHDRI------LQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:COG4152   83 ---YPKMKVGEQLVYLARlkglSKAEAKRRAdewlerLGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 747 ATSALD-TNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEElIKRDGGAYK 814
Cdd:COG4152  156 PFSGLDpVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDE-IRRQFGRNT 224
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
597-806 1.27e-20

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 92.38  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTIL- 675
Cdd:PRK11231  15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVr 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 ---------YNIKYAKPSATNEEIYAAAKAAQihdRILQFPDgynSRVGErglkLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:PRK11231  95 elvaygrspWLSLWGRLSAEDNARVNQAMEQT---RINHLAD---RRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 747 ATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 599-809 1.34e-20

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 91.73  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSSIGVVP--QDSTLFND-TIL 675
Cdd:cd03219   15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElTVL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNI----------KYAKPSATNEEIYAAAKAAQIHDRI-LQfpDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILL 744
Cdd:cd03219   94 ENVmvaaqartgsGLLLARARREEREARERAEELLERVgLA--DLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 745 DEATSALdTNTERQ-IQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEElIKRD 809
Cdd:cd03219  168 DEPAAGL-NPEETEeLAELIRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE-VRNN 233
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 596-759 1.52e-20

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 90.62  E-value: 1.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN---SGSITIDDQDIRnvTLSSLRSSIGVVPQDSTLF-N 671
Cdd:COG4136   13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT--ALPAEQRRIGILFQDDLLFpH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 DTILYNIKYAKPSATN-----EEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:COG4136   91 LSVGENLAFALPPTIGraqrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDE 159

                        170
                 ....*....|...
gi 162312131 747 ATSALDTNTERQI 759
Cdd:COG4136  160 PFSKLDAALRAQF 172
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 587-783 1.53e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 92.02  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNS-----GSITIDDQDI--RNVTLSSLRSS 659
Cdd:PRK14258  11 NNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLRRQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDSTLFNDTILYNIKYA------KPSATNEEIYAAA-KAAQIHDRIlqfpdgyNSRVGERGLKLSGGEKQRVAVA 732
Cdd:PRK14258  90 VSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162312131 733 RAILKDPSIILLDEATSALDTNTERQIQAALN--RLASGRTAIVIAHRLSTIT 783
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVS 215
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 591-804 1.87e-20

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 91.44  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 591 FAYDPRkpvLSDINFVAQPGKVIALVGESGGGKST-IMRI--LLRFfdvnSGSITIDDQDIRNVTLSSLRSSIGVVPQ-D 666
Cdd:COG4138    6 VAVAGR---LGPISAQVNAGELIHLIGPNGAGKSTlLARMagLLPG----QGEILLNGRPLSDWSAAELARHRAYLSQqQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFNDTILYNIKYAKPSATNEEIYAAAkAAQIHDRiLQFPDGYNSRVGerglKLSGGEKQRVAVARAILK-DPSI---- 741
Cdd:COG4138   79 SPPFAMPVFQYLALHQPAGASSEAVEQL-LAQLAEA-LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvWPTInpeg 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 742 --ILLDEATSALDTnteRQiQAALNRL-----ASGRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEE 804
Cdd:COG4138  153 qlLLLDEPMNSLDV---AQ-QAALDRLlrelcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAE 219
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
586-811 2.24e-20

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 92.56  E-value: 2.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSlRSSIGVVPQ 665
Cdd:PRK13537  10 FRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFND-TILYNIK-YAKpsatneeiYAAAKAAQIHDRI---LQFP---DGYNSRVGErglkLSGGEKQRVAVARAILK 737
Cdd:PRK13537  88 FDNLDPDfTVRENLLvFGR--------YFGLSAAAARALVpplLEFAkleNKADAKVGE----LSGGMKRRLTLARALVN 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLILC-ISNGRIVETGTHEELIKRDGG 811
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLCDRLCvIEEGRKIAEGAPHALIESEIG 231
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 582-798 2.31e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 95.52  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFS--HVSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITiddqdiRNVTLSslrss 659
Cdd:COG0488  312 GKKVLEleGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK------LGETVK----- 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDSTLF--NDTILYNIKYAKPSATNEEIYAAAKAaqihdriLQFPdgynsrvGERGLK----LSGGEKQRVAVAR 733
Cdd:COG0488  380 IGYFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGR-------FLFS-------GDDAFKpvgvLSGGEKARLALAK 445

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 734 AILKDPSIILLDEATSALDTNTERQIQAALNRLAsGrTAIVIAH-R--LSTItnADLILCISNGRIVE 798
Cdd:COG0488  446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 571-808 2.62e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 91.13  E-value: 2.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 571 KPNAPDLKVTQGKVifshvsfaydprkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN-----SGSITIDD 645
Cdd:PRK14247   3 KIEIRDLKVSFGQV-------------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 646 QDIRNVTLSSLRSSIGVVPQ-DSTLFNDTILYNI----KYAKPSATNEEIYA----AAKAAQIHDRIlqfpdgyNSRVGE 716
Cdd:PRK14247  70 QDIFKMDVIELRRRVQMVFQiPNPIPNLSIFENValglKLNRLVKSKKELQErvrwALEKAQLWDEV-------KDRLDA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 717 RGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAH------RLStitnaDLILC 790
Cdd:PRK14247 143 PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAF 217

                        250
                 ....*....|....*...
gi 162312131 791 ISNGRIVETGTHEELIKR 808
Cdd:PRK14247 218 LYKGQIVEWGPTREVFTN 235
cbiO PRK13643
energy-coupling factor transporter ATPase;
586-829 2.73e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 92.10  E-value: 2.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDPRKPVLS----DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT----LSSLR 657
Cdd:PRK13643   4 FEKVNYTYQPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 658 SSIGVVPQ--DSTLFNDTILYNIKYAKP----SATNEEIYAAAKAAQIhdrilqfpdGYNSRVGERG-LKLSGGEKQRVA 730
Cdd:PRK13643  84 KKVGVVFQfpESQLFEETVLKDVAFGPQnfgiPKEKAEKIAAEKLEMV---------GLADEFWEKSpFELSGGQMRRVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234

                        250       260
                 ....*....|....*....|....*...
gi 162312131 809 -------DGGAYKKMWFQQAMGKTSAET 829
Cdd:PRK13643 235 vdflkahELGVPKATHFADQLQKTGAVT 262
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 584-806 3.02e-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: 90.91  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRF-FDVNSGSITIDDQDIRNVTLSSLRSSIGV 662
Cdd:COG1119    4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 V--------PQDSTLFN-------DTI-LYNikyaKPSATNEEiyaaaKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEK 726
Cdd:COG1119   83 VspalqlrfPRDETVLDvvlsgffDSIgLYR----EPTDEQRE-----RARELLELL-----GLAHLADRPFGTLSQGEQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 727 QRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIV-IAHRL----STITNAdliLCISNGRIVETG 800
Cdd:COG1119  149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAG 225


                 ....*.
gi 162312131 801 THEELI 806
Cdd:COG1119  226 PKEEVL 231
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
599-805 3.13e-20

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 91.18  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV-------------TLSSLRSSIGVVPQ 665
Cdd:PRK10619  20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFND-TILYNIKYAKPsatneEIYAAAKAaQIHDRILQFPD--GYNSRV-GERGLKLSGGEKQRVAVARAILKDPSI 741
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPI-----QVLGLSKQ-EARERAVKYLAkvGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEV 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
579-783 3.28e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 91.48  E-value: 3.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 579 VTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLrs 658
Cdd:PRK15056   2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 659 sIGVVPQDS-------TLFNDTILYNiKYA------KPSATNEEIYAAAKAAqihdriLQFPDGYNSRVGErglkLSGGE 725
Cdd:PRK15056  80 -VAYVPQSEevdwsfpVLVEDVVMMG-RYGhmgwlrRAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQ 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 726 KQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTIT 783
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVT 206
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 597-813 4.22e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.77  E-value: 4.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFfdVNS-GSITIDDQDIRNVT---LSSLRSSIGVVPQD--STLf 670
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL--INSqGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDpnSSL- 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 ndtilynikyaKPSATNEEIYA--------AAKAAQIHDRILQFpdgynsrVGERGL----------KLSGGEKQRVAVA 732
Cdd:PRK15134 376 -----------NPRLNVLQIIEeglrvhqpTLSAAQREQQVIAV-------MEEVGLdpetrhrypaEFSGGQRQRIAIA 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 733 RAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTA-IVIAHRLSTITNadliLC-----ISNGRIVETGTHEEL 805
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLHVVRA----LChqvivLRQGEVVEQGDCERV 513


                 ....*...
gi 162312131 806 IKRDGGAY 813
Cdd:PRK15134 514 FAAPQQEY 521
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 600-805 4.52e-20

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 94.32  E-value: 4.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDirnVTLSS----LRSSIGVVPQDSTLFND-TI 674
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP---VRIRSprdaIALGIGMVHQHFMLVPNlTV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 LYNIKYAKPSATNEEIyaaaKAAQIHDRILQFPDGY------NSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:COG3845   98 AENIVLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 749 SALdtnTERQIQ---AALNRLAS-GRTAIVIAHRLSTI-TNADLILCISNGRIVETG-----THEEL 805
Cdd:COG3845  170 AVL---TPQEADelfEILRRLAAeGKSIIFITHKLREVmAIADRVTVLRRGKVVGTVdtaetSEEEL 233
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
584-805 6.25e-20

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 92.40  E-value: 6.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSslRSSIGVV 663
Cdd:PRK11000   4 VTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDSTLF-----NDTILYNIKYAKpsATNEEIYAAAKAAQihdRILQFpdgynSRVGERGLK-LSGGEKQRVAVARAILK 737
Cdd:PRK11000  81 FQSYALYphlsvAENMSFGLKLAG--AKKEEINQRVNQVA---EVLQL-----AHLLDRKPKaLSGGQRQRVAIGRTLVA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAH-RLSTITNADLILCISNGRIVETGTHEEL 805
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 587-809 6.91e-20

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 89.76  E-value: 6.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV-------TLSSLRss 659
Cdd:COG4604    5 KNVSKRYGG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpsrelakRLAILR-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 igvvpQDSTLfndtilyNIK-------------YAK--PSATNEEIYAAAKA----AQIHDRILqfpDgynsrvgerglK 720
Cdd:COG4604   82 -----QENHI-------NSRltvrelvafgrfpYSKgrLTAEDREIIDEAIAyldlEDLADRYL---D-----------E 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLstitN-----ADLILCISN 793
Cdd:COG4604  136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDI----NfascyADHIVAMKD 211

                        250
                 ....*....|....*.
gi 162312131 794 GRIVETGTHEELIKRD 809
Cdd:COG4604  212 GRVVAQGTPEEIITPE 227
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 595-813 8.72e-20

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 94.34  E-value: 8.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  595 PRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLrFFDVN----SGSITIDDqdiRNVTLSSLRSSIGVVPQDSTLF 670
Cdd:TIGR00955  36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  671 ndtilynikyakPSATNEE------------IYAAAKAAQIHDRILQ---FPDGYNSRVGERGLK--LSGGEKQRVAVAR 733
Cdd:TIGR00955 112 ------------PTLTVREhlmfqahlrmprRVTKKEKRERVDEVLQalgLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  734 AILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLST--ITNADLILCISNGRIVETGTHEELIK--R 808
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPffS 259


                  ....*
gi 162312131  809 DGGAY 813
Cdd:TIGR00955 260 DLGHP 264
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 602-805 8.89e-20

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: 88.97  E-value: 8.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSSIGVVPQDSTLFNDTI------- 674
Cdd:cd03265   18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDELTgwenlyi 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 ---LYNIKYAKPSATNEEIYAAAKAAQIHDRILQfpdgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:cd03265   97 harLYGVPGAERRERIDELLDFVGLLEAADRLVK--------------TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 752 DTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:cd03265  163 DPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 591-805 9.16e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 89.72  E-value: 9.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 591 FAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ------DIRNVTLSSLRSSIGVVP 664
Cdd:PRK14246  17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 665 QDSTLFNDTILY-NIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIIL 743
Cdd:PRK14246  97 QQPNPFPHLSIYdNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 744 LDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 597-823 1.19e-19

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 88.97  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRF--FDVNSGSITIDDQD-----------------------IRNV 651
Cdd:COG0396   13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDilelspderaragiflafqypveIPGV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 652 TLSSLrssigvvpqdstlfndtilynIKYAKPSATNEEIYAAAKAAQIHD--RILQFPDGYNSR---VGerglkLSGGEK 726
Cdd:COG0396   93 SVSNF---------------------LRTALNARRGEELSAREFLKLLKEkmKELGLDEDFLDRyvnEG-----FSGGEK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 727 QRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAH--RLSTITNADLILCISNGRIVETGTHE 803
Cdd:COG0396  147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226

                        250       260
                 ....*....|....*....|..
gi 162312131 804 --ELIKRDGgaYKkmWFQQAMG 823
Cdd:COG0396  227 laLELEEEG--YD--WLKEEAA 244
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
599-780 1.31e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 88.72  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRnvTLSS-----LRS-SIGVVPQDSTLFND 672
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS--KLSSaakaeLRNqKLGFIYQFHHLLPD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 -TILYNIkyAKPSatneeIYAAAKAAQIHDRILQF--PDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:PRK11629 102 fTALENV--AMPL-----LIGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174

                        170       180       190
                 ....*....|....*....|....*....|...
gi 162312131 750 ALDTNTERQIQAALNRL--ASGRTAIVIAHRLS 780
Cdd:PRK11629 175 NLDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 589-805 1.82e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 89.37  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR--NVTLSSLRSSIGVVPQ- 665
Cdd:PRK13639   7 LKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQn 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 -DSTLFNDTILYNIKYAKPSA--TNEEIYAAAKAAqihdriLQfpdgynsRVGERGLK------LSGGEKQRVAVARAIL 736
Cdd:PRK13639  87 pDDQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEA------LK-------AVGMEGFEnkpphhLSGGQKKRVAIAGILA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTI-TNADLILCISNGRIVETGTHEEL 805
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 596-800 2.23e-19

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: 87.34  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlsslRSSIGVVPQDSTLFND-TI 674
Cdd:cd03269   12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKmKV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 LYNIKY-AKPSATNEEiYAAAKAAQIHDRiLQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:cd03269   88 IDQLVYlAQLKGLKKE-EARRRIDEWLER-LELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 162312131 754 NTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03269  162 VNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 599-800 2.29e-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: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRIL---LRFFDVNSGSITIDDQDIRNVTLsslRSSIGVVPQDSTLF-NDTI 674
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQF---QKCVAYVRQDDILLpGLTV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 LYNIKYAKPSATNEEIYAAAKAAQIHDRILQfpDGYNSRVGERGLK-LSGGEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:cd03234   99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312131 754 NTERQIQAALNRLA-SGRTAIVIAH--RLSTITNADLILCISNGRIVETG 800
Cdd:cd03234  177 FTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
551-807 3.79e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 89.50  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 551 SIIDTERLLEIFEEK-PTVVEKPNAPDLKVTQGKVIFSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRI 629
Cdd:PRK13536   8 EEAPRRLELSPIERKhQGISEAKASIPGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 630 LLRFFDVNSGSITI-DDQDIRNVTLSslRSSIGVVPQDSTLFND-TILYNI----KYAKPSAtnEEIYAAAKAaqihdrI 703
Cdd:PRK13536  87 ILGMTSPDAGKITVlGVPVPARARLA--RARIGVVPQFDNLDLEfTVRENLlvfgRYFGMST--REIEAVIPS------L 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 704 LQFPDgYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNR-LASGRTAIVIAHRLSTI 782
Cdd:PRK13536 157 LEFAR-LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEA 235

                        250       260
                 ....*....|....*....|....*.
gi 162312131 783 TN-ADLILCISNGRIVETGTHEELIK 807
Cdd:PRK13536 236 ERlCDRLCVLEAGRKIAEGRPHALID 261
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
595-786 5.39e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 85.75  E-value: 5.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 595 PRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDqdirnvtlsslRSSIGVVPQDSTLfNDTI 674
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEV-PDSL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 lynikyakPsATNEEIYA-------------AAKAAQIHDRILQfpdgynsRVGERGL------KLSGGEKQRVAVARAI 735
Cdd:NF040873  71 --------P-LTVRDLVAmgrwarrglwrrlTRDDRAAVDDALE-------RVGLADLagrqlgELSGGQRQRALLAQGL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNAD 786
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRAD 186
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 584-778 5.42e-19

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: 84.90  E-value: 5.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIddqdirnvtlsSLRSSIGVV 663
Cdd:cd03223    1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQ-----DSTLfNDTILYnikyakPSatneeiyaaakaaqihDRILqfpdgynsrvgerglklSGGEKQRVAVARAILKD 738
Cdd:cd03223   70 PQrpylpLGTL-REQLIY------PW----------------DDVL-----------------SGGEQQRLAFARLLLHK 109

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRLasGRTAIVIAHR 778
Cdd:cd03223  110 PKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
cbiO PRK13642
energy-coupling factor transporter ATPase;
591-805 5.93e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 87.84  E-value: 5.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 591 FAYDPRKPV--LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQ--D 666
Cdd:PRK13642  12 FKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFNDTILYNIKYAKPSA--TNEEIYAAAKAAQIHDRILQFPDGYNSRvgerglkLSGGEKQRVAVARAILKDPSIILL 744
Cdd:PRK13642  92 NQFVGATVEDDVAFGMENQgiPREEMIKRVDEALLAVNMLDFKTREPAR-------LSGGQKQRVAVAGIIALRPEIIIL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 745 DEATSALDTNTERQIQAALNRLASGR--TAIVIAHRLSTITNADLILCISNGRIVETGTHEEL 805
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 597-801 8.38e-19

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: 92.38  E-value: 8.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGVVPQDSTLFN----- 671
Cdd:TIGR01257  943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhltva 1021

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   672 DTILYnikYAKPSATNEEiyaaakAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:TIGR01257 1022 EHILF---YAQLKGRSWE------EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 162312131   752 DTNTERQIQAALNRLASGRTAIVIAHRLStitNADL----ILCISNGRIVETGT 801
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 611-801 1.14e-18

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 86.76  E-value: 1.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 611 KVIALVGESGGGKSTIMRILLRFFD-VNS----GSITIDDQDI--RNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAK- 682
Cdd:PRK14243  37 QITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGAr 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 683 ----PSATNEEIYAAAKAAQIHDRIlqfpdgyNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQ 758
Cdd:PRK14243 117 ingyKGDMDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLR 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 162312131 759 IQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGT 801
Cdd:PRK14243 190 IEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 592-806 1.49e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 85.72  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 592 AYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTL-SSLRSSIGVVPQDSTLF 670
Cdd:PRK10895  12 AYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 NDTILYNIKYAKPsatneEIYAAAKAAQIHDRILQFPDGYN-SRVGER-GLKLSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:PRK10895  91 RRLSVYDNLMAVL-----QIRDDLSAEQREDRANELMEEFHiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 749 SALDTNTERQIQAALNRLA-SGRTAIVIAHRL-STITNADLILCISNGRIVETGTHEELI 806
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
cbiO PRK13645
energy-coupling factor transporter ATPase;
582-805 1.75e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 86.60  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI-----RNVT 652
Cdd:PRK13645   5 KDIILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 653 LSSLRSSIGVVPQ--DSTLFNDTILYNIKYA--KPSATNEEIYAaaKAAQIHDrILQFPDGYNSRvgeRGLKLSGGEKQR 728
Cdd:PRK13645  85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLK-LVQLPEDYVKR---SPFELSGGQKRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 729 VAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
599-797 1.83e-18

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 90.17  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSL----RSSIGVVPQDstlfndti 674
Cdd:PRK10535  23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQR-------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 lYNIKYAKPSATNEEI---YAAAKAAQIHDRILQFPD--GYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:PRK10535  95 -YHLLSHLTAAQNVEVpavYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 162312131 750 ALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLILCISNGRIV 797
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 589-809 4.19e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 85.17  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQD-- 666
Cdd:PRK13647  10 LHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpd 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFNDTILYNIKYA------KPSATNEEIYAAAKAAQIHDRILQFPdgYNsrvgerglkLSGGEKQRVAVARAILKDPS 740
Cdd:PRK13647  90 DQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPP--YH---------LSYGQKKRVAIAGVLAMDPD 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 741 IILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRD 809
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
599-808 6.23e-18

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 86.31  E-value: 6.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDirnVTLSSLRS-SIGVVPQDSTLF-----ND 672
Cdd:PRK11432  21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQrDICMVFQSYALFphmslGE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 TILYNIKYAKPSatNEEIYAAAKAAqihdriLQFPD--GYNSRVGErglKLSGGEKQRVAVARAILKDPSIILLDEATSA 750
Cdd:PRK11432  98 NVGYGLKMLGVP--KEERKQRVKEA------LELVDlaGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSN 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 751 LDTNTERQIQAALNRLAS--GRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK11432 167 LDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 599-796 8.66e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 83.96  E-value: 8.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDdqdirNVTLSSLRSSIGVVPQDSTLFN-DTILYN 677
Cdd:PRK11247  27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 678 IKYAKPSATNEEIYAAAKAAQIHDRILQFPDGynsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTER 757
Cdd:PRK11247 102 VGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 162312131 758 QIQAALNRL--ASGRTAIVIAHRLS-TITNADLILCISNGRI 796
Cdd:PRK11247 171 EMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 599-809 1.14e-17

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: 83.55  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSSIGVVP--QDSTLFND-TIL 675
Cdd:COG0411   19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElTVL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNIKYA---------------KPSATNEEIYAAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPS 740
Cdd:COG0411   98 ENVLVAaharlgrgllaallrLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPK 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 741 IILLDEATSALdTNTERQ-IQAALNRLA--SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEElIKRD 809
Cdd:COG0411  173 LLLLDEPAAGL-NPEETEeLAELIRRLRdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE-VRAD 243
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 602-800 2.05e-17

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 86.83  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGVVPQDStlfndtilyni 678
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP----------- 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 679 kYAKPSATNEEIYAAAKAAQIHdRILQfPDGYNSRVG---ER-GLK----------LSGGEKQRVAVARAILKDPSIILL 744
Cdd:PRK10261 411 -YASLDPRQTVGDSIMEPLRVH-GLLP-GKAAAARVAwllERvGLLpehawrypheFSGGQRQRICIARALALNPKVIIA 487

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 745 DEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
568-805 2.38e-17

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 84.89  E-value: 2.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 568 VVEKPNAPDLKVTQGKVIFSHVSFAYDPrKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQD 647
Cdd:PRK11607   4 AIPRPQAKTRKALTPLLEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 648 IRNVtlSSLRSSIGVVPQDSTLF-NDTILYNIKYAkpsATNEEIYAAAKAAQIHD-----RILQFpdgynsrVGERGLKL 721
Cdd:PRK11607  83 LSHV--PPYQRPINMMFQSYALFpHMTVEQNIAFG---LKQDKLPKAEIASRVNEmlglvHMQEF-------AKRKPHQL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 722 SGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAA----LNRLasGRTAIVIAH-RLSTITNADLILCISNGRI 796
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEvvdiLERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228


                 ....*....
gi 162312131 797 VETGTHEEL 805
Cdd:PRK11607 229 VQIGEPEEI 237
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
587-801 2.44e-17

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 82.81  E-value: 2.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 587 SHVSFAY--------DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLS---S 655
Cdd:PRK10419   7 SGLSHHYahgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 656 LRSSIGVVPQDStlfndtilynikyakPSATNE-----EIYA-----------AAKAAQIHD--RILQFPDGYNSRvgeR 717
Cdd:PRK10419  87 FRRDIQMVFQDS---------------ISAVNPrktvrEIIReplrhllsldkAERLARASEmlRAVDLDDSVLDK---R 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 718 GLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNG 794
Cdd:PRK10419 149 PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqqQFGTACLFITHDLRLVERfCQRVMVMDNG 228


                 ....*..
gi 162312131 795 RIVETGT 801
Cdd:PRK10419 229 QIVETQP 235
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 597-810 4.89e-17

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: 80.26  E-value: 4.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRF--FDVNSGSITIDDQDIRNVTLSSlRSSIGVvpqdstlfndTI 674
Cdd:cd03217   13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGI----------FL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 LYNIKYAKPSATNEEIyaaakaaqihdriLQFpdgynsrVGErglKLSGGEKQRVAVARAILKDPSIILLDEATSALDTN 754
Cdd:cd03217   82 AFQYPPEIPGVKNADF-------------LRY-------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 755 TERQIQAALNRLAS-GRTAIVIAH--RLSTITNADLILCISNGRIVETGTHE--ELIKRDG 810
Cdd:cd03217  139 ALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 597-797 8.14e-17

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 81.29  E-value: 8.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSlRSS-IGVVPQDS---TLFND 672
Cdd:COG1101   19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKyIGRVFQDPmmgTAPSM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 TILYNIKYA---------KPSATNEEIyaaakaAQIHDRILQFPDGYNSRVGER-GLkLSGGEKQRVAVARAILKDPSII 742
Cdd:COG1101   98 TIEENLALAyrrgkrrglRRGLTKKRR------ELFRELLATLGLGLENRLDTKvGL-LSGGQRQALSLLMATLTKPKLL 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 743 LLDEATSALDTNTERQIQAALNRLASGR--TAIVIAHRLS-TITNADLILCISNGRIV 797
Cdd:COG1101  171 LLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 582-805 8.35e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 81.68  E-value: 8.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPRKpvlsdinfvaqpgkVIALVGESGGGKSTIMRILLRFFDV-----NSGSITIDDQDIRNV-TLSS 655
Cdd:PRK14271  33 GKTVLDQVSMGFPARA--------------VTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 656 LRSSIGVVPQDSTLFNDTILYNI---KYAKPSATNEEIYAAAKAAQIHdriLQFPDGYNSRVGERGLKLSGGEKQRVAVA 732
Cdd:PRK14271  99 FRRRVGMLFQRPNPFPMSIMDNVlagVRAHKLVPRKEFRGVAQARLTE---VGLWDAVKDRLSDSPFRLSGGQQQLLCLA 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 733 RAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 596-796 9.94e-17

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: 79.01  E-value: 9.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDI-RNVTLSSLRSSIGVVPQDstlfndti 674
Cdd:cd03215   12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAGIAYVPED-------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 lynikyakpsatneeiyaaakaaqihdR-----ILQFPDGYNSRVGERglkLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:cd03215   84 ---------------------------RkreglVLDLSVAENIALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTR 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 750 ALDTNTERQIQAALNRLASGRTAIVIahrLST-----ITNADLILCISNGRI 796
Cdd:cd03215  134 GVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
600-800 1.18e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 83.68  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLS-SLRSSIGVVPQDSTLFND-TILYN 677
Cdd:PRK09700  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 678 IKYA-----KPSATNEEIYAAAKA-AQIHDRILQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:PRK09700 101 LYIGrhltkKVCGVNIIDWREMRVrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 752 dTNTE-RQIQAALNRLASGRTAIV-IAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:PRK09700 177 -TNKEvDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 583-800 1.35e-16

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 79.50  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 583 KVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDdqdiRNVTlSSLRSSIGV 662
Cdd:cd03220   21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR----GRVS-SLLGLGGGF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQ----DSTLFNDTILynikyakpSATNEEIyaaakaAQIHDRILQF---PDGYNSRVGErglkLSGGEKQRVAVARAI 735
Cdd:cd03220   96 NPEltgrENIYLNGRLL--------GLSRKEI------DEKIDEIIEFselGDFIDLPVKT----YSSGMKARLAFAIAT 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAAL-NRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03220  158 ALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
589-807 1.37e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 80.90  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAY-----DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV-TLSSLRSSIGV 662
Cdd:PRK13633  10 VSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGM 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 VPQDStlfNDTILYNIKyakpsatnEEIYA------AAKAAQIHDRIlqfpDGYNSRVGERGLK------LSGGEKQRVA 730
Cdd:PRK13633  90 VFQNP---DNQIVATIV--------EEDVAfgpenlGIPPEEIRERV----DESLKKVGMYEYRrhaphlLSGGQKQRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIK 807
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
599-805 1.63e-16

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 80.27  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQD-STLFN-----D 672
Cdd:COG4167   28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDpNTSLNprlniG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 TILynikyAKPSATNEEIYAAAKAAQIHDRILQ---FPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:COG4167  108 QIL-----EEPLRLNTDLTAEEREERIFATLRLvglLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 750 ALDTNTERQIqaaLNRLAS-----GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:COG4167  179 ALDMSVRSQI---INLMLElqeklGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEV 237
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 609-782 2.00e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 83.13  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 609 PGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQdirNVTLSSLRSS----IGVVPQDSTLF-NDTILYNIKYAKP 683
Cdd:PRK10762  29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK---EVTFNGPKSSqeagIGIIHQELNLIpQLTIAENIFLGRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 684 SATN------EEIYAAAkaaqihDRILQ---FPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSAL-DT 753
Cdd:PRK10762 106 FVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDT 175

                        170       180       190
                 ....*....|....*....|....*....|
gi 162312131 754 NTErQIQAALNRL-ASGRTAIVIAHRLSTI 782
Cdd:PRK10762 176 ETE-SLFRVIRELkSQGRGIVYISHRLKEI 204
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 602-805 2.01e-16

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 81.29  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRSSIGVVPQD--STL-----FN 671
Cdd:PRK15079  39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDplASLnprmtIG 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 DTILYNIKYAKPSATNEEIYAAAKAaqIHDRILQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:PRK15079 119 EIIAEPLRTYHPKLSRQEVKDRVKA--MMLKVGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSAL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 752 DTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 600-794 2.04e-16

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: 79.43  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLrssigVVPQDSTLF-----NDTI 674
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLpwltvRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  675 LYNIKYAKPSATNEEiyaaakAAQIHDRILQFPdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTN 754
Cdd:TIGR01184  76 ALAVDRVLPDLSKSE------RRAIVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 162312131  755 TERQIQAALNRLA--SGRTAIVIAHRL-STITNADLILCISNG 794
Cdd:TIGR01184 149 TRGNLQEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 597-808 2.58e-16

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 82.93  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRIL--LRFFDVNSGSI----------------------------TIDDQ 646
Cdd:TIGR03269  13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvgepcpvcggTLEPE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  647 DIRNVTLS-----SLRSSIGVVPQDS-TLF-NDTILYNIKYAKPSATNEEIYAAAKAAQIHDRIlqfpdGYNSRVGERGL 719
Cdd:TIGR03269  93 EVDFWNLSdklrrRIRKRIAIMLQRTfALYgDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV-----QLSHRITHIAR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  720 KLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITN-ADLILCISNGRI 796
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEI 247

                         250
                  ....*....|..
gi 162312131  797 VETGTHEELIKR 808
Cdd:TIGR03269 248 KEEGTPDEVVAV 259
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
600-807 3.69e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 82.27  E-value: 3.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR-NVTLSSLRSSIGVVPQDSTLFndtilyni 678
Cdd:PRK11288  20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLV-------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 679 kyakPSAT-NEEIYAA---AKAAQIHDRILqfpdgyNSRVGER----GLK---------LSGGEKQRVAVARAILKDPSI 741
Cdd:PRK11288  92 ----PEMTvAENLYLGqlpHKGGIVNRRLL------NYEAREQlehlGVDidpdtplkyLSIGQRQMVEIAKALARNARV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETG------THEELIK 807
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVATFddmaqvDRDQLVQ 235
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 597-777 4.53e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 77.61  E-value: 4.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIrnvTLSSLRSSIGVV-PQDSTLFNDTIL 675
Cdd:PRK13539  15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNAMKPALTVA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNIKY-AKPSATNE-EIYAAAKAAQIHDrILQFPDGYnsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:PRK13539  92 ENLEFwAAFLGGEElDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160

                        170       180
                 ....*....|....*....|....*
gi 162312131 754 NTERQIQAAL-NRLASGRTAIVIAH 777
Cdd:PRK13539 161 AAVALFAELIrAHLAQGGIVIAATH 185
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
589-805 4.61e-16

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 79.04  E-value: 4.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSL---RSSIGVVPQ 665
Cdd:PRK11831  13 VSFTRGNR-CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFND-TILYNIKYAKPSATNeeiyaaAKAAQIHDRILQFPDGynsrVGERGL------KLSGGEKQRVAVARAILKD 738
Cdd:PRK11831  92 SGALFTDmNVFDNVAYPLREHTQ------LPAPLLHSTVMMKLEA----VGLRGAaklmpsELSGGMARRAALARAIALE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 588-805 4.63e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 79.51  E-value: 4.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ--DIRNVTLSSLRSSIGVVPQ 665
Cdd:PRK13636  10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 --DSTLFNDTILYNIKYAkpsATNEEIyaaaKAAQIHDRIlqfpDGYNSRVGERGLK------LSGGEKQRVAVARAILK 737
Cdd:PRK13636  90 dpDNQLFSASVYQDVSFG---AVNLKL----PEDEVRKRV----DNALKRTGIEHLKdkpthcLSFGQKKRVAIAGVLVM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTIT-NADLILCISNGRIVETGTHEEL 805
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
604-806 1.06e-15

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 77.31  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 604 NFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSslRSSIGVVPQDSTLFND-TILYNIKYA- 681
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 682 KP-----SATNEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTE 756
Cdd:PRK10771  97 NPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162312131 757 RQIQAALNRLASGR--TAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 597-800 1.13e-15

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: 77.37  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSITIDDQDIRNVTL------SSLRSSIGVV------- 663
Cdd:cd03267   34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL-------SGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVVfgqktql 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 -----PQDSTLFNDTIlYNIKYAKPSATNEEIYAAAKAAQIHDRILQfpdgynsrvgerglKLSGGEKQRVAVARAILKD 738
Cdd:cd03267  107 wwdlpVIDSFYLLAAI-YDLPPARFKKRLDELSELLDLEELLDTPVR--------------QLSLGQRMRAEIAAALLHE 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 739 PSIILLDEATSALDTNTERQIQAALNRLASGRTAIVI--AHRLSTITN-ADLILCISNGRIVETG 800
Cdd:cd03267  172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLLYDG 236
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 593-805 1.15e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 77.57  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 593 YDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN-----SGSITIDDQDIRN--VTLSSLRSSIGVVPQ 665
Cdd:PRK14267  13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEVRREVGMVFQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFNDTILYN-----IKYAKPSATNEEI-----YAAAKAA---QIHDRILQFPDgynsrvgerglKLSGGEKQRVAVA 732
Cdd:PRK14267  93 YPNPFPHLTIYDnvaigVKLNGLVKSKKELderveWALKKAAlwdEVKDRLNDYPS-----------NLSGGQRQRLVIA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 733 RAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKV 235
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 596-807 1.42e-15

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 76.99  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIrnvtlSSL------RSSIGVVPQDSTL 669
Cdd:COG1137   15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-----THLpmhkraRLGIGYLPQEASI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 670 FND-TILYNIK----YAKPSAtneeiyaaakaAQIHDRIlqfpdgyNSRVGE---------RGLKLSGGEKQRVAVARAI 735
Cdd:COG1137   90 FRKlTVEDNILavleLRKLSK-----------KEREERL-------EELLEEfgithlrksKAYSLSGGERRRVEIARAL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIA-HR----LSTITNADLilcISNGRIVETGTHEELIK 807
Cdd:COG1137  152 ATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNvretLGICDRAYI---ISEGKVLAEGTPEEILN 225
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 584-777 1.55e-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: 74.41  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDqdirnvtlsslRSSIGVV 663
Cdd:cd03221    1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQdstlfndtilynikyakpsatneeiyaaakaaqihdrilqfpdgynsrvgerglkLSGGEKQRVAVARAILKDPSIIL 743
Cdd:cd03221   69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93

                        170       180       190
                 ....*....|....*....|....*....|....
gi 162312131 744 LDEATSALDTNTERQIQAALNRLAsgRTAIVIAH 777
Cdd:cd03221   94 LDEPTNHLDLESIEALEEALKEYP--GTVILVSH 125
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 602-805 1.60e-15

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 78.61  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN---SGSITIDDQDIRNV---TLSSLRS-SIGVVPQDS-TLFN-- 671
Cdd:PRK09473  34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLpekELNKLRAeQISMIFQDPmTSLNpy 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 --------DTILYNIKYAKPSATNEEIYA--AAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSI 741
Cdd:PRK09473 114 mrvgeqlmEVLMLHKGMSKAEAFEESVRMldAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALLCRPKL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLASG-RTAIV-IAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
cbiO PRK13644
energy-coupling factor transporter ATPase;
589-806 1.83e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 77.33  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 589 VSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT-LSSLRSSIGVVPQ-- 665
Cdd:PRK13644   7 VSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQnp 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DSTLFNDTILYNIKYAKPSATNEEIyaaakaaQIHDRIlqfpdgyNSRVGERGLK---------LSGGEKQRVAVARAIL 736
Cdd:PRK13644  87 ETQFVGRTVEEDLAFGPENLCLPPI-------EIRKRV-------DRALAEIGLEkyrhrspktLSGGQGQCVALAGILT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELI 806
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 600-799 2.02e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 79.97  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNS--GSITIDDQDIRNVTLS-SLRSSIGVVPQDSTLFND-TIL 675
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNI----KYAKPSATN-EEIYAAAKA--AQIHDRIlqfpdGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:PRK13549 101 ENIflgnEITPGGIMDyDAMYLRAQKllAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPT 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 749 SALdtnTERQIQAALNRL----ASGRTAIVIAHRLSTITN-ADLILCISNGRIVET 799
Cdd:PRK13549 172 ASL---TESETAVLLDIIrdlkAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGT 224
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 583-752 2.52e-15

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: 79.98  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  583 KVIFS--HVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSitidDQDIRNVTLSSLRSSI 660
Cdd:TIGR03719   2 QYIYTmnRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV----DKDFNGEARPQPGIKV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  661 GVVPQDSTL-FNDTILYNI-------------------KYAKPSA----------TNEEIYAAAKAAQIHDRI------L 704
Cdd:TIGR03719  71 GYLPQEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDAdfdklaaeqaELQEIIDAADAWDLDSQLeiamdaL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 162312131  705 QFPDGyNSRVGerglKLSGGEKQRVAVARAILKDPSIILLDEATSALD 752
Cdd:TIGR03719 151 RCPPW-DADVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
 588-800 3.01e-15

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: 76.15  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  588 HVSFAydpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILL--RFFDVNSGSITIDDQDIRNVTLSSlRSSIGV--- 662
Cdd:TIGR01978   7 HVSVE---DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDE-RARAGLfla 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  663 ------VPQDStlfNDTILYNIKYAKPSATNEEiyaAAKAAQIHDRI------LQFPDGYNSRVGERGLklSGGEKQRVA 730
Cdd:TIGR01978  83 fqypeeIPGVS---NLEFLRSALNARRSARGEE---PLDLLDFEKLLkeklalLDMDEEFLNRSVNEGF--SGGEKKRNE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131  731 VARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTA-IVIAH--RLSTITNADLILCISNGRIVETG 800
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSfLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 598-805 3.36e-15

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 79.32  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT-LSSLRSSIGVVPQDSTLF-NDTIL 675
Cdd:PRK15439  25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFpNLSVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNIKY--AKPSATNEEIYAAAKAAQIHDRiLQFPDGynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEATSALD- 752
Cdd:PRK15439 105 ENILFglPKRQASMQKMKQLLAALGCQLD-LDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 753 TNTER---QIQAAlnrLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK15439 174 AETERlfsRIREL---LAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 596-778 3.91e-15

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 75.38  E-value: 3.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLR--FFDVNSGSITIDDQDI-RNVTLsslrssIGVVPQDSTlFND 672
Cdd:COG2401   42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFgREASL------IDAIGRKGD-FKD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 TIlynikyakpsatneEIYAAAKaaqIHDRILqfpdgYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSALD 752
Cdd:COG2401  115 AV--------------ELLNAVG---LSDAVL-----WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168

                        170       180
                 ....*....|....*....|....*...
gi 162312131 753 TNTERQIQAALNRLA--SGRTAIVIAHR 778
Cdd:COG2401  169 RQTAKRVARNLQKLArrAGITLVVATHH 196
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
586-806 4.69e-15

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 75.30  E-value: 4.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 586 FSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRN-VTLSSLRSSIGVVP 664
Cdd:PRK11614   8 FDKVSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 665 QDSTLFNdtilynikyakpSATNEEIYAA----AKAAQIHDRILQ----FPDGYNSRVgERGLKLSGGEKQRVAVARAIL 736
Cdd:PRK11614  87 EGRRVFS------------RMTVEENLAMggffAERDQFQERIKWvyelFPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 737 KDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEELI 806
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
593-808 8.73e-15

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 76.81  E-value: 8.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 593 YDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSsIGVVPQDSTLF-- 670
Cdd:PRK11650  13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-PADRD-IAMVFQNYALYph 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 ---NDTILYNIKYAK-PSAT-NEEIYAAAKAAQIhdrilqfpDGYNSRvgeRGLKLSGGEKQRVAVARAILKDPSIILLD 745
Cdd:PRK11650  91 msvRENMAYGLKIRGmPKAEiEERVAEAARILEL--------EPLLDR---KPRELSGGQRQRVAMGRAIVREPAVFLFD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 746 EATSALDTNTERQIQAALNRL--ASGRTAIVIAH-RLSTITNADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLhrRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
580-809 8.78e-15

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 75.21  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 580 TQGKVIFSHVSFAYD------PRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQdirnvTL 653
Cdd:PRK10575   1 MQEYTNHSDTTFALRnvsfrvPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-----PL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 654 SSLrssigvvpqDSTLFNDTILYnIKYAKPSA---TNEEIYAAAKAAQiHDRILQFPDGYNSRVGER----GLK------ 720
Cdd:PRK10575  76 ESW---------SSKAFARKVAY-LPQQLPAAegmTVRELVAIGRYPW-HGALGRFGAADREKVEEAislvGLKplahrl 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 ---LSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAhRLSTITNA----DLILCISN 793
Cdd:PRK10575 145 vdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRG 223

                        250
                 ....*....|....*.
gi 162312131 794 GRIVETGTHEELIKRD 809
Cdd:PRK10575 224 GEMIAQGTPAELMRGE 239
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 599-777 8.83e-15

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 74.43  E-value: 8.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT---LSSLRS-SIGVVPQDSTLFND-T 673
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRAkHVGFVFQSFMLIPTlN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 674 ILYNIKYAKPSATNEEIYAAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQL-----GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179

                        170       180
                 ....*....|....*....|....*..
gi 162312131 754 NTERQIQA---ALNRlASGRTAIVIAH 777
Cdd:PRK10584 180 QTGDKIADllfSLNR-EHGTTLILVTH 205
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
575-805 1.17e-14

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 77.37  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 575 PDLKVTQGKVIFS--HVSfaydpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ--DIRN 650
Cdd:COG1129  246 PKRAAAPGEVVLEveGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRS 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 651 VTlSSLRSSIGVVPQD---STLF-NDTILYNI------KYAKPSATNE-EIYAAA---------KAAQIHDRILQfpdgy 710
Cdd:COG1129  321 PR-DAIRAGIAYVPEDrkgEGLVlDLSIRENItlasldRLSRGGLLDRrRERALAeeyikrlriKTPSPEQPVGN----- 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 711 nsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIahrlST-----ITN 784
Cdd:COG1129  395 ----------LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAaEGKAVIVI----SSelpelLGL 460

                        250       260
                 ....*....|....*....|.
gi 162312131 785 ADLILCISNGRIVETGTHEEL 805
Cdd:COG1129  461 SDRILVMREGRIVGELDREEA 481
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 592-804 1.90e-14

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 73.81  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 592 AYDPRkpvLSDINFVAQPGKVIALVGESGGGKSTIM-RI--LLRFfdvnSGSITIDDQDIRNVTLSSL-RSSIGVVPQDS 667
Cdd:PRK03695   7 AVSTR---LGPLSAEVRAGEILHLVGPNGAGKSTLLaRMagLLPG----SGSIQFAGQPLEAWSAAELaRHRAYLSQQQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 TLFNDTILYNIKYAKPSATNEeiyaAAKAAQIHD--RILQFPDGYNSRVGErglkLSGGEKQRVAVARAILK-DPSI--- 741
Cdd:PRK03695  80 PPFAMPVFQYLTLHQPDKTRT----EAVASALNEvaEALGLDDKLGRSVNQ----LSGGEWQRVRLAAVVLQvWPDInpa 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 742 ---ILLDEATSALDTNTerqiQAALNRL-----ASGRTAIVIAHRLS-TITNADLILCISNGRIVETGTHEE 804
Cdd:PRK03695 152 gqlLLLDEPMNSLDVAQ----QAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
596-809 2.97e-14

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 73.87  E-value: 2.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTIL 675
Cdd:PRK10253  19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 YNI----KYA-KPSAT------NEEIYAAAKAAQIHDRILQFPDgynsrvgerglKLSGGEKQRVAVARAILKDPSIILL 744
Cdd:PRK10253  99 QELvargRYPhQPLFTrwrkedEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 745 DEATSALDTNTE---RQIQAALNRlASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRD 809
Cdd:PRK10253 168 DEPTTWLDISHQidlLELLSELNR-EKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAE 235
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
602-806 3.31e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 73.67  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQD-STLFNDTILYNIKY 680
Cdd:PRK15112  31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpSTSLNPRQRISQIL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 681 AKPSATNEEIYAAAKAAQIHDRILQ---FPD--GYNSRVgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNT 755
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQvglLPDhaSYYPHM------LAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 162312131 756 ERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:PRK15112 185 RSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 597-803 4.03e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 73.14  E-value: 4.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRF--FDVNSGSITIDDQDIRNVTlSSLRSSIGvvpqdstlfndtI 674
Cdd:CHL00131  20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLG------------I 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 675 LYNIKYAK--PSATNEEIYAAAkaaqihdrilqfpdgYNSRVGERGL--------------KL----------------- 721
Cdd:CHL00131  87 FLAFQYPIeiPGVSNADFLRLA---------------YNSKRKFQGLpeldplefleiineKLklvgmdpsflsrnvneg 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 722 -SGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIV-IAH--RLSTITNADLILCISNGRIV 797
Cdd:CHL00131 152 fSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKII 231


                 ....*.
gi 162312131 798 ETGTHE 803
Cdd:CHL00131 232 KTGDAE 237
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 583-805 4.21e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 73.97  E-value: 4.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 583 KVIFSHVSFAYDPRKP----VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSS--- 655
Cdd:PRK13651   2 QIKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKeke 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 656 ---------------------LRSSIGVVPQ--DSTLFNDTILYNIKYAKPS--ATNEEiyaAAKAAQIHDRILQFPDGY 710
Cdd:PRK13651  82 kvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEE---AKKRAAKYIELVGLDESY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 711 NSRvgeRGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTI---TNAD 786
Cdd:PRK13651 159 LQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlewTKRT 235

                        250       260
                 ....*....|....*....|
gi 162312131 787 LILciSNGRIVETG-THEEL 805
Cdd:PRK13651 236 IFF--KDGKIIKDGdTYDIL 253
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 603-806 5.91e-14

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: 75.22  E-value: 5.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  603 INFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSIT-------IDDQDIRNVTLSSLRSSIGVVPQDSTLF-NDTI 674
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTV 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  675 LYNIKYAKPSATNEEIyaAAKAAQIHDRILQFPDGYNSRVGER-GLKLSGGEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:TIGR03269 383 LDNLTEAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131  754 NTERQIQAAL--NRLASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:TIGR03269 461 ITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 572-809 6.52e-14

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 75.39  E-value: 6.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 572 PNAPDLKVTQG-----KVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ 646
Cdd:PRK10522 306 PYKAEFPRPQAfpdwqTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 647 DIRNVTLSSLRSSIGVVPQDSTLFNDTIlyniKYAKPSATNEEIYAAAKAAQIHDRiLQFPDGynsRVgeRGLKLSGGEK 726
Cdd:PRK10522 386 PVTAEQPEDYRKLFSAVFTDFHLFDQLL----GPEGKPANPALVEKWLERLKMAHK-LELEDG---RI--SNLKLSKGQK 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 727 QRVAVARAILKDPSIILLDEATSALDTNTERQI-QAALNRL-ASGRTAIVIAHRLSTITNADLILCISNGRIVE-TGTHE 803
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEER 535


                 ....*.
gi 162312131 804 ELIKRD 809
Cdd:PRK10522 536 DAASRD 541
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
612-804 1.52e-13

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 72.98  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 612 VIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ---DIRN-VTLSSLRSSIGVVPQDSTLF-NDTILYNIKYAkpsat 686
Cdd:PRK11144  26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFpHYKVRGNLRYG----- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 687 neeiYAAAKAAQIhDRILQ----------FPdgynsrvgergLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTE 756
Cdd:PRK11144 101 ----MAKSMVAQF-DKIVAllgieplldrYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162312131 757 RQIQAALNRLASG-RTAIV-IAHRLSTITN-ADLILCISNGRIVETGTHEE 804
Cdd:PRK11144 165 RELLPYLERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 566-815 1.73e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 74.12  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 566 PTVVEKPNAPDLKVTQGKVIFSHVSfaydPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDD 645
Cdd:PRK10261   2 PHSDELDARDVLAVENLNIAFMQEQ----QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 646 Q----------DIRNVTLSSLR----SSIGVVPQDS-TLFN------DTILYNIKYAKpSATNEEIYAAAKAAQIHDRIl 704
Cdd:PRK10261  78 MllrrrsrqviELSEQSAAQMRhvrgADMAMIFQEPmTSLNpvftvgEQIAESIRLHQ-GASREEAMVEAKRMLDQVRI- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 705 qfPDGyNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRT--AIVIAHRLSTI 782
Cdd:PRK10261 156 --PEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVV 232

                        250       260       270
                 ....*....|....*....|....*....|....
gi 162312131 783 TN-ADLILCISNGRIVETGTHEELIKRDGGAYKK 815
Cdd:PRK10261 233 AEiADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 597-815 1.91e-13

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 73.59  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKS----TIMRILLRFFDV-NSGSITIDDQDIRNVTLSSLRSSIGvvPQDSTLFN 671
Cdd:PRK15134  22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTLRGVRG--NKIAMIFQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 DTI-----LYNIK---YAKPSATNEEIYAAAKAaqihdRILQFPDgynsRVGERGLK---------LSGGEKQRVAVARA 734
Cdd:PRK15134 100 EPMvslnpLHTLEkqlYEVLSLHRGMRREAARG-----EILNCLD----RVGIRQAAkrltdyphqLSGGERQRVMIAMA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRDGG 811
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTH 250


                 ....
gi 162312131 812 AYKK 815
Cdd:PRK15134 251 PYTQ 254
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 583-752 1.95e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 74.00  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 583 KVIFS--HVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSitidDQDIRNVTLSSLRSSI 660
Cdd:PRK11819   4 QYIYTmnRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV----DKEFEGEARPAPGIKV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFND-TILYNI-------------------KYAKPSATNEEIyaAAKAAQIHDRI----------------- 703
Cdd:PRK11819  73 GYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDAL--AAEQGELQEIIdaadawdldsqleiamd 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312131 704 -LQFPDGyNSRVGerglKLSGGEKQRVAVARAILKDPSIILLDEATSALD 752
Cdd:PRK11819 151 aLRCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 563-805 2.97e-13

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 73.14  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 563 EEKPTVVEKPNApdlkvTQGKVIFS--HVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRIL--LRffDVNS 638
Cdd:COG3845  240 REVLLRVEKAPA-----EPGEVVLEveNLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPAS 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 639 GSITIDDQDIRNVTLSSLRSS-IGVVPQD---------STLFNDTIL---YNIKYAKPSATNEEiyAAAKAAQihDRILQ 705
Cdd:COG3845  313 GSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrglvpdMSVAENLILgryRRPPFSRGGFLDRK--AIRAFAE--ELIEE 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 706 F---PDGYNSRVGerglKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAI-VIAHRLST 781
Cdd:COG3845  389 FdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLISEDLDE 464

                        250       260
                 ....*....|....*....|....*
gi 162312131 782 ITN-ADLILCISNGRIVETGTHEEL 805
Cdd:COG3845  465 ILAlSDRIAVMYEGRIVGEVPAAEA 489
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 583-816 3.85e-13

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 70.11  E-value: 3.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 583 KVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIddqdirNVTLSSLrssIGV 662
Cdd:COG1134   25 KELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV------NGRVSAL---LEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 663 vpqdSTLFNdtilynikyakPSATNEE-IYAAA-----KAAQIH---DRILQFpdgynSRVGE---RGLK-LSGGEKQRV 729
Cdd:COG1134   96 ----GAGFH-----------PELTGREnIYLNGrllglSRKEIDekfDEIVEF-----AELGDfidQPVKtYSSGMRARL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 730 AVARAILKDPSIILLDEATSALDTN-TERQIQAALNRLASGRTAIVIAHRLSTITNadliLC-----ISNGRIVETGTHE 803
Cdd:COG1134  156 AFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRR----LCdraiwLEKGRLVMDGDPE 231

                        250
                 ....*....|...
gi 162312131 804 ELIKrdggAYKKM 816
Cdd:COG1134  232 EVIA----AYEAL 240
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 600-799 5.12e-13

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: 72.16  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNS--GSITIDDQDIRNVTLSSL-RSSIGVVPQDSTLFND-TIL 675
Cdd:TIGR02633  17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  676 YNIKYAKPSATNEEI--YAA-AKAAQIHDRILQFPDGYNSR-VGERGlklsGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:TIGR02633  97 ENIFLGNEITLPGGRmaYNAmYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 162312131  752 dtnTERQIQAALNRL----ASGRTAIVIAHRLSTITN-ADLILCISNGRIVET 799
Cdd:TIGR02633 173 ---TEKETEILLDIIrdlkAHGVACVYISHKLNEVKAvCDTICVIRDGQHVAT 222
ABC_6TM_McjD_like cd18556
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...
 263-551 6.22e-13

Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.


Pssm-ID: 350000  Cd Length: 298  Bit Score: 70.36  E-value: 6.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 263 FQIFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQG----NMGVIGSLRSFLWVPvsqyAYR 338
Cdd:cd18556    2 LLFFSILFISLLSSILISISPVILAKITDLLTSSSSDSYNYIVVLAALYVITISatklLGFLSLYLQSSLRVE----LII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 339 AISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSS-LNTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLC 417
Cdd:cd18556   78 SISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNdLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 418 YCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDI-------YLKQERKVLFSLNF 490
Cdd:cd18556  158 FVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnsqkrYWKLTFKMLILNSL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 491 LN-IVQGGIFTFSLaiacllsaYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNS 551
Cdd:cd18556  238 LNvILFGLSFFYSL--------YGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQS 291
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 597-777 6.68e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 71.85  E-value: 6.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDqdirNVTLSSLR---------SSIGVVpqds 667
Cdd:PRK15064  14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP----NERLGKLRqdqfafeefTVLDTV---- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 668 tLFNDTILYNIK------YAKPSATNEEIYAAAkaaqihDRILQFP--DGYN--SRVGE------------RGL--KLSG 723
Cdd:PRK15064  86 -IMGHTELWEVKqerdriYALPEMSEEDGMKVA------DLEVKFAemDGYTaeARAGElllgvgipeeqhYGLmsEVAP 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 162312131 724 GEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASgrTAIVIAH 777
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS--TMIIISH 210
PLN03211 PLN03211
ABC transporter G-25; Provisional
 597-795 9.02e-13

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 71.83  E-value: 9.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNS--GSITIDDqdiRNVTLSSLRSsIGVVPQDSTLF---- 670
Cdd:PLN03211  81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILKR-TGFVTQDDILYphlt 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 -NDTILYNIKYAKPSATNEEIYAAAKAAQIHDriLQFPDGYNSRVGERGLK-LSGGEKQRVAVARAILKDPSIILLDEAT 748
Cdd:PLN03211 157 vRETLVFCSLLRLPKSLTKQEKILVAESVISE--LGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPT 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312131 749 SALDTNTERQIQAALNRLAS-GRTAIVIAHRLST--ITNADLILCISNGR 795
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 596-781 1.04e-12

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: 67.65  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILL--RFFDVNSGSITIDDQDIRnvtlSSLRSSIGVVPQDSTLFndt 673
Cdd:cd03232   19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD----KNFQRSTGYVEQQDVHS--- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 674 ilynikyakPSATNEEiyaaakAAQIHDRIlqfpdgynsrvgeRGLKLSggEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:cd03232   92 ---------PNLTVRE------ALRFSALL-------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDS 141

                        170       180
                 ....*....|....*....|....*....
gi 162312131 754 NTERQIQAALNRLA-SGRTAIVIAHRLST 781
Cdd:cd03232  142 QAAYNIVRFLKKLAdSGQAILCTIHQPSA 170
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 593-800 1.31e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 68.80  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 593 YDPRKPvLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSL---------RSSIGVV 663
Cdd:PRK11701  16 YGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 ---PQDSTLFNDTILYNIKyAKPSATNEEIYAAAKAAQIH---------DRILQFPDGYnsrvgerglklSGGEKQRVAV 731
Cdd:PRK11701  95 hqhPRDGLRMQVSAGGNIG-ERLMAVGARHYGDIRATAGDwlerveidaARIDDLPTTF-----------SGGMQQRLQI 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 732 ARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAH-----RLStitnADLILCISNGRIVETG 800
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHdlavaRLL----AHRLLVMKQGRVVESG 234
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 610-783 3.84e-12

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 67.05  E-value: 3.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILlrffdvnSGSITIDDQDIrnvtlSSLRSSIGVVPQ----DSTLFNDTILYNI---KYAK 682
Cdd:cd03237   25 SEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDI-----EIELDTVSYKPQyikaDYEGTVRDLLSSItkdFYTH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 683 PSaTNEEIYAAAKAAQIHDRilQFPDgynsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAA 762
Cdd:cd03237   93 PY-FKTEIAKPLQIEQILDR--EVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157

                        170       180
                 ....*....|....*....|...
gi 162312131 763 LNRLA--SGRTAIVIAHRLSTIT 783
Cdd:cd03237  158 IRRFAenNEKTAFVVEHDIIMID 180
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 572-781 5.41e-12

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: 69.19  E-value: 5.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  572 PNAPDLKvtqGKVI-FSHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDqdirN 650
Cdd:TIGR03719 313 PPGPRLG---DKVIeAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE----T 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  651 VTLSSLRSSIGVVPQDSTLFndtilynikyakpsatnEEIYAAAKAAQIHDRilQFPD-GYNSRVGERGL-------KLS 722
Cdd:TIGR03719 385 VKLAYVDQSRDALDPNKTVW-----------------EEISGGLDIIKLGKR--EIPSrAYVGRFNFKGSdqqkkvgQLS 445

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131  723 GGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALnrLASGRTAIVIAH------RLST 781
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVVISHdrwfldRIAT 508
hmuV PRK13547
heme ABC transporter ATP-binding protein;
588-801 6.48e-12

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 66.77  E-value: 6.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 588 HVSFAYDPRKpVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN--------SGSITIDDQDIRNVTLSSLRSS 659
Cdd:PRK13547   6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDS----TLFNDTILYNIKYakPSATneeiyaAAKAAQIHDRILQFPD----GYNSRVGERGLKLSGGEKQRVAV 731
Cdd:PRK13547  85 RAVLPQAAqpafAFSAREIVLLGRY--PHAR------RAGALTHRDGEIAWQAlalaGATALVGRDVTTLSGGELARVQF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 732 ARAILK---------DPSIILLDEATSALDTNTERQIQAALNRLAS----GRTAIVIAHRLSTiTNADLILCISNGRIVE 798
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVA 235


                 ...
gi 162312131 799 TGT 801
Cdd:PRK13547 236 HGA 238
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 603-807 6.92e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 67.46  E-value: 6.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 603 INFVAQPGKVIALVGESGGGKS----TIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVvpQDSTLFND--TIL- 675
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGA--EVAMIFQDpmTSLn 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 676 --YNIKYakpsatneEIYAAAKAAQ------IHDRILQF------PDGyNSRVGERGLKLSGGEKQRVAVARAILKDPSI 741
Cdd:PRK11022 104 pcYTVGF--------QIMEAIKVHQggnkktRRQRAIDLlnqvgiPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLASGRTA--IVIAHRLSTITN-ADLILCISNGRIVETGTHEELIK 807
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFR 243
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 603-805 7.00e-12

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 66.55  E-value: 7.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 603 INFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlSSLRSSIGVVP--QDSTLFND-TILYNIK 679
Cdd:PRK11300  24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFREmTVIENLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 680 YAK---------------PSATNEEIYAAAKAAQIHDRI--LQFPdgyNSRVGerglKLSGGEKQRVAVARAILKDPSII 742
Cdd:PRK11300 103 VAQhqqlktglfsgllktPAFRRAESEALDRAATWLERVglLEHA---NRQAG----NLAYGQQRRLEIARCMVTQPEIL 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 743 LLDEATSALDTNTERQIQAALNRLAS--GRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 609-797 1.76e-11

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: 62.78  E-value: 1.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   609 PGKVIALVGESGGGKSTIMRILLRFFDVNSGS-ITIDDQDIRNVTLSSLRssigvvpqdstlfndtilynikyakpsatn 687
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   688 eeiyaaakaaqihdrilqfpdgyNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAA----- 762
Cdd:smart00382  51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 162312131   763 -LNRLASGRTAIVIAHRLSTITNADLILCISNGRIV 797
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
610-788 1.94e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 67.53  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILLRFFDVNSGSITID------------DQDirnVTLSSLRSSIGvvpqdsTLFNDTIlYN 677
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpDYD---GTVEDLLRSIT------DDLGSSY-YK 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 678 IKYAKPsatneeiyaaakaaqihdriLQFPDGYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSALDtnTER 757
Cdd:PRK13409 435 SEIIKP--------------------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQ 488

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 162312131 758 QIQAA--LNRLA--SGRTAIVIAHRLSTItnaDLI 788
Cdd:PRK13409 489 RLAVAkaIRRIAeeREATALVVDHDIYMI---DYI 520
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 595-797 2.67e-11

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: 63.82  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 595 PRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVN---SGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLfn 671
Cdd:cd03233   18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 dtilynikyakPSATNEE-IYAAAKAaQIHDRIlqfpdgynsrvgeRGLklSGGEKQRVAVARAILKDPSIILLDEATSA 750
Cdd:cd03233   96 -----------PTLTVREtLDFALRC-KGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRG 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162312131 751 LDTNTERQIQAALNRLA--SGRTAIVIAHRLSTITNA--DLILCISNGRIV 797
Cdd:cd03233  149 LDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQI 199
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 582-796 3.07e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 66.49  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFS--HVSfAYDP---RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILlrfFDV----NSGSITIDDQ--DIRN 650
Cdd:PRK13549 256 GEVILEvrNLT-AWDPvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCL---FGAypgrWEGEIFIDGKpvKIRN 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 651 vTLSSLRSSIGVVPQDSTlfNDTIL------YNI------KYAKPSATNEeiyaAAKAAQIHDRILQF------PDgynS 712
Cdd:PRK13549 332 -PQQAIAQGIAMVPEDRK--RDGIVpvmgvgKNItlaaldRFTGGSRIDD----AAELKTILESIQRLkvktasPE---L 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 713 RVGerglKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILC 790
Cdd:PRK13549 402 AIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLV 477


                 ....*.
gi 162312131 791 ISNGRI 796
Cdd:PRK13549 478 MHEGKL 483
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 268-558 3.41e-11

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: 64.81  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 268 CIVLLFLGRAVNILAPRQLGVLTEKLT--KHSEKIPWSDVILFVIYrFLQGnmgVIGSLRSFLWVPVSQYAYRAISTKAL 345
Cdd:cd18576    1 GLILLLLSSAIGLVFPLLAGQLIDAALggGDTASLNQIALLLLGLF-LLQA---VFSFFRIYLFARVGERVVADLRKDLY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 346 RHVLNLSYDFHLNKRAGEVLTALTK---------GSSLNTFAEQVVFQIGpvlldlGVAMVyFFIKFDIyfTLIVLImTL 416
Cdd:cd18576   77 RHLQRLPLSFFHERRVGELTSRLSNdvtqiqdtlTTTLAEFLRQILTLIG------GVVLL-FFISWKL--TLLMLA-TV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 417 CYCYVTVKITSWRTearRKMVNSWRESYAVQN----DAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLfslnfln 492
Cdd:cd18576  147 PVVVLVAVLFGRRI---RKLSKKVQDELAEANtiveETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRA------- 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 493 IVQGG-----IFTFSLAIACLL--SAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18576  217 RIRALfssfiIFLLFGAIVAVLwyGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 606-781 4.08e-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: 4.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 606 VAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSIT-----IDDQ-DIRNVtlssLRssigvvpqdstLFNDTILYNik 679
Cdd:COG1245   95 VPKKGKVTGILGPNGIGKSTALKIL-------SGELKpnlgdYDEEpSWDEV----LK-----------RFRGTELQD-- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 680 YAKPSAtNEEIYAAAKAAQIhDRILQFPDGYNS----RVGERGL-------------------KLSGGEKQRVAVARAIL 736
Cdd:COG1245  151 YFKKLA-NGEIKVAHKPQYV-DLIPKVFKGTVRelleKVDERGKldelaeklglenildrdisELSGGELQRVAIAAALL 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 162312131 737 KDPSIILLDEATSALDTNtERqIQAA--LNRLA-SGRTAIVIAHRLST 781
Cdd:COG1245  229 RDADFYFFDEPSSYLDIY-QR-LNVArlIRELAeEGKYVLVVEHDLAI 274
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
606-779 7.07e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 65.60  E-value: 7.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 606 VAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSItiddqdIRNvtlssLRSSIGVVPQDSTL--FNDTILYNikYAKP 683
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKIL-------SGEL------IPN-----LGDYEEEPSWDEVLkrFRGTELQN--YFKK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 684 SAtNEEIYAAAKAAQIhDRILQFPDGYNS----RVGERGL-------------------KLSGGEKQRVAVARAILKDPS 740
Cdd:PRK13409 155 LY-NGEIKVVHKPQYV-DLIPKVFKGKVRellkKVDERGKldevverlglenildrdisELSGGELQRVAIAAALLRDAD 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 162312131 741 IILLDEATSALDTNtERqIQAA--LNRLASGRTAIVIAHRL 779
Cdd:PRK13409 233 FYFFDEPTSYLDIR-QR-LNVArlIRELAEGKYVLVVEHDL 271
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 610-788 7.59e-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: 65.58  E-value: 7.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILLRFFDVNSGSITID------------DQDIRNVTLssLRSSIGVvPQDSTLFNdtilyn 677
Cdd:COG1245  366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyispDYDGTVEEF--LRSANTD-DFGSSYYK------ 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 678 ikyakpsatnEEIyaaAKAAQIHdRIlqfpdgYNSRVGErglkLSGGEKQRVAVARAILKDPSIILLDEATSALDtnTER 757
Cdd:COG1245  437 ----------TEI---IKPLGLE-KL------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQ 490

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 162312131 758 QIQAA--LNRLA--SGRTAIVIAHRLSTItnaDLI 788
Cdd:COG1245  491 RLAVAkaIRRFAenRGKTAMVVDHDIYLI---DYI 522
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 572-796 9.68e-11

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 65.23  E-value: 9.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  572 PNAPDlkvTQGKVIFS--HVSfAYDP----RKPVlSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFD-VNSGSITID 644
Cdd:TIGR02633 247 PHEPH---EIGDVILEarNLT-CWDVinphRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFIN 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  645 DQ--DIRNvTLSSLRSSIGVVPQDSTlfNDTIL------YNIKYA--KPSATNEEIYAAAKAAQIHDRILQF------PD 708
Cdd:TIGR02633 322 GKpvDIRN-PAQAIRAGIAMVPEDRK--RHGIVpilgvgKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLkvktasPF 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  709 GYNSRvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-AD 786
Cdd:TIGR02633 399 LPIGR-------LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSD 471

                         250
                  ....*....|
gi 162312131  787 LILCISNGRI 796
Cdd:TIGR02633 472 RVLVIGEGKL 481
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
597-808 1.09e-10

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 63.10  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQ--DIRNVTLSSLRSSIGVVPQD--STLFND 672
Cdd:PRK13638  14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpeQQIFYT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 TILYNIKYakpSATNEEIyAAAKAAQIHDRILQFPDGYNSRvgERGLK-LSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:PRK13638  94 DIDSDIAF---SLRNLGV-PEAEITRRVDEALTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 752 DTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK13638 168 DPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC 226
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
600-779 1.12e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 63.11  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSITIDD--------------------QDIRNVtlsslRSS 659
Cdd:PRK09984  20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKsagshiellgrtvqregrlaRDIRKS-----RAN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 660 IGVVPQDSTLFND-TILYNI---------------KYAKPSATNEEIYAAAKAAQIHdrilqfpdgynsRVGERGLKLSG 723
Cdd:PRK09984  88 TGYIFQQFNLVNRlSVLENVligalgstpfwrtcfSWFTREQKQRALQALTRVGMVH------------FAHQRVSTLSG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 724 GEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRL 779
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQV 213
GguA NF040905
sugar ABC transporter ATP-binding protein;
600-799 1.68e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 64.43  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNS--GSITIDDQDIRnvtLSSLRSS--IGVV---------PQD 666
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCR---FKDIRDSeaLGIViihqelaliPYL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 StlfndtILYNIKYAKPSATNEEI---YAAAKAAQIHDRI-LQfpDGYNSRVGERGLklsgGEKQRVAVARAILKDPSII 742
Cdd:NF040905  94 S------IAENIFLGNERAKRGVIdwnETNRRARELLAKVgLD--ESPDTLVTDIGV----GKQQLVEIAKALSKDVKLL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 743 LLDEATSALDtntERQIQAALNRL----ASGRTAIVIAHRLSTITN-ADLILCISNGRIVET 799
Cdd:NF040905 162 ILDEPTAALN---EEDSAALLDLLlelkAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 260-558 2.07e-10

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 62.58  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 260 RLQFQIFIC-IVLLFLGRAVNILAprQLgVLTEKLTKHSEKIPWSDVILFVIYRFLQGnmgVIGSLRSFLWVPVSQYAYR 338
Cdd:cd18568    2 KLLAEILLAsLLLQLLGLALPLFT--QI-ILDRVLVHKNISLLNLILIGLLIVGIFQI---LLSAVRQYLLDYFANRIDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 339 AISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSSLNTFAEQVVFQIgpvLLDLGVAMVYFFIKF--DIYFTLIVLIMTL 416
Cdd:cd18568   76 SLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTT---ILDLLMVFIYLGLMFyyNLQLTLIVLAFIP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 417 CYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDF-----ENeRYGHAVDIYLKQERKVlfslNFL 491
Cdd:cd18568  153 LYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPirwrwEN-KFAKALNTRFRGQKLS----IVL 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 492 NIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18568  228 QLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 594-808 2.25e-10

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 62.02  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 594 DPRKPVLSDINFVAQPGKVIALVGESGGGKS----TIMRILLRFFDVNSGSITIDDQ-----DIRNVTLSSL----RSSI 660
Cdd:PRK10418  13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapcALRGRKIATImqnpRSAF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 661 GVVPQDSTLFNDTILyniKYAKPsATNEEIYAAAKAAQIHD--RILQ-FPdgynsrvgergLKLSGGEKQRVAVARAILK 737
Cdd:PRK10418  93 NPLHTMHTHARETCL---ALGKP-ADDATLTAALEAVGLENaaRVLKlYP-----------FEMSGGMLQRMMIALALLC 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312131 738 DPSIILLDEATSALDTNTERQIQAALNRLASGRT--AIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKR 808
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 300-558 3.68e-10

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: 61.67  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 300 IPWSDVILFVIyrflqgnMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALT------KGSS 373
Cdd:cd18552   41 VPLAIIGLFLL-------RGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITndvnqvQNAL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 374 LNTFaeQVVFQIGPVLLDLGVAMVYFfikfDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMN 453
Cdd:cd18552  114 TSAL--TVLVRDPLTVIGLLGVLFYL----DWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSG 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 454 FETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLN-IVQggiFTFSLAIACLL--SAYRVTFGFNTVGDFVILLTY 530
Cdd:cd18552  188 IRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSpLME---LLGAIAIALVLwyGGYQVISGELTPGEFISFITA 264

                        250       260
                 ....*....|....*....|....*...
gi 162312131 531 MIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18552  265 LLLLYQPIKRLSNVNANLQRGLAAAERI 292
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 713-806 5.59e-10

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: 63.11  E-value: 5.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  713 RVGERGLKLSGGEKQRVAVARAILKD---PSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITNADLI 788
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYI 901

                          90       100
                  ....*....|....*....|....
gi 162312131  789 LCI------SNGRIVETGTHEELI 806
Cdd:TIGR00630 902 IDLgpeggdGGGTVVASGTPEEVA 925
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 597-802 8.54e-10

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 60.19  E-value: 8.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILL--RFFDVNSGSITIDDQDIRNVTLSSlRSSIGV---------VPQ 665
Cdd:PRK09580  14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIfmafqypveIPG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 DST-LFNDTILYNI-KYAKPSATNEEIYAAAKAAQIhdRILQFPDGYNSRVGERGLklSGGEKQRVAVARAILKDPSIIL 743
Cdd:PRK09580  93 VSNqFFLQTALNAVrSYRGQEPLDRFDFQDLMEEKI--ALLKMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPELCI 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 744 LDEATSALDTNTERQIQAALNRLASG-RTAIVIAH--RLSTITNADLILCISNGRIVETGTH 802
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 598-776 8.65e-10

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: 59.29  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIrnvtlsslrssigvvPQDSTLFNDTILY- 676
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---------------AEQRDEPHENILYl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  677 ----NIKYAKPSATNEEIYAAakaaqIHDRILQFPDGYNSRVGERGLK------LSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:TIGR01189  79 ghlpGLKPELSALENLHFWAA-----IHGGAQRTIEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDE 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 162312131  747 ATSALDTNTERQIqAALNRLASGRTAIVIA 776
Cdd:TIGR01189 154 PTTALDKAGVALL-AGLLRAHLARGGIVLL 182
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 590-784 1.51e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 61.50  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 590 SFAYdprKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILlrffdvnSGSITIDDQDI---RNVTLSSLRssigvvpQD 666
Cdd:PRK11147  12 SFSD---APLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLQ-------QD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 ------STLFnDTILYNIK----YAK------------PSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGL----- 719
Cdd:PRK11147  75 pprnveGTVY-DFVAEGIEeqaeYLKryhdishlvetdPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLdpdaa 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 720 --KLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTerqIQAALNRLASGRTAIV-IAHRLSTITN 784
Cdd:PRK11147 154 lsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfISHDRSFIRN 218
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 265-557 1.68e-09

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


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 59.83  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAP---RQL--GVLTEKLTKHSEKIPWSDVILFVIYRFLQGnmgVIGSLRSFLWVPVSQYAYRA 339
Cdd:cd18563    1 LILGFLLMLLGTALGLVPPyltKILidDVLIQLGPGGNTSLLLLLVLGLAGAYVLSA---LLGILRGRLLARLGERITAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 340 ISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSS-LNTF-AEQVVFQIGPVLLDLGVAMVYFFIkfDIYFTLIVLImtlc 417
Cdd:cd18563   78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDrLQDFlSDGLPDFLTNILMIIGIGVVLFSL--NWKLALLVLI---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 418 ycyvTVKITSWRTEARRKMVN--------SWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLN 489
Cdd:cd18563  152 ----PVPLVVWGSYFFWKKIRrlfhrqwrRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWA 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 490 FLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTER 557
Cdd:cd18563  228 TFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
PLN03073 PLN03073
ABC transporter F family; Provisional
 564-816 2.05e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 61.03  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 564 EKPTVVEKPNAPDLKvtqgkviFSHVSFAYdPRKPVL-SDINFVAQPGKVIALVGESGGGKSTIMRIllrffdvnsgsIT 642
Cdd:PLN03073 496 EFPTPDDRPGPPIIS-------FSDASFGY-PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKL-----------IS 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 643 IDDQDIRNVTLSSLRSSIGVVPQDST----LFNDTILYNIKyAKPSATNEEIYAAAKAAQIhdrilqfpdgynsrVGERG 718
Cdd:PLN03073 557 GELQPSSGTVFRSAKVRMAVFSQHHVdgldLSSNPLLYMMR-CFPGVPEQKLRAHLGSFGV--------------TGNLA 621

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 719 LK----LSGGEKQRVAVARAILKDPSIILLDEATSALDTNTerqIQAALNRLASGRTAI-VIAHRLSTITNA-DLILCIS 792
Cdd:PLN03073 622 LQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVlMVSHDEHLISGSvDELWVVS 698

                        250       260
                 ....*....|....*....|....*
gi 162312131 793 NGRIVE-TGTHEElikrdggaYKKM 816
Cdd:PLN03073 699 EGKVTPfHGTFHD--------YKKT 715
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 584-804 2.37e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 60.68  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 584 VIFSHVSFAYDPRkPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIddqdirnvtlsSLRSSIGVV 663
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------SENANIGYY 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 664 PQDST--LFNDTILYN--IKYAKPSATNEEIYAaakaaqIHDRILQFPDGYNSRVGerglKLSGGEKQRVAVARAILKDP 739
Cdd:PRK15064 388 AQDHAydFENDLTLFDwmSQWRQEGDDEQAVRG------TLGRLLFSQDDIKKSVK----VLSGGEKGRMLFGKLMMQKP 457

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 740 SIILLDEATSALDTNTERQIQAALNRLASgrTAIVIAH-R--LSTItnADLILCISNGRIVE-TGTHEE 804
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYEE 522
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 265-558 4.60e-09

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


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 58.60  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSekIPWSDVILFVIYRFLQGnmgVIGSLRSFLWVPVSQYAYRAISTKA 344
Cdd:cd18551    1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG--SSGGLLALLVALFLLQA---VLSALSSYLLGRTGERVVLDLRRRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 345 LRHVLNLSYDFHLNKRAGEVLTALTKGSSL--NTFAEQVVFQIGPVLLDLGVAMVYFFIkfDIYFTLIVLIMTLCYCYVT 422
Cdd:cd18551   76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLlrELITSGLPQLVTGVLTVVGAVVLMFLL--DWVLTLVTLAVVPLAFLII 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 423 VKITswrtearRKMVnswRESYAVQND----------AIMNFETVKNFDADDFENER-YGHAVDIYlKQERKVLFSLNFL 491
Cdd:cd18551  154 LPLG-------RRIR---KASKRAQDAlgelsaalerALSAIRTVKASNAEERETKRgGEAAERLY-RAGLKAAKIEALI 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 492 NIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18551  223 GPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 527-779 5.27e-09

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: 60.41  E-value: 5.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   527 LLTYMIQLQqplnFFGTLY--RSLQNSIIDTERllEIFEEKPTVVEKPNAPD-LKVTQGKVIFSHVSfaydprKPVLSDI 603
Cdd:TIGR01257 1891 LLTLLIQHH----FFLSRWiaEPAKEPIFDEDD--DVAEERQRIISGGNKTDiLRLNELTKVYSGTS------SPAVDRL 1958

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   604 NFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGVVPQ----DSTLFNDTILYniK 679
Cdd:TIGR01257 1959 CVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaiDDLLTGREHLY--L 2035

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   680 YAKPSAT-NEEIYAAAkaaqihdrilqfpdgyNSRVGERGLKL---------SGGEKQRVAVARAILKDPSIILLDEATS 749
Cdd:TIGR01257 2036 YARLRGVpAEEIEKVA----------------NWSIQSLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTT 2099

                          250       260       270
                   ....*....|....*....|....*....|.
gi 162312131   750 ALDTNTERQI-QAALNRLASGRTAIVIAHRL 779
Cdd:TIGR01257 2100 GMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 556-780 5.71e-09

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: 59.76  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  556 ERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFD 635
Cdd:TIGR00954 424 EEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP 503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  636 VNSGSITID-DQDIRNV------TLSSLRssigvvpqDSTLFNDTILYNIKYAKPSATNEEIYaaaKAAQIHDrILQFPD 708
Cdd:TIGR00954 504 VYGGRLTKPaKGKLFYVpqrpymTLGTLR--------DQIIYPDSSEDMKRRGLSDKDLEQIL---DNVQLTH-ILEREG 571

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131  709 GYNSrVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLasGRTAIVIAHRLS 780
Cdd:TIGR00954 572 GWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 713-801 8.07e-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: 57.24  E-value: 8.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 713 RVGERGLKLSGGEKQRVAVARAILK---DPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLI 788
Cdd:cd03271  162 KLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWI 241

                         90
                 ....*....|....*....
gi 162312131 789 LCIS------NGRIVETGT 801
Cdd:cd03271  242 IDLGpeggdgGGQVVASGT 260
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 582-777 9.63e-09

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 55.96  E-value: 9.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIFSHVSFAYDPrkpvlsdinfvaqpGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIG 661
Cdd:cd03231   12 GRALFSGLSFTLAA--------------GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 662 VVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAkaaqihdrilqfpdgynSRVGERGLK------LSGGEKQRVAVARAI 735
Cdd:cd03231   78 LGHAPGIKTTLSVLENLRFWHADHSDEQVEEAL-----------------ARVGLNGFEdrpvaqLSAGQQRRVALARLL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 162312131 736 LKDPSIILLDEATSALDTNTERQIQAAL-NRLASGRTAIVIAH 777
Cdd:cd03231  141 LSGRPLWILDEPTTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 600-816 9.78e-09

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 57.79  E-value: 9.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRIL---LRffdVNSGSITIDDQDI---RNvtlsSLRSSIGVV-PQDSTLFND 672
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgiLV---PTSGEVRVLGYVPfkrRK----EFARRIGVVfGQRSQLWWD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 673 TIL---YNIkyakpsatNEEIYaaakaaQIHDRIlqfpdgYNSRVGE---------------RglKLSGGEKQRVAVARA 734
Cdd:COG4586  111 LPAidsFRL--------LKAIY------RIPDAE------YKKRLDElvelldlgelldtpvR--QLSLGQRMRCELAAA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRdGG 811
Cdd:COG4586  169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER-FG 247


                 ....*
gi 162312131 812 AYKKM 816
Cdd:COG4586  248 PYKTI 252
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 721-800 9.95e-09

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: 55.41  E-value: 9.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAILKDP--SIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITNADLILCI------ 791
Cdd:cd03238   88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFgpgsgk 167


                 ....*....
gi 162312131 792 SNGRIVETG 800
Cdd:cd03238  168 SGGKVVFSG 176
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 596-807 1.12e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 58.59  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 596 RKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT-----------LSSLRSSIGVVP 664
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYA 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 665 QDSTLFNdTILYNIKYAKPSA---TNEEIYAAAKAAqIHDRILQFPdGYNSRVGErglkLSGGEKQRVAVARAILKDPSI 741
Cdd:PRK10982 340 YLDIGFN-SLISNIRNYKNKVgllDNSRMKSDTQWV-IDSMRVKTP-GHRTQIGS----LSGGNQQKVIIGRWLLTQPEI 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLASGRTAIVIAH----RLSTITnaDLILCISNGR---IVETG--THEELIK 807
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISsempELLGIT--DRILVMSNGLvagIVDTKttTQNEILR 485
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
610-806 1.74e-08

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 57.12  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMRILLRF----FDVNSGSITIDDQDIRNVTLSSLRSSIG-------VVPQDSTLFNDTILYNI 678
Cdd:PRK15093  33 GEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsmifQEPQSCLDPSERVGRQL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 679 KYAKPSATneeiYAAAKAAQIHDR------ILQfpdgynsRVGERGLK---------LSGGEKQRVAVARAILKDPSIIL 743
Cdd:PRK15093 113 MQNIPGWT----YKGRWWQRFGWRkrraieLLH-------RVGIKDHKdamrsfpyeLTEGECQKVMIAIALANQPRLLI 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 744 LDEATSALDTNTERQIQAALNRL--ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELI 806
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 572-777 1.91e-08

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 57.82  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 572 PNAPDLKvtqGKVI-FSHVSFAYDPRkpVL-SDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDqdir 649
Cdd:PRK11819 315 PPGPRLG---DKVIeAENLSKSFGDR--LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE---- 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 650 NVTLSSLRSSIGVVPQDSTLF------NDTILYNiKYAKPSATneeiYAAAkaaqihdrilqF----PDgYNSRVGErgl 719
Cdd:PRK11819 386 TVKLAYVDQSRDALDPNKTVWeeisggLDIIKVG-NREIPSRA----YVGR-----------FnfkgGD-QQKKVGV--- 445

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 720 kLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASgrTAIVIAH 777
Cdd:PRK11819 446 -LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPG--CAVVISH 500
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
573-807 1.92e-08

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 57.87  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 573 NAPDLKVTQGKVIFSHVSFAYDPRKPVlSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIR-NV 651
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRS 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 652 TLSSLRSSIGVVPQ---DSTLF-NDTILYNIKYAkPSATNEEIYAA---------AKAAQIHDRILQFP-DGYNSRVGEr 717
Cdd:PRK09700 332 PLDAVKKGMAYITEsrrDNGFFpNFSIAQNMAIS-RSLKDGGYKGAmglfhevdeQRTAENQRELLALKcHSVNQNITE- 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 718 glkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTI-TNADLILCISNGR 795
Cdd:PRK09700 410 ---LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIiTVCDRIAVFCEGR 486

                        250
                 ....*....|....*...
gi 162312131 796 IVE------TGTHEELIK 807
Cdd:PRK09700 487 LTQiltnrdDMSEEEIMA 504
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 305-558 4.37e-08

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


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 55.53  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 305 VILFVIYrFLQGnmgVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSSLNTFAEQVVFQ 384
Cdd:cd18570   46 IGLILLY-LFQS---LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTIS 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 385 IgpvLLDLGVAMVYFFIKFDIYFTL--IVLIMTLCYCyvtvkITSWRTEAR-RKMVNSWRESYAVQN----DAIMNFETV 457
Cdd:cd18570  122 L---FLDLLMVIISGIILFFYNWKLflITLLIIPLYI-----LIILLFNKPfKKKNREVMESNAELNsyliESLKGIETI 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 458 KNFDAddfENERYGHAVDIYLKQERKVlFSLNFLNIVQGGIFTF--SLAIACLL--SAYRVTFGFNTVGD---FVILLTY 530
Cdd:cd18570  194 KSLNA---EEQFLKKIEKKFSKLLKKS-FKLGKLSNLQSSIKGLisLIGSLLILwiGSYLVIKGQLSLGQliaFNALLGY 269

                        250       260
                 ....*....|....*....|....*...
gi 162312131 531 MIqlqQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18570  270 FL---GPIENLINLQPKIQEAKVAADRL 294
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
598-777 4.74e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.47  E-value: 4.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVP---QD-STLFNDT 673
Cdd:PRK13543  25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPglkADlSTLENLH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 674 ILYNIKYAKPSATNEEIYAAAKAAQIHDRILQfpdgynsrvgerglKLSGGEKQRVAVARAILKDPSIILLDEATSALD- 752
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR--------------QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDl 170

                        170       180
                 ....*....|....*....|....*...
gi 162312131 753 ---TNTERQIQAALNrlaSGRTAIVIAH 777
Cdd:PRK13543 171 egiTLVNRMISAHLR---GGGAALVTTH 195
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 600-805 5.65e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 56.28  E-value: 5.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 600 LSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIrNVTLS--SLRSSIGVVPQDSTLFND-TILY 676
Cdd:PRK10982  14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkeALENGISMVHQELNLVLQrSVMD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 NI---KYAK--PSATNEEIYAAAKAaqIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:PRK10982  93 NMwlgRYPTkgMFVDQDKMYRDTKA--IFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 752 dtnTERQIQ---AALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEEL 805
Cdd:PRK10982 166 ---TEKEVNhlfTIIRKLkERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 597-796 6.14e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.21  E-value: 6.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLS----------DINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNV-TLSSLRSSIGVVPQ 665
Cdd:PRK15439 266 APVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLPE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 666 D---STLFND--------TILYN-----IKYAKPSATNEEIYAAAKaaqihdriLQFPDGyNSRVGerglKLSGGEKQRV 729
Cdd:PRK15439 346 DrqsSGLYLDaplawnvcALTHNrrgfwIKPARENAVLERYRRALN--------IKFNHA-EQAAR----TLSGGNQQKV 412

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312131 730 AVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIV-IAHRLSTITN-ADLILCISNGRI 796
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 719-783 7.23e-08

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: 52.96  E-value: 7.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131 719 LKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA--SGRTAIVIAHRLSTIT 783
Cdd:cd03222   70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLD 136
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 606-791 1.01e-07

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: 53.91  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 606 VAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITiDDQDIRNVtLSSLRssiGVVPQDstLFNDTILYNIKYAKPSA 685
Cdd:cd03236   22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI-LDEFR---GSELQN--YFTKLLEGDVKVIVKPQ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 686 TNEEIYAAAKAA------QIHDRilQFPDGYNSRVGERGL------KLSGGEKQRVAVARAILKDPSIILLDEATSALDT 753
Cdd:cd03236   95 YVDLIPKAVKGKvgellkKKDER--GKLDELVDQLELRHVldrnidQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 162312131 754 NTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILCI 791
Cdd:cd03236  173 KQRLNAARLIRELAEdDNYVLVVEHDLAVLDYlSDYIHCL 212
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 553-782 1.08e-07

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.89  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   553 IDTERLlEIFEEKPTVVEKPNAPDLKVTQ---GKVIFSHVSFAYD-----PRKPVLSDINFVAQPGKVIALVGESGGGKS 624
Cdd:TIGR00956  725 NDIEAG-EVLGSTDLTDESDDVNDEKDMEkesGEDIFHWRNLTYEvkikkEKRVILNNVDGWVKPGTLTALMGASGAGKT 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   625 TIMRILLRffDVNSGSITIDDQDIRNVTL-SSLRSSIGVVPQ-DSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHD- 701
Cdd:TIGR00956  804 TLLNVLAE--RVTTGVITGGDRLVNGRPLdSSFQRSIGYVQQqDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEv 881

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   702 -RILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDP-SIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHR 778
Cdd:TIGR00956  882 iKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQ 961


                   ....
gi 162312131   779 LSTI 782
Cdd:TIGR00956  962 PSAI 965
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 265-558 1.12e-07

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 54.44  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLL-FLGRAVNILAPrqlgVLTEKLTKH---SEKIPWSDVIL--FVIYRFLQGnmgVIGSLRSFLWVPVSQYAYR 338
Cdd:cd18555    3 LLISILLLsLLLQLLTLLIP----ILTQYVIDNvivPGNLNLLNVLGigILILFLLYG---LFSFLRGYIIIKLQTKLDK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 339 AISTKALRHVLNLSYDFHLNKRAGEVLTALtkgSSLNTFAEQVVFQIGPVLLDLGVAMVYFF--IKFDIYFTLIVLIMTL 416
Cdd:cd18555   76 SLMSDFFEHLLKLPYSFFENRSSGDLLFRA---NSNVYIRQILSNQVISLIIDLLLLVIYLIymLYYSPLLTLIVLLLGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 417 CYCYVTVkITSWRT-EARRKMVNSWRESYAVQNDAIMNFETVKNFDAddfENERYGHAVDIYLKQ---ERKVLFSLNFLN 492
Cdd:cd18555  153 LIVLLLL-LTRKKIkKLNQEEIVAQTKVQSYLTETLYGIETIKSLGS---EKNIYKKWENLFKKQlkaFKKKERLSNILN 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312131 493 IVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18555  229 SISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
597-777 1.50e-07

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 52.50  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRnvtlsSLRSSigvvpqdstlFNDTILY 676
Cdd:PRK13538  14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDE----------YHQDLLY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 677 nIKYA---KPSATNEE---IYAA----AKAAQIHDrILQfpdgynsRVGERGLK------LSGGEKQRVAVARAILKDPS 740
Cdd:PRK13538  79 -LGHQpgiKTELTALEnlrFYQRlhgpGDDEALWE-ALA-------QVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAP 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 162312131 741 IILLDEATSALDTNTERQIQAALNR-LASGRTAIVIAH 777
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
 341-558 1.56e-07

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350013 [Multi-domain]  Cd Length: 294  Bit Score: 53.63  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 341 STKALRHVLNLSYDFHLNKRAGEVLTALtkgSSLNTFAEQVVFQIGPVLLDLGVAMVYFFI--KFDIYFTLIVLIMTLCY 418
Cdd:cd18569   78 SSRFFWHVLRLPVEFFSQRYAGDIASRV---QSNDRVANLLSGQLATTVLNLVMAVFYALLmlQYDVPLTLIGIAIALLN 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 419 CYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDA-DDFENERYGHAVDiYLKQERKVLFSLNFLNIVQGG 497
Cdd:cd18569  155 LLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAeSDFFSRWAGYQAK-VLNAQQELGRTNQLLGALPTL 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 498 IFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18569  234 LSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 597-786 2.52e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 51.87  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 597 KPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNvTLSSLRSSIGVVPQDSTL-----FN 671
Cdd:PRK13540  14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGInpyltLR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 672 DTILYNIKYakpSATNEEIYAAAKAAQIhDRILQFPDGYnsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSAL 751
Cdd:PRK13540  93 ENCLYDIHF---SPGAVGITELCRLFSL-EHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 162312131 752 DtntERQIQAALNRL----ASGRTAIVIAHRLSTITNAD 786
Cdd:PRK13540 159 D---ELSLLTIITKIqehrAKGGAVLLTSHQDLPLNKAD 194
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 265-557 3.13e-07

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


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 52.79  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSD--------VILFVIYrflqgnmgVIGSLRSFLW----VPV 332
Cdd:cd18547    1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDfsgllrilLLLLGLY--------LLSALFSYLQnrlmARV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 333 SQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTK-----GSSLNTFAEQV---VFQIgpvlldlgVAMVYFFIKFD 404
Cdd:cd18547   73 SQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNdvdniSQALSQSLTQLissILTI--------VGTLIMMLYIS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 405 IYFTLIVLIMTLCYCYVTVKITSWrteARRKMVNSWR----------ESYAvqndaimNFETVKNFDADDFENERYGHAV 474
Cdd:cd18547  145 PLLTLIVLVTVPLSLLVTKFIAKR---SQKYFRKQQKalgelngyieEMIS-------GQKVVKAFNREEEAIEEFDEIN 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 475 DIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIID 554
Cdd:cd18547  215 EELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAG 294


                 ...
gi 162312131 555 TER 557
Cdd:cd18547  295 AER 297
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 598-796 6.61e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 52.70  E-value: 6.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 598 PVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVT-----------LSSLRSSIGVVPQD 666
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyISEDRKRDGLVLGM 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STLFNDTiLYNIKYAkpSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLkLSGGEKQRVAVARAILKDPSIILLDE 746
Cdd:PRK10762 346 SVKENMS-LTALRYF--SRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 747 ATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITN-ADLILCISNGRI 796
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFkAEGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 563-783 7.80e-07

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 53.19  E-value: 7.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   563 EEKPTVvekPNAPdLKVTqgKVIFSHV-SFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRIL---LRFFDVNS 638
Cdd:TIGR00956   45 DYQPTF---PNAL-LKIL--TRGFRKLkKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasnTDGFHIGV 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131   639 GSIT----IDDQDIRN-VTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPS----ATNEEIYAAaKAAQIHDRILQFPDG 709
Cdd:TIGR00956  119 EGVItydgITPEEIKKhYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrpdGVSREEYAK-HIADVYMATYGLSHT 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312131   710 YNSRVGE---RGLklSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALnrlasgRTAIVIAHRLSTIT 783
Cdd:TIGR00956  198 RNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVA 266
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 272-557 1.74e-06

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: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 50.64  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 272 LFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSD-----VILFVIYRFLqgnmGVIGSLRSFLWVPVSQYAYRAISTKALR 346
Cdd:cd18565   20 LLIGVAIDAVFNGEASFLPLVPASLGPADPRGQlwllgGLTVAAFLLE----SLFQYLSGVLWRRFAQRVQHDLRTDTYD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 347 HVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLGVAMVYFFIkFDIYFTLIVLIMTLcycyVTVKI 425
Cdd:cd18565   96 HVQRLDMAFFEDRQTGDLMSVLNNDvNQLERFLDDGANSIIRVVVTVLGIGAILFY-LNWQLALVALLPVP----LIIAG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 426 TSW---RTEARRKMVnswRESYAVQN----DAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVL-------FSLNFL 491
Cdd:cd18565  171 TYWfqrRIEPRYRAV---REAVGDLNarleNNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIrlraaffPVIRLV 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131 492 NIVqGGIFTFslaiacLLSAYRVTFGFN------TVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTER 557
Cdd:cd18565  248 AGA-GFVATF------VVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKR 312
uvrA PRK00349
excinuclease ABC subunit UvrA;
721-807 2.20e-06

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 51.61  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAILKDP---SIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITNADLILCI----- 791
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVdKGNTVVVIEHNLDVIKTADWIIDLgpegg 910

                         90
                 ....*....|....*..
gi 162312131 792 -SNGRIVETGTHEELIK 807
Cdd:PRK00349 911 dGGGEIVATGTPEEVAK 927
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 268-558 2.41e-06

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 50.25  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 268 CIVLLFLGRAVNILAPRQLGVLTEKL--TKHSEKIPWSDVILFVIYrFLQGnmgVIGSLRSFLWVPVSQYAYRAISTKAL 345
Cdd:cd18557    1 GLLFLLISSAAQLLLPYLIGRLIDTIikGGDLDVLNELALILLAIY-LLQS---VFTFVRYYLFNIAGERIVARLRRDLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 346 RHVLNLSYDFHLNKRAGEVLTALTKGSSL--NTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIyfTLIVLIMTLCYCYVTV 423
Cdd:cd18557   77 SSLLRQEIAFFDKHKTGELTSRLSSDTSVlqSAVTDNLSQLLRNILQVIGGLIILFILSWKL--TLVLLLVIPLLLIASK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 424 KITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSL 503
Cdd:cd18557  155 IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 504 AIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERL 558
Cdd:cd18557  235 LLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
PLN03073 PLN03073
ABC transporter F family; Provisional
 610-777 5.42e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 50.24  E-value: 5.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 610 GKVIALVGESGGGKSTIMR---------------ILLRFFDVNSGSIT----IDDQDIRNVTLssLRSSIGVVPQDSTLF 670
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEVVGDDTTalqcVLNTDIERTQL--LEEEAQLVAQQRELE 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 671 NDTILYNIKYAKPSATNEEIyAAAKAAQIHDRiLQFPDGYN--SRVGE--RGLKL------------SGGEKQRVAVARA 734
Cdd:PLN03073 281 FETETGKGKGANKDGVDKDA-VSQRLEEIYKR-LELIDAYTaeARAASilAGLSFtpemqvkatktfSGGWRMRIALARA 358

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALnrLASGRTAIVIAH 777
Cdd:PLN03073 359 LFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
721-807 6.32e-06

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 50.02  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAILK---DPSIILLDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLIlcI----- 791
Cdd:COG0178  827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLvDKGNTVVVIEHNLDVIKTADWI--Idlgpe 904

                         90
                 ....*....|....*....
gi 162312131 792 --SN-GRIVETGTHEELIK 807
Cdd:COG0178  905 ggDGgGEIVAEGTPEEVAK 923
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 266-544 6.93e-06

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


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 48.58  E-value: 6.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 266 FICIVLLFLGRAVNILAPRQLGVLTEK-LTKHSEKIPWSDVILFVIYRFLQGnmgVIGSLRSFLWVPVSQYAYRAISTKA 344
Cdd:cd18542    2 LLAILALLLATALNLLIPLLIRRIIDSvIGGGLRELLWLLALLILGVALLRG---VFRYLQGYLAEKASQKVAYDLRNDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 345 LRHVLNLSYDFHLNKRAGEVLTALTkgSSLNT---FAEQVVFQIGPVLLDLGVAMVYFFIkFDIYFTLIVLIMTLCycyv 421
Cdd:cd18542   79 YDHLQRLSFSFHDKARTGDLMSRCT--SDVDTirrFLAFGLVELVRAVLLFIGALIIMFS-INWKLTLISLAIIPF---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 422 tVKITSWRTEAR-RKMVNSWRESYAVQNDA----IMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSL-NFLNIVQ 495
Cdd:cd18542  152 -IALFSYVFFKKvRPAFEEIREQEGELNTVlqenLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLaKYWPLMD 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 162312131 496 GgIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTL 544
Cdd:cd18542  231 F-LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRL 278
GguA NF040905
sugar ABC transporter ATP-binding protein;
594-797 8.87e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 594 DPRKPVLSDINFVAQPGKVIALVGESGGGKSTI-MRILLRFFDVN-SGSITIDDQ--DIRNVTlSSLRSSIGVVPQDST- 668
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKevDVSTVS-DAIDAGLAYVTEDRKg 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 669 ---LFNDTILYNIKYAKPSA--------TNEEIYAAAkaaqihdrilQFPDGYNSR---VGERGLKLSGGEKQRVAVARA 734
Cdd:NF040905 349 yglNLIDDIKRNITLANLGKvsrrgvidENEEIKVAE----------EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSKW 418

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 735 ILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRL-STITNADLILCISNGRIV 797
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELpELLGMCDRIYVMNEGRIT 483
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 265-557 1.10e-05

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


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 48.15  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKA 344
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 345 LRHVLNLSYDFHLNKRAGEVLTALTkgS---SLNTFAEQVVFQ-IGPVLLDLGVAMVYFFIkfDIYFTLIVLIMTLCYCY 420
Cdd:cd18544   81 FSHIQRLPLSFFDRTPVGRLVTRVT--NdteALNELFTSGLVTlIGDLLLLIGILIAMFLL--NWRLALISLLVLPLLLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 421 VTVKITSWRTEARRKMvnswRESYAVQN----DAIMNFETVKNFDADDFENERYGHAVDIYLKQERK--VLFSLnFLNIV 494
Cdd:cd18544  157 ATYLFRKKSRKAYREV----REKLSRLNaflqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKsiKLFAL-FRPLV 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 495 QggiFTFSLAIACLL--SAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTER 557
Cdd:cd18544  232 E---LLSSLALALVLwyGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAER 293
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 701-789 2.07e-05

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: 46.30  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 701 DRILQFPDGYNSRVGerglKLSGGEKQRVAVAR--AILK-DPS-IILLDEATSALD-TNTERQIQaALNRLASGRTAIVI 775
Cdd:cd03278   98 SEIIEAPGKKVQRLS----LLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDdANVERFAR-LLKEFSKETQFIVI 172

                         90
                 ....*....|....
gi 162312131 776 AHRLSTITNADLIL 789
Cdd:cd03278  173 THRKGTMEAADRLY 186
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 599-788 2.17e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.02  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 599 VLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTlsslRSSIGVVPQDSTLFND-TILYN 677
Cdd:PRK13541  15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLKLEmTVFEN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 678 IKY-AKPSATNEEIYAAAKAAQIHDRIlqfpdgynsrvGERGLKLSGGEKQRVAVARAILKDPSIILLDEatsaLDTNTE 756
Cdd:PRK13541  91 LKFwSEIYNSAETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDE----VETNLS 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 162312131 757 RQIQAALNRLA-----SGRTAIVIAHRLSTITNADLI 788
Cdd:PRK13541 156 KENRDLLNNLIvmkanSGGIVLLSSHLESSIKSAQIL 192
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 721-809 2.37e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 48.29  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  721 LSGGEKQRVAVARAIL---KDPSIILLDEATSALDTNTERQ-IQAALNRLASGRTAIVIAHRLSTITNADLILCIS---- 792
Cdd:PRK00635  810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpegg 889

                          90
                  ....*....|....*....
gi 162312131  793 --NGRIVETGTHEELIKRD 809
Cdd:PRK00635  890 nlGGYLLASCSPEELIHLH 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 721-789 3.67e-05

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: 47.74  E-value: 3.67e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131   721 LSGGEKQRVAVAR--AILK-DPS-IILLDEATSALD-TNTERqiQAALNRLASGRTA-IVIAHRLSTITNADLIL 789
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFKvKPApFCILDEVDAPLDdANVER--FANLLKEFSKNTQfIVITHNKGTMEVADQLY 1162
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 265-558 4.19e-05

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


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 46.35  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVIL------FVIYRFLQGNMGVIGSLRSFL---------W 329
Cdd:cd18564    1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPllgpdpLALLLLAAAALVGIALLRGLAsyagtyltaL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 330 VpvSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKG-SSLNTFAEQVVFQIGPVLLDLgVAMVYFFIKFDIYFT 408
Cdd:cd18564   81 V--GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDvGAIQDLLVSGVLPLLTNLLTL-VGMLGVMFWLDWQLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 409 LIVLIMT----LCYCYVTVKITSWRTEARRkmvnswRES--YAVQNDAIMNFETVKNFDADDFENERYGHA----VDIYL 478
Cdd:cd18564  158 LIALAVAplllLAARRFSRRIKEASREQRR------REGalASVAQESLSAIRVVQAFGREEHEERRFAREnrksLRAGL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 479 KQER-KVLFSLnflniVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTER 557
Cdd:cd18564  232 RAARlQALLSP-----VVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAER 306


                 .
gi 162312131 558 L 558
Cdd:cd18564  307 V 307
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 602-789 4.45e-05

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: 44.66  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 602 DINFVaqPGKVIALVGESGGGKSTIMRillrffdvnsgsitiddqdirnvtlsslrsSIGVVpqdstlfndTILYNIKYA 681
Cdd:cd03227   15 DVTFG--EGSLTIITGPNGSGKSTILD------------------------------AIGLA---------LGGAQSATR 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 682 KPSATNEEIYAAAKAAQIHDRILQfpdgynsrvgerglkLSGGEKQRVAVARAI----LKDPSIILLDEATSALDT-NTE 756
Cdd:cd03227   54 RRSGVKAGCIVAAVSAELIFTRLQ---------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPrDGQ 118

                        170       180       190
                 ....*....|....*....|....*....|...
gi 162312131 757 RQIQAALNRLASGRTAIVIAHRLSTITNADLIL 789
Cdd:cd03227  119 ALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 714-794 5.17e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.13  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  714 VGERGLKLSGGEKQRVAVARAIL---KDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITNADLIL 789
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSlGHSVIYIDHDPALLKQADYLI 1772


                  ....*
gi 162312131  790 CISNG 794
Cdd:PRK00635 1773 EMGPG 1777
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
601-804 6.19e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 46.44  E-value: 6.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 601 SDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRnvtLSSLRSSI--------------GVVPQD 666
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIragimlcpedrkaeGIIPVH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 667 STlfNDTIlyNIKYAKPSATNEEIYAAAKAAQIHDRILQfpdgyNSRVGERGLK-----LSGGEKQRVAVARAILKDPSI 741
Cdd:PRK11288 347 SV--ADNI--NISARRHHLRAGCLINNRWEAENADRFIR-----SLNIKTPSREqlimnLSGGNQQKAILGRWLSEDMKV 417

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312131 742 ILLDEATSALDTNTERQIQAALNRLA-SGRTAIVIAHRLSTITN-ADLILCISNGRIVETGTHEE 804
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
PRK01156 PRK01156
chromosome segregation protein; Provisional
 710-795 1.25e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 45.66  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 710 YNSRVGERGL-----KLSGGEKQ------RVAVARAILKDPSIILLDEATSALD----TNTERQIQAALNRLASGRTAIV 774
Cdd:PRK01156 786 FNITVSRGGMvegidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrrTNLKDIIEYSLKDSSDIPQVIM 865

                         90       100
                 ....*....|....*....|...
gi 162312131 775 IAHRLSTITNADLILCI--SNGR 795
Cdd:PRK01156 866 ISHHRELLSVADVAYEVkkSSGS 888
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
692-811 1.30e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.11  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 692 AAAKAAQIHDRIlqfpdGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLA-SGR 770
Cdd:NF000106 121 ARARADELLERF-----SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGA 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 162312131 771 TAIVIAHRLSTITN-ADLILCISNGRIVETGTHEELIKRDGG 811
Cdd:NF000106 196 TVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGG 237
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 582-755 2.06e-04

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 44.94  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 582 GKVIF--SHVSFAYDpRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSI------------------ 641
Cdd:PRK11147 316 GKIVFemENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhrael 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 642 ----TIDD------QDI------RNVtLSSLrssigvvpQDstlfndtILYNIKYAKpsatneeiyAAAKAaqihdrilq 705
Cdd:PRK11147 395 dpekTVMDnlaegkQEVmvngrpRHV-LGYL--------QD-------FLFHPKRAM---------TPVKA--------- 440

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312131 706 fpdgynsrvgerglkLSGGEKQRVAVARAILKDPSIILLDEATSALDTNT 755
Cdd:PRK11147 441 ---------------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
PLN03140 PLN03140
ABC transporter G family member; Provisional
 594-801 2.14e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 45.22  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  594 DPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMrillrffDVNSGSIT--IDDQDIRnvtlsslrssIGVVPQDSTLFN 671
Cdd:PLN03140  890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKTggYIEGDIR----------ISGFPKKQETFA 952

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  672 DTILY--NIKYAKPSATNEE--IYAA--------AKAAQIH--DRILQFPDGYNSR---VGERGLK-LSGGEKQRVAVAR 733
Cdd:PLN03140  953 RISGYceQNDIHSPQVTVREslIYSAflrlpkevSKEEKMMfvDEVMELVELDNLKdaiVGLPGVTgLSTEQRKRLTIAV 1032

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312131  734 AILKDPSIILLDEATSALDTNTERQIQAAL-NRLASGRTAIVIAHRLST-ITNA--DLILCISNGRIVETGT 801
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfdELLLMKRGGQVIYSGP 1104
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 265-538 2.61e-04

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: 43.94  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 265 IFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSekIPWSDVILFVIYRFLqgnMGVIGSLRSFLWVPVSQYAYRAIS--- 341
Cdd:cd18541    1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGT--LTASQLLRYALLILL---LALLIGIFRFLWRYLIFGASRRIEydl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 342 -TKALRHVLNLSYDFHLNKRAGEVLTALTkgSSLNtfaeQVVFQIGPVLL---D---LGVAMVYFFIKFDIYFTLIVLI- 413
Cdd:cd18541   76 rNDLFAHLLTLSPSFYQKNRTGDLMARAT--NDLN----AVRMALGPGILylvDalfLGVLVLVMMFTISPKLTLIALLp 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 414 ---MTLCYCYVTVKITSwRTEARRkmvnswrESYAVQNDAIM-NFE---TVKNFDADDFENERYGHAVDIYLKQERKVLF 486
Cdd:cd18541  150 lplLALLVYRLGKKIHK-RFRKVQ-------EAFSDLSDRVQeSFSgirVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162312131 487 SLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPL 538
Cdd:cd18541  222 VDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPM 273
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 721-786 3.58e-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: 44.19  E-value: 3.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131   721 LSGGEKQRVAVA--RAILK-DPS-IILLDEATSALDtNTERQIQAALNRLASGRT-AIVIAHRLSTITNAD 786
Cdd:pfam02463 1078 LSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALD-DQNVSRVANLLKELSKNAqFIVISLREEMLEKAD 1147
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 721-808 3.78e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.85  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLAS-GRTAIVIAHRLSTITN-ADLILCISNGRIVE 798
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsGITLVLVLNRFDEIPDfVQFAGVLADCTLAE 215

                         90
                 ....*....|
gi 162312131 799 TGTHEELIKR 808
Cdd:PRK10938 216 TGEREEILQQ 225
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 721-800 4.24e-04

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: 42.63  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAILKDPSIIL--LDEATSALDTNTERQIQAALNRL-ASGRTAIVIAHRLSTITNADLILCIS----- 792
Cdd:cd03270  138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIGpgagv 217


                 ....*....
gi 162312131 793 -NGRIVETG 800
Cdd:cd03270  218 hGGEIVAQG 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 721-807 1.42e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 42.31  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  721 LSGGEKQRVAVARAI----------LKDPSIILLDEatsaldtNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILC 790
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgvlyvLDEPSIGLHQR-------DNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVID 561

                          90       100
                  ....*....|....*....|...
gi 162312131  791 IS------NGRIVETGTHEELIK 807
Cdd:TIGR00630 562 IGpgagehGGEVVASGTPEEILA 584
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 405-552 1.66e-03

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


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 41.37  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 405 IYFTLIVLIMtlcycYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKV 484
Cdd:cd18572  141 LAFITVPVIA-----LITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312131 485 LFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDfviLLTYMI---QLQQPLNFFGTLYRSLQNSI 552
Cdd:cd18572  216 ALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ---LVTFMLyqqQLGEAFQSLGDVFSSLMQAV 283
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 457-534 1.67e-03

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


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 41.23  E-value: 1.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312131 457 VKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQL 534
Cdd:cd18548  191 IRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQI 268
PLN03140 PLN03140
ABC transporter G family member; Provisional
 714-806 3.66e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 40.98  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131  714 VGERGLK-LSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLS----TITNADLI 788
Cdd:PLN03140  329 VGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDI 408

                          90
                  ....*....|....*...
gi 162312131  789 LCISNGRIVETGTHEELI 806
Cdd:PLN03140  409 ILLSEGQIVYQGPRDHIL 426
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 346-552 4.14e-03

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


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 40.13  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 346 RHVLNLSYDFHLNKRAGEVLTALTkgSSLNTFAEqvVFQIGP-----VLLDLGVAMVYFFIkFDIYFTLIVLIMTLCYCY 420
Cdd:cd18549   83 EHLQKLSFSFFDNNKTGQLMSRIT--NDLFDISE--LAHHGPedlfiSIITIIGSFIILLT-INVPLTLIVFALLPLMII 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 421 VTVKItswrteaRRKMVNSWRESY---AVQNDAIMN----FETVKNFDADDFENERYGHAVDIYLKQERKVLF------- 486
Cdd:cd18549  158 FTIYF-------NKKMKKAFRRVRekiGEINAQLEDslsgIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKamayffs 230

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312131 487 SLNFLN-------IVQGGIFTFSLAIacllsayrvtfgfnTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSI 552
Cdd:cd18549  231 GMNFFTnllnlvvLVAGGYFIIKGEI--------------TLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGM 289
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
721-813 8.59e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 39.62  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312131 721 LSGGEKQRVAVARAI----------LKDPSIIL--LDeatsaldtnTERQIqAALNRLAS-GRTAIVIAHRLSTITNADL 787
Cdd:COG0178  486 LSGGEAQRIRLATQIgsglvgvlyvLDEPSIGLhqRD---------NDRLI-ETLKRLRDlGNTVIVVEHDEDTIRAADY 555

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 162312131 788 ILCI------SNGRIVETGTHEELIKRDG---GAY 813
Cdd:COG0178  556 IIDIgpgageHGGEVVAQGTPEEILKNPDsltGQY 590
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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