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Conserved domains on  [gi|738468658|ref|WP_036419172|]
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MULTISPECIES: ABC transporter ATP-binding protein [Morganella]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467437)

ABC transporter ATP-binding protein is the ATPase catalytic subunit 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 including Fe(3+) ions and polyamines such as spermidine and putrescine

CATH:  3.40.50.300
EC:  7.-.-.-
Gene Ontology:  GO:0042626|GO:0140359|GO:0005524|GO:0016887
PubMed:  25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-338 9.86e-170

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 476.13  E-value: 9.86e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG3842   83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLV 240
Cdd:COG3842  163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 241 SAHNANS------LLGLNLS------------GIVAIRPESIYVREAGRQygehisHPVSGTIRDSQLLGNIIRYQVDTG 302
Cdd:COG3842  243 PGTVLGDegggvrTGGRTLEvpadaglaaggpVTVAIRPEDIRLSPEGPE------NGLPGTVEDVVFLGSHVRYRVRLG 316

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 738468658 303 LGA-LTVDLLNRSSeRLFEQGTQLELMFNKNEIRALA 338
Cdd:COG3842  317 DGQeLVVRVPNRAA-LPLEPGDRVGLSWDPEDVVVLP 352
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-338 9.86e-170

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 476.13  E-value: 9.86e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG3842   83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLV 240
Cdd:COG3842  163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 241 SAHNANS------LLGLNLS------------GIVAIRPESIYVREAGRQygehisHPVSGTIRDSQLLGNIIRYQVDTG 302
Cdd:COG3842  243 PGTVLGDegggvrTGGRTLEvpadaglaaggpVTVAIRPEDIRLSPEGPE------NGLPGTVEDVVFLGSHVRYRVRLG 316

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 738468658 303 LGA-LTVDLLNRSSeRLFEQGTQLELMFNKNEIRALA 338
Cdd:COG3842  317 DGQeLVVRVPNRAA-LPLEPGDRVGLSWDPEDVVVLP 352
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-338 4.55e-125

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 362.82  E-value: 4.55e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNL- 239
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWl 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  240 ---VSAHNANSLLGLNL-----------SGIVAIRPESIYVREAGRQYGEhishpVSGTIRDSQLLGNI--IRYQVDtGL 303
Cdd:TIGR03265 242 pgtRGGGSRARVGGLTLacapglaqpgaSVRLAVRPEDIRVSPAGNAANL-----LLARVEDMEFLGAFyrLRLRLE-GL 315

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 738468658  304 G--ALTVDLLNRSSERL-FEQGTQLELMFNKNEIRALA 338
Cdd:TIGR03265 316 PgqALVADVSASEVERLgIRAGQPIWIELPAERLRAFA 353
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 7-235 1.47e-119

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: 344.22  E-value: 1.47e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYAL 86
Cdd:cd03300    4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDA 166
Cdd:cd03300   84 FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 167 QIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMG 235
Cdd:cd03300  164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
8-242 2.84e-114

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 336.15  E-value: 2.84e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALF 87
Cdd:PRK09452  19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  88 PNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:PRK09452  99 PHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 168 IRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVSA 242
Cdd:PRK09452 179 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDA 253
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
22-315 7.24e-90

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 272.72  E-value: 7.24e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLK 101
Cdd:NF040840  19 ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGLK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 102 MQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQR 181
Cdd:NF040840  99 LRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHR 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 182 ELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVS--AHNANSLLGLNLSGI--- 256
Cdd:NF040840 179 EFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgvAEKGGEGTILDTGNIkie 258

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 257 ----------VAIRPESIY-----VREAGRQYGEhishpvsGTIRDSQLLGNIIRYQVDTGLgALTVdLLNRSS 315
Cdd:NF040840 259 lpeekkgkvrIGIRPEDITistekVKTSARNEFK-------GKVEEIEDLGPLVKLTLDVGI-ILVA-FITRSS 323
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 1.21e-46

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: 155.11  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   19 FSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNMTTERNI 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   97 AFGLKMQKVPENEQRKSVAEVIELVGLKGKE----QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-206 5.22e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 113.10  E-value: 5.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  12 SFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGmvfqsyALFPnMT 91
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGL----KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:NF040873  74 VRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 738468658 168 IRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFL 206
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-221 3.15e-26

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 109.83  E-value: 3.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAA-TPVfSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIY-----VNKQDITSsppqQREIGM 79
Cdd:NF033858 269 ARGLTMRFGDfTAV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT----RRRVGY 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLtTIFV-THDQEEAMLmSDRIFLMNKGEIVQSDTAENL 221
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGV-TIFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
GguA NF040905
sugar ABC transporter ATP-binding protein;
8-204 2.11e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 76.75  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN--DGRIYVNKQ-----DITSSppQQREIGMV 80
Cdd:NF040905   6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEvcrfkDIRDS--EALGIVII 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGlkmqkvpeNEQRKS-----------VAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV 149
Cdd:NF040905  84 HQELALIPYLSIAENIFLG--------NERAKRgvidwnetnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRI 204
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSI 209
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 28-211 6.96e-14

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: 68.17  E-value: 6.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    28 KGEFITLLGPSGCGKSTLLRCLAG-LEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYalfpnmtterniafglkmqkvp 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   107 eneqrksvaevielvglkgkeqhlpHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIR-----QIQR 181
Cdd:smart00382  59 -------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKS 113

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 738468658   182 ELNLTTIFVTHDQE-----EAMLMSDRIFLMNKGE 211
Cdd:smart00382 114 EKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
9-224 9.48e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.06  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   9 LTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGK------STLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIgmvfq 82
Cdd:NF000106  19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**rgalpAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPV----- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:NF000106  94 R*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 163 ALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-224 3.00e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 55.13  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSppQQREigMVFQSYA- 85
Cdd:NF033858   5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRR--AVCPRIAy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 --------LFPNMTTERNIAF-----GlkmQKVPENEQRksVAEVIELVGLK-------GKeqhlphqLSGGQRQRVALA 145
Cdd:NF033858  81 mpqglgknLYPTLSVFENLDFfgrlfG---QDAAERRRR--IDELLRATGLApfadrpaGK-------LSGGMKQKLGLC 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 146 RALVMKPRILLLDE------PLSaldaqirkhlRQQ----IRQIQREL-NLTTIFVTHDQEEAMLMsDRIFLMNKGEIVQ 214
Cdd:NF033858 149 CALIHDPDLLILDEpttgvdPLS----------RRQfwelIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217

                        250
                 ....*....|
gi 738468658 215 SDTAENLYTQ 224
Cdd:NF033858 218 TGTPAELLAR 227
GguA NF040905
sugar ABC transporter ATP-binding protein;
134-213 9.81e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.01  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 134 LSGGQRQRVALARALVMKPRILLLDEPLSALD--AqirkhlRQQIRQIQRELNLT---TIFVTHDQEEAMLMSDRIFLMN 208
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgA------KYEIYTIINELAAEgkgVIVISSELPELLGMCDRIYVMN 478


                 ....*
gi 738468658 209 KGEIV 213
Cdd:NF040905 479 EGRIT 483
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-338 9.86e-170

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 476.13  E-value: 9.86e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG3842   83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLV 240
Cdd:COG3842  163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 241 SAHNANS------LLGLNLS------------GIVAIRPESIYVREAGRQygehisHPVSGTIRDSQLLGNIIRYQVDTG 302
Cdd:COG3842  243 PGTVLGDegggvrTGGRTLEvpadaglaaggpVTVAIRPEDIRLSPEGPE------NGLPGTVEDVVFLGSHVRYRVRLG 316

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 738468658 303 LGA-LTVDLLNRSSeRLFEQGTQLELMFNKNEIRALA 338
Cdd:COG3842  317 DGQeLVVRVPNRAA-LPLEPGDRVGLSWDPEDVVVLP 352
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-334 5.60e-140

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 400.60  E-value: 5.60e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:COG3839    1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG3839   81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHY--N 238
Cdd:COG3839  161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 239 LVSAHNANSllGLNLSG-----------------IVAIRPESIYVREAGrqygehiSHPVSGTIRDSQLLGNIIRYQVDT 301
Cdd:COG3839  241 LLPGTVEGG--GVRLGGvrlplpaalaaaaggevTLGIRPEHLRLADEG-------DGGLEATVEVVEPLGSETLVHVRL 311

                        330       340       350
                 ....*....|....*....|....*....|...
gi 738468658 302 GLGALTVDLlnrSSERLFEQGTQLELMFNKNEI 334
Cdd:COG3839  312 GGQELVARV---PGDTRLRPGDTVRLAFDPERL 341
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-338 4.55e-125

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 362.82  E-value: 4.55e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNL- 239
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWl 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  240 ---VSAHNANSLLGLNL-----------SGIVAIRPESIYVREAGRQYGEhishpVSGTIRDSQLLGNI--IRYQVDtGL 303
Cdd:TIGR03265 242 pgtRGGGSRARVGGLTLacapglaqpgaSVRLAVRPEDIRVSPAGNAANL-----LLARVEDMEFLGAFyrLRLRLE-GL 315

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 738468658  304 G--ALTVDLLNRSSERL-FEQGTQLELMFNKNEIRALA 338
Cdd:TIGR03265 316 PgqALVADVSASEVERLgIRAGQPIWIELPAERLRAFA 353
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 1-319 5.59e-123

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 357.15  E-value: 5.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIaENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS-PPQQREIGM 79
Cdd:COG1118    1 MSIEV-RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRERRVGF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:COG1118   80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNL 239
Cdd:COG1118  160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 240 VSAHNANSLL---GLNL---------SGIVAIRPESIYVREagrqyGEHISHPVSGTIRDSQLLGNIIRYQV---DTGLG 304
Cdd:COG1118  240 LRGRVIGGQLeadGLTLpvaeplpdgPAVAGVRPHDIEVSR-----EPEGENTFPATVARVSELGPEVRVELkleDGEGQ 314

                        330
                 ....*....|....*
gi 738468658 305 ALTVDLLNRSSERLF 319
Cdd:COG1118  315 PLEAEVTKEAWAELG 329
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 7-235 1.47e-119

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: 344.22  E-value: 1.47e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYAL 86
Cdd:cd03300    4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDA 166
Cdd:cd03300   84 FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 167 QIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMG 235
Cdd:cd03300  164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 4-214 1.70e-114

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: 330.64  E-value: 1.70e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQS 83
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQ 214
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
8-242 2.84e-114

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 336.15  E-value: 2.84e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALF 87
Cdd:PRK09452  19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  88 PNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:PRK09452  99 PHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 168 IRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVSA 242
Cdd:PRK09452 179 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDA 253
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
2-270 2.40e-109

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 322.82  E-value: 2.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   2 SYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVF 81
Cdd:PRK11432   5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:PRK11432  85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 162 SALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVS 241
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFP 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 738468658 242 AHNANSLLGLN----------------LSGIVAIRPESIYVREAG 270
Cdd:PRK11432 245 ATLSGDYVDIYgyrlprpaafafnlpdGECTVGVRPEAITLSEQG 289
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-213 9.58e-105

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 307.40  E-value: 9.58e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFA----ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPqqrE 76
Cdd:COG1116    5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:COG1116   82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNK--GEIV 213
Cdd:COG1116  162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 1-235 1.41e-102

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: 301.18  E-value: 1.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIaENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:cd03296    1 MSIEV-RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKV----PENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:cd03296   80 FQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMG 235
Cdd:cd03296  160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 34-337 1.39e-101

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 302.11  E-value: 1.39e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   34 LLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKS 113
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  114 VAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHD 193
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  194 QEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVSA----HNANSLLGLNLSGI------------- 256
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAtvieRKSEQVVLAGVEGRrcdiytdvpvekd 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  257 ----VAIRPESIYVREAGRQYGehiSHPVSGTIRDSQLLGNIIRYQV---DTGLGALTVDLLNRSSERLFEQGTQLELMF 329
Cdd:TIGR01187 241 qplhVVLRPEKIVIEEEDEANS---SNAIIGHVIDITYLGMTLEVHVrleTGQKVLVSEFFNEDDPHMSPSIGDRVGLTW 317


                  ....*...
gi 738468658  330 NKNEIRAL 337
Cdd:TIGR01187 318 HPGSEVVL 325
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 4-214 1.78e-99

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: 292.62  E-value: 1.78e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQS 83
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd03301   81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQ 214
Cdd:cd03301  161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 4-214 1.30e-98

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: 290.53  E-value: 1.30e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSF----AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQqreIGM 79
Cdd:cd03293    1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNK--GEIVQ 214
Cdd:cd03293  158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 4-238 5.34e-98

sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 289.78  E-value: 5.34e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQS 83
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   84 YALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658  164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYN 238
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 7-236 7.52e-94

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 281.59  E-value: 7.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFA-ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQS 83
Cdd:COG1125    5 ENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKE--QHLPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:COG1125   85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 162 SALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGH 236
Cdd:COG1125  165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
8-271 1.20e-92

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 280.19  E-value: 1.20e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAA-TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYAL 86
Cdd:PRK11650   8 AVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLkgkEQHL---PHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:PRK11650  88 YPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILEL---EPLLdrkPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGH--YNLVS 241
Cdd:PRK11650 165 LDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLLD 244

                        250       260       270
                 ....*....|....*....|....*....|
gi 738468658 242 AHNANSLLGLNLSGIVAIRPESIYVREAGR 271
Cdd:PRK11650 245 GRVSADGAAFELAGGIALPLGGGYRQYAGR 274
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
22-315 7.24e-90

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 272.72  E-value: 7.24e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLK 101
Cdd:NF040840  19 ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGLK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 102 MQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQR 181
Cdd:NF040840  99 LRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHR 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 182 ELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVS--AHNANSLLGLNLSGI--- 256
Cdd:NF040840 179 EFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgvAEKGGEGTILDTGNIkie 258

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 257 ----------VAIRPESIY-----VREAGRQYGEhishpvsGTIRDSQLLGNIIRYQVDTGLgALTVdLLNRSS 315
Cdd:NF040840 259 lpeekkgkvrIGIRPEDITistekVKTSARNEFK-------GKVEEIEDLGPLVKLTLDVGI-ILVA-FITRSS 323
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
8-268 4.37e-89

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 272.09  E-value: 4.37e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALF 87
Cdd:PRK11607  24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  88 PNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 168 IRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYN----LVSAH 243
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNvfegVLKER 263

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 738468658 244 NANSLL----GL--------------NLSGIVAIRPESIYVRE 268
Cdd:PRK11607 264 QEDGLVidspGLvhplkvdadasvvdNVPVHVALRPEKIMLCE 306
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1-238 8.51e-88

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 267.72  E-value: 8.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAeNLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:PRK10851   1 MSIEIA-NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMqkVPENEQ------RKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRI 154
Cdd:PRK10851  80 FQHYALFRHMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 155 LLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFM 234
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237


                 ....
gi 738468658 235 GHYN 238
Cdd:PRK10851 238 GEVN 241
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 7-239 8.77e-86

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: 258.42  E-value: 8.77e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATpVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYAL 86
Cdd:cd03299    4 ENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLkgkeQHL----PHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03299   83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI----DHLlnrkPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 163 ALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNL 239
Cdd:cd03299  159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 7-235 9.12e-86

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: 258.77  E-value: 9.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA-TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGL-EPvNDGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:cd03295    4 ENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEP-TSGEIFIDGEDIREQDPVElrRKIGYVIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKE--QHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03295   83 QIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMG 235
Cdd:cd03295  163 FGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 6-233 1.40e-85

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: 259.11  E-value: 1.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ------REIGM 79
Cdd:cd03294   27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:cd03294  107 VFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARF 233
Cdd:cd03294  187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 7-234 1.02e-84

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: 256.06  E-value: 1.02e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMVF 81
Cdd:COG1127    9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGMLF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTERNIAFGLKMQ-KVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG1127   89 QGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEP 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPaNEFVARFM 234
Cdd:COG1127  169 TAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-284 1.91e-84

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 259.96  E-value: 1.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMV 80
Cdd:PRK11000   1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:PRK11000  81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMG--HYN 238
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMN 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 738468658 239 LVSAHnansllglnlsgIVAIRPESIYVREAGRQygeHISHPVSGT 284
Cdd:PRK11000 241 FLPVK------------VTATAIEQVQVELPNRQ---QVWLPVEGR 271
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 4-271 2.29e-84

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.


Pssm-ID: 132302 [Multi-domain]  Cd Length: 362  Bit Score: 259.54  E-value: 2.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPVN-DGRIYVNKQDITSSPPQQREIGMVF 81
Cdd:TIGR03258   6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGfVKAAGlTGRIAIADRDLTHAPPHKRGLALLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   82 QSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:TIGR03258  86 QNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  162 SALDAQIRKHLRQQIRQIQREL-NLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLV 240
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245

                         250       260       270
                  ....*....|....*....|....*....|.
gi 738468658  241 SahnANSLLGLNLSGIVAIRPESIYVREAGR 271
Cdd:TIGR03258 246 P---AIALGITEAPGLVDVSCGGAVIFAFGD 273
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 4-236 3.67e-82

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 249.14  E-value: 3.67e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ----QREIGM 79
Cdd:COG1126    2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGL-KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:COG1126   82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGH 236
Cdd:COG1126  162 EPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSK 238
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-213 3.46e-81

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 246.49  E-value: 3.46e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSF----AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR 75
Cdd:COG1136    1 MSPLLeLRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 ------EIGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV 149
Cdd:COG1136   81 arlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDqEEAMLMSDRIFLMNKGEIV 213
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 6-228 1.65e-76

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: 243.66  E-value: 1.65e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFA-----ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----R 75
Cdd:COG1123  263 VRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrR 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 EIGMVFQ--SYALFPNMTTERNIAFGLKMQKV-PENEQRKSVAEVIELVGLKgkEQHL---PHQLSGGQRQRVALARALV 149
Cdd:COG1123  343 RVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLP--PDLAdryPHELSGGQRQRVAIARALA 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANE 228
Cdd:COG1123  421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 7-233 8.18e-75

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: 230.47  E-value: 8.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS-SPPQQ----REIGMVF 81
Cdd:cd03261    4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELyrlrRRMGMLF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTERNIAFGLKMQ-KVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03261   84 QSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 161 LSALDAqIRKHLRQQ-IRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLyTQPANEFVARF 233
Cdd:cd03261  164 TAGLDP-IASGVIDDlIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 6-225 1.03e-74

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: 229.91  E-value: 1.03e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFA-ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:COG1122    3 LENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 S--YALFpNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG1122   83 NpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:COG1122  162 TAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
7-328 2.43e-74

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 232.66  E-value: 2.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF----AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REI 77
Cdd:COG1135    5 ENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRKI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLL 157
Cdd:COG1135   85 GMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLC 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 158 DEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDqeeamlMS------DRIFLMNKGEIVQSDTAENLYTQPANEFVA 231
Cdd:COG1135  165 DEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQSELTR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 232 RFMGH-----------YNLVSAHNANSLLGLNLSGIVAIRPesiYVREAGRQYGehishpVSGTIrdsqLLGNIIRYQvD 300
Cdd:COG1135  239 RFLPTvlndelpeellARLREAAGGGRLVRLTFVGESADEP---LLSELARRFG------VDVNI----LSGGIEEIQ-G 304

                        330       340       350
                 ....*....|....*....|....*....|....
gi 738468658 301 TGLGALTVDL------LNRSSERLFEQGTQLELM 328
Cdd:COG1135  305 TPVGRLIVELegddaaIDAALAYLREQGVVVEVL 338
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 6-212 1.30e-73

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: 226.60  E-value: 1.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAA----TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR------ 75
Cdd:cd03255    3 LKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrrr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 EIGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRIL 155
Cdd:cd03255   83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 156 LLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMlMSDRIFLMNKGEI 212
Cdd:cd03255  163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-235 1.58e-73

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: 227.76  E-value: 1.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAA----TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REI 77
Cdd:COG1124    2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSY--ALFPNMTTERNIAFGLKMQKVPENEQRksVAEVIELVGLKgkEQHL---PHQLSGGQRQRVALARALVMKP 152
Cdd:COG1124   82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLP--PSFLdryPHQLSGGQRQRVAIARALILEP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVAR 232
Cdd:COG1124  158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRE 237


                 ...
gi 738468658 233 FMG 235
Cdd:COG1124  238 LLA 240
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 28-216 1.66e-73

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: 226.41  E-value: 1.66e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  28 KGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS------PPQQREIGMVFQSYALFPNMTTERNIAFGLK 101
Cdd:cd03297   22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 102 mqKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQR 181
Cdd:cd03297  102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 738468658 182 ELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSD 216
Cdd:cd03297  180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 23-317 2.26e-73

glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 231.28  E-value: 2.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ------REIGMVFQSYALFPNMTTERNI 96
Cdd:TIGR01186  13 DLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQFALFPHMTILQNT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   97 AFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQI 176
Cdd:TIGR01186  93 SLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQDEL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  177 RQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVSAHNANSLLGLNLSGI 256
Cdd:TIGR01186 173 KKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFDAERIAQRMNTGP 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  257 VAIRP----------------ESIYVREAGRQYGEHISHPVSGTIRDSQL-LGNIIR---YQVDTglGALTVDLLNRSSE 316
Cdd:TIGR01186 253 ITKTAdkgprsalqlmrdervDSLYVVDRQNKLVGVVDVESIKQARKKAQgLQDVLIddiYTVDA--GTLLRETVRKVLK 330


                  .
gi 738468658  317 R 317
Cdd:TIGR01186 331 A 331
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 4-212 2.74e-71

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: 220.48  E-value: 2.74e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ----QREIGM 79
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGL-KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:cd03262  161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 7-211 2.81e-71

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: 220.42  E-value: 2.81e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:cd03225    3 KNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 syalFP-----NMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLL 157
Cdd:cd03225   83 ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 158 DEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGE 211
Cdd:cd03225  159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 7-211 3.59e-71

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: 218.98  E-value: 3.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS----SPPQQREIGMVFQ 82
Cdd:cd03229    4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGMVFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLkmqkvpeneqrksvaevielvglkgkeqhlphqlSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03229   84 DFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738468658 163 ALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGE 211
Cdd:cd03229  130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
23-235 6.45e-71

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 220.40  E-value: 6.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLKM 102
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLRP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 103 QKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRE 182
Cdd:COG3840   99 GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRE 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 183 LNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMG 235
Cdd:COG3840  179 RGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
6-221 3.88e-70

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 218.39  E-value: 3.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMVFQSY 84
Cdd:COG1131    3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQEP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:COG1131   83 ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 165 DAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:COG1131  163 DPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-216 5.10e-68

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 212.61  E-value: 5.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA-TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMV 80
Cdd:COG2884    5 ENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG2884   85 FQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 161 LSALDAQirkhLRQQIRQIQRELNL--TTIFV-THDQEEAMLMSDRIFLMNKGEIVQSD 216
Cdd:COG2884  165 TGNLDPE----TSWEIMELLEEINRrgTTVLIaTHDLELVDRMPKRVLELEDGRLVRDE 219
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 6-213 7.64e-68

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: 212.37  E-value: 7.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSF----AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR-----E 76
Cdd:cd03257    4 VKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSY--ALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMK 151
Cdd:cd03257   84 IQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIARALALN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03257  164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 23-226 3.75e-67

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: 214.96  E-value: 3.75e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNK---QDITSS---PPQQREIGMVFQSYALFPNMTTERNI 96
Cdd:COG4148   19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGiflPPHRRRIGYVFQEARLFPHLSVRGNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  97 AFGLKmqKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQirkhLRQQI 176
Cdd:COG4148   99 LYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA----RKAEI 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 177 ----RQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:COG4148  173 lpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 7-225 4.41e-66

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: 208.20  E-value: 4.41e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAAT----PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP-----QQREI 77
Cdd:cd03258    5 KNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkARRRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLL 157
Cdd:cd03258   85 GMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 158 DEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:cd03258  165 DEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 7-211 2.83e-65

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 205.02  E-value: 2.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPV--NDGRIYVNKQDITSSPPQQREIGMVFQS 83
Cdd:COG4136    5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKmQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:COG4136   85 DLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGE 211
Cdd:COG4136  164 LDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-214 3.02e-65

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 207.02  E-value: 3.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSF----AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSsPPQQRe 76
Cdd:COG4525    1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 iGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:COG4525   79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLM--NKGEIVQ 214
Cdd:COG4525  158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-226 3.43e-65

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: 214.38  E-value: 3.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIA-ENLTKSFA--ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN---DGRIYVNKQDITSSPPQQ 74
Cdd:COG1123    1 MTPLLEvRDLSVRYPggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  75 R--EIGMVFQS--YALFPnMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVM 150
Cdd:COG1123   81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 151 KPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:COG1123  160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
8-236 4.31e-63

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 200.70  E-value: 4.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREI----GMVFQS 83
Cdd:PRK09493   6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFG-LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PRK09493  86 FYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 163 ALDAQirkhLRQQIRQIQREL---NLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGH 236
Cdd:PRK09493 166 ALDPE----LRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQH 238
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 6-219 3.00e-62

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: 198.73  E-value: 3.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQS 83
Cdd:COG1120    4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFG----LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:COG1120   84 PPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 160 PLSALD--AQIRkhLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAE 219
Cdd:COG1120  164 PTSHLDlaHQLE--VLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 7-226 3.30e-62

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: 201.05  E-value: 3.30e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFA----ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN---DGRIYVNKQDITSSPPQQ----- 74
Cdd:COG0444    5 RNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKElrkir 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  75 -REIGMVFQ-SY-ALFPNMTTERNIAFGLKM-QKVPENEQRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARA 147
Cdd:COG0444   85 gREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:COG0444  165 LALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 7-221 5.86e-62

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 197.97  E-value: 5.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA-TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMV 80
Cdd:COG3638    6 RNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGMI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFG-------LK--MQKVPENEQRKsVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMK 151
Cdd:COG3638   86 FQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQE 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:COG3638  165 PKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 7-224 1.26e-61

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: 197.65  E-value: 1.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDiTSSPPQQREI----GMV 80
Cdd:TIGR04520   4 ENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLWEIrkkvGMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSyalfP-----NMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRIL 155
Cdd:TIGR04520  83 FQN----PdnqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658  156 LLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAmLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 4-225 1.93e-61

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


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 197.67  E-value: 1.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    4 VIAENLTKSFAA-TP----VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ---- 74
Cdd:TIGR04521   1 IKLKNVSYIYQPgTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   75 -REIGMVFQ--SYALFPNmTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKG--KEQHlPHQLSGGQRQRVALARALV 149
Cdd:TIGR04521  81 rKKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIAGVLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658  150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
6-212 1.31e-60

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 193.11  E-value: 1.31e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQS 83
Cdd:COG4619    3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNmTTERNIAFGLKMQKVPENEQRksVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:COG4619   83 PALWGG-TVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTS 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 163 ALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:COG4619  160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 4-226 1.92e-60

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 196.88  E-value: 1.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFaatPVFSGL--------------NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS 69
Cdd:COG4608    8 LEVRDLKKHF---PVRGGLfgrtvgvvkavdgvSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  70 SPPQQ-----REIGMVFQ-SYA-LFPNMTTERNIAFGLKMQKV-PENEQRKSVAEVIELVGLKgkEQHL---PHQLSGGQ 138
Cdd:COG4608   85 LSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLR--PEHAdryPHEFSGGQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 139 RQRVALARALVMKPRILLLDEPLSALDAQIRKhlrqQI----RQIQRELNLTTIFVTHDqeeamL-----MSDRIFLMNK 209
Cdd:COG4608  163 RQRIGIARALALNPKLIVCDEPVSALDVSIQA----QVlnllEDLQDELGLTYLFISHD-----LsvvrhISDRVAVMYL 233

                        250
                 ....*....|....*..
gi 738468658 210 GEIVQSDTAENLYTQPA 226
Cdd:COG4608  234 GKIVEIAPRDELYARPL 250
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 21-210 2.98e-59

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: 190.37  E-value: 2.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   21 GLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQReigMVFQSYALFPNMTTERNIAFGL 100
Cdd:TIGR01184   3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIALAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  101 K--MQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQ 178
Cdd:TIGR01184  80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 738468658  179 IQRELNLTTIFVTHDQEEAMLMSDRIFLMNKG 210
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 7-326 1.10e-57

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 190.01  E-value: 1.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA----TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REI 77
Cdd:PRK11153   5 KNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLL 157
Cdd:PRK11153  85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 158 DEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGhy 237
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ-- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 238 nlvsahnanSLLGLNLSGIVAIRPESIYVREAGRQY-----GEHISHPV-SGTIRDSQLLGNIIRYQVD----TGLGALT 307
Cdd:PRK11153 243 ---------STLHLDLPEDYLARLQAEPTTGSGPLLrleftGESVDAPLlSETARRFGVDFNILSGQIDyiggVKFGSLL 313

                        330       340
                 ....*....|....*....|....*
gi 738468658 308 VDL------LNRSSERLFEQGTQLE 326
Cdd:PRK11153 314 VELtgdpgdIQAAIAYLQEHGVKVE 338
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
 8-234 6.63e-56

ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.


Pssm-ID: 132050 [Multi-domain]  Cd Length: 252  Bit Score: 182.72  E-value: 6.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-------------- 73
Cdd:TIGR03005   5 DVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRngplvpadekhlrq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   74 -QREIGMVFQSYALFPNMTTERNIAFG-LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMK 151
Cdd:TIGR03005  85 mRNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVA 231
Cdd:TIGR03005 165 PKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTR 244


                  ...
gi 738468658  232 RFM 234
Cdd:TIGR03005 245 EFL 247
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
23-235 8.43e-56

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 181.70  E-value: 8.43e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLKM 102
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 103 QKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRE 182
Cdd:PRK10771  99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 183 LNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV-QSDTAEnLYTQPANEfvARFMG 235
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAwDGPTDE-LLSGKASA--SALLG 229
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 4-221 2.70e-55

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: 179.87  E-value: 2.70e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMVFQ 82
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRrIGIVFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03265   81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 163 ALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:cd03265  161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-236 3.53e-55

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 180.72  E-value: 3.53e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP---QQREI 77
Cdd:PRK11264   1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqQKGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 -------GMVFQSYALFPNMTTERNIAFG-LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV 149
Cdd:PRK11264  81 rqlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANE- 228
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPr 239

                        250
                 ....*....|.
gi 738468658 229 ---FVARFMGH 236
Cdd:PRK11264 240 trqFLEKFLLQ 250
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 4-212 4.49e-55

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: 177.59  E-value: 4.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMVFQ 82
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIafglkmqkvpeneqrksvaevielvglkgkeqhlphQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03230   81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 163 ALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:cd03230  125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 6-228 4.75e-55

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 180.05  E-value: 4.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-QREIGMVFQSY 84
Cdd:COG4555    4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:COG4555   84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 165 DAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANE 228
Cdd:COG4555  164 DVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 6-219 7.10e-55

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: 178.91  E-value: 7.10e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN-----DGRIYVNKQDITSSPPQ----QRE 76
Cdd:cd03260    3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlelRRR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSYALFPnMTTERNIAFGLKMQKVPENEQRKS-VAEVIELVGLKG--KEQHLPHQLSGGQRQRVALARALVMKPR 153
Cdd:cd03260   83 VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPE 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 154 ILLLDEPLSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAE 219
Cdd:cd03260  162 VLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 6-215 8.40e-55

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: 177.24  E-value: 8.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQReigmvfqsyA 85
Cdd:cd03214    2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---------A 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 lfpnmtteRNIAFglkmqkvpeneqrksVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:cd03214   73 --------RKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 166 AQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:cd03214  130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 6-197 1.48e-53

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: 174.97  E-value: 1.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-QREIGMVFQSY 84
Cdd:COG4133    5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGHAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ALFPNMTTERNIAFGLKMQKVPENEQRksVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:COG4133   85 GLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 738468658 165 DAQIRKHLRQQIRQiQRELNLTTIFVTHDQEEA 197
Cdd:COG4133  163 DAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-221 1.57e-53

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 176.05  E-value: 1.57e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP------PQQ 74
Cdd:COG1121    4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvPQR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  75 REIGmvfqsyALFPnMTTERNIAFGL----KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVM 150
Cdd:COG1121   84 AEVD------WDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 151 KPRILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:COG1121  157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVL 226
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 22-213 2.19e-53

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: 174.60  E-value: 2.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLK 101
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 102 MQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQR 181
Cdd:cd03298   97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176

                        170       180       190
                 ....*....|....*....|....*....|..
gi 738468658 182 ELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03298  177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 7-228 7.92e-53

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: 174.29  E-value: 7.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA-TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP-----QQREIGMV 80
Cdd:cd03256    4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIGMI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQK---------VPENEQRKSvAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMK 151
Cdd:cd03256   84 FQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEKQRA-LAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANE 228
Cdd:cd03256  163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 6-219 5.22e-52

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: 171.85  E-value: 5.22e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSF--AATPV--FSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR------ 75
Cdd:COG4181   11 LRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrar 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 EIGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRksVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRIL 155
Cdd:COG4181   91 HVGFVFQSFQLLPTLTALENVMLPLELAGRRDARAR--ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 156 LLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAmLMSDRIFLMNKGEIVQSDTAE 219
Cdd:COG4181  169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAAT 231
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 7-221 6.70e-52

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: 182.34  E-value: 6.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:COG2274  477 ENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQ 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFpNMTTERNIAFGlkMQKVPENEqrksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMK 151
Cdd:COG2274  557 DVFLF-SGTIRENITLG--DPDATDEE----IIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRN 629

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDqEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:COG2274  630 PRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 22-232 1.07e-51

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: 174.92  E-value: 1.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS------PPQQREIGMVFQSYALFPNMTTERN 95
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPEKRRIGYVFQEARLFPHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   96 IAFGLKMQKVPEneQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQ 175
Cdd:TIGR02142  96 LRYGMKRARPSE--RRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658  176 IRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVAR 232
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 4-217 3.62e-51

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: 169.22  E-value: 3.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFA--ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-QREIGMV 80
Cdd:cd03263    1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03263   81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDT 217
Cdd:cd03263  161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
6-214 4.34e-51

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 170.27  E-value: 4.34e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDItSSPPQQReiGMVFQSYA 85
Cdd:PRK11248   4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER--GVVFQNEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:PRK11248  81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738468658 166 AQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLM--NKGEIVQ 214
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 7-211 5.44e-51

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 168.58  E-value: 5.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSF-AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMV 80
Cdd:TIGR02673   5 HNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:TIGR02673  85 FQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 738468658  161 LSALDAqirkHLRQQIRQIQRELN---LTTIFVTHDQEEAMLMSDRIFLMNKGE 211
Cdd:TIGR02673 165 TGNLDP----DLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDGR 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 21-228 7.59e-51

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: 176.80  E-value: 7.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  21 GLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPvNDGRIYVNKQDITSSPPQQ-----REIGMVFQS-YA-LFPNMTTE 93
Cdd:COG4172  304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVG 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFGLKMQKVPEN--EQRKSVAEVIELVGLKGKEQH-LPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:COG4172  383 QIIAEGLRVHGPGLSaaERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQA 462

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 171 hlrqQI----RQIQRELNLTTIFVTHDqeeamL-----MSDRIFLMNKGEIVQSDTAENLYTQPANE 228
Cdd:COG4172  463 ----QIldllRDLQREHGLAYLFISHD-----LavvraLAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 7-204 7.98e-51

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 167.79  E-value: 7.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQD---ITSSPPQQ--RE-IGMV 80
Cdd:TIGR03608   2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKfrREkLGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:TIGR03608  82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 738468658  161 LSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMlMSDRI 204
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAK-QADRV 203
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 6-219 2.07e-50

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: 167.61  E-value: 2.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---IGMVFQ 82
Cdd:cd03219    3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQKVP----------ENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKP 152
Cdd:cd03219   83 IPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAE 219
Cdd:cd03219  163 KLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-212 2.73e-50

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 168.32  E-value: 2.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSppqQREIGMVFQS 83
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLMFQD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKmqkvpeNEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:PRK11247  90 ARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 7-221 3.34e-50

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: 166.84  E-value: 3.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---IGMVFQS 83
Cdd:cd03224    4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVPEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLkmQKVPENEQRKSVAEVIELV-GLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03224   84 RRIFPELTVEENLLLGA--YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 163 ALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:cd03224  162 GLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 6-219 3.70e-50

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: 167.91  E-value: 3.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR-EIGMV--FQ 82
Cdd:COG0411    7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIArtFQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIA---------------FGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARA 147
Cdd:COG0411   87 NPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAE 219
Cdd:COG0411  167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-211 4.20e-50

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: 164.34  E-value: 4.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQs 83
Cdd:cd00267    2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 yalfpnmtterniafglkmqkvpeneqrksvaevielvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd00267   81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738468658 164 LDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGE 211
Cdd:cd00267  111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 7-224 9.26e-50

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 166.32  E-value: 9.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSF-AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-----QREIGMV 80
Cdd:TIGR02315   5 ENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRRIGMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSYALFPNMTTERNI---AFGLK------MQKVPENEQRKSVaEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMK 151
Cdd:TIGR02315  85 FQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDKERAL-SALERVGLADKAYQRADQLSGGQQQRVAIARALAQQ 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658  152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 6-210 1.22e-49

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: 165.01  E-value: 1.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSppqQREIGMVFQSYA 85
Cdd:cd03235    2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---RKRIGYVPQRRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 L---FPnMTTERNIAFGL----KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:cd03235   79 IdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKG 210
Cdd:cd03235  158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
8-236 1.24e-49

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 165.96  E-value: 1.24e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDG--RIYVNKQDITSSPPQQ------REIGM 79
Cdd:COG4161    7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlNIAGHQFDFSQKPSEKairllrQKVGM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERN-IAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:COG4161   87 VFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 159 EPLSALDAQIRKhlrqQIRQIQRELN---LTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAeNLYTQPANEFVARFMG 235
Cdd:COG4161  167 EPTAALDPEITA----QVVEIIRELSqtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYLS 241


                 .
gi 738468658 236 H 236
Cdd:COG4161  242 H 242
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 7-236 1.25e-49

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 165.96  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYV--NKQDITSSP-PQQ-----REIG 78
Cdd:PRK11124   6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPsDKAirelrRNVG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  79 MVFQSYALFPNMTTERN-IAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLL 157
Cdd:PRK11124  86 MVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 158 DEPLSALDAQIrkhlRQQIRQIQREL---NLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENlYTQPANEFVARFM 234
Cdd:PRK11124 166 DEPTAALDPEI----TAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240


                 ..
gi 738468658 235 GH 236
Cdd:PRK11124 241 SH 242
cbiO PRK13637
energy-coupling factor transporter ATPase;
1-213 1.11e-48

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 164.84  E-value: 1.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIaENLT-----KSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR 75
Cdd:PRK13637   1 MSIKI-ENLThiymeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 EI----GMVFQ--SYALFPNmTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKE--QHLPHQLSGGQRQRVALARA 147
Cdd:PRK13637  80 DIrkkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 4-211 1.68e-48

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 160.63  E-value: 1.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGM 79
Cdd:cd03228    1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFpNMTTERNIafglkmqkvpeneqrksvaevielvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:cd03228   81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDqEEAMLMSDRIFLMNKGE 211
Cdd:cd03228  123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 23-217 3.41e-48

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 161.57  E-value: 3.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYALFPNMTTERNIAFGLKM 102
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  103 QKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRE 182
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 738468658  183 LNLTTIFVTHDQEEAMLMSDRIFLMNKGEI-VQSDT 217
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIkVVSDC 213
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 7-212 1.11e-47

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: 160.27  E-value: 1.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF-AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-----SSPPQQREIGMV 80
Cdd:cd03292    4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKIGVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03292   84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 161 LSALDAQIRKhlrqQIRQIQRELNL--TTIFV-THDQEEAMLMSDRIFLMNKGEI 212
Cdd:cd03292  164 TGNLDPDTTW----EIMNLLKKINKagTTVVVaTHAKELVDTTRHRVIALERGKL 214
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
23-261 1.93e-47

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 164.82  E-value: 1.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS-SPPQQRE-----IGMVFQSYALFPNMTTERNI 96
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREvrrkkIAMVFQSFALMPHMTVLDNT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  97 AFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQI 176
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 177 RQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGHYNLVSAHNANSLLGLNLSGI 256
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGL 287


                 ....*
gi 738468658 257 VAIRP 261
Cdd:PRK10070 288 IRKTP 292
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
4-236 3.26e-47

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 160.35  E-value: 3.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP----------PQ 73
Cdd:COG4598    9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpadRR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  74 Q-----REIGMVFQSYALFPNMTTERNIAFG-LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARA 147
Cdd:COG4598   89 QlqrirTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNlTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPAN 227
Cdd:COG4598  169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247


                 ....*....
gi 738468658 228 EFVARFMGH 236
Cdd:COG4598  248 ERLRQFLSS 256
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
14-222 4.14e-47

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 160.57  E-value: 4.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNkqDITSSPPQ----QREIGMVFQSY-ALFP 88
Cdd:PRK13635  18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG--GMVLSEETvwdvRRQVGMVFQNPdNQFV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  89 NMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQI 168
Cdd:PRK13635  96 GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 169 RKHLRQQIRQIQRELNLTTIFVTHDQEEAmLMSDRIFLMNKGEIVQSDTAENLY 222
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIF 228
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 1.21e-46

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: 155.11  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   19 FSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNMTTERNI 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   97 AFGLKMQKVPENEQRKSVAEVIELVGLKGKE----QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-213 1.92e-46

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 158.33  E-value: 1.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF-AATP----VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE--IGM 79
Cdd:COG1101    5 KNLSKTFnPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYAL--FPNMTTERNIA--------FGLKMQKvpENEQRKSVAEVIELVGLkGKEQHLPHQ---LSGGQRQRVALAR 146
Cdd:COG1101   85 VFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGL--TKKRRELFRELLATLGL-GLENRLDTKvglLSGGQRQALSLLM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 147 ALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:COG1101  162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 4-224 9.05e-46

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: 163.78  E-value: 9.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFA-ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMV 80
Cdd:COG4988  337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPnMTTERNIAFGlkMQKVPENEqrksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALV 149
Cdd:COG4988  417 PQNPYLFA-GTIRENLRLG--RPDASDEE----LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALL 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQEEAMLMsDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:COG4988  490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 18-213 1.53e-45

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 154.79  E-value: 1.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMVFQSYALFPNMTT 92
Cdd:TIGR02982  20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlrRRIGYIFQAHNLLGFLTA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   93 ERNIAFGLKMQKVPENEQRKSVA-EVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKH 171
Cdd:TIGR02982 100 RQNVQMALELQPNLSYQEARERArAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 738468658  172 LRQQIRQIQRELNLTTIFVTHDQeEAMLMSDRIFLMNKGEIV 213
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKLL 220
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 4-226 2.25e-45

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: 154.62  E-value: 2.25e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---IGMV 80
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03218   81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 161 LSALDAqIRKHLRQQIRQIQRELNLtTIFVT-HDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:cd03218  161 FAGVDP-IAVQDIQKIIKILKDRGI-GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
cbiO PRK13650
energy-coupling factor transporter ATPase;
17-222 5.31e-45

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 155.27  E-value: 5.31e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP--PQQREIGMVFQSY-ALFPNMTTE 93
Cdd:PRK13650  21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRHKIGMVFQNPdNQFVGATVE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLR 173
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738468658 174 QQIRQIQRELNLTTIFVTHDQEEAMLmSDRIFLMNKGEIVQSDTAENLY 222
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQVESTSTPRELF 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 7-226 5.57e-45

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: 161.01  E-value: 5.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA----TPVFSGLNFSVSKGEFITLLGPSGCGKS----TLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ---- 74
Cdd:COG4172   10 EDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrri 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  75 --REIGMVFQ--SYALFPNMTTERNIAFGLKM-QKVPENEQRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALAR 146
Cdd:COG4172   90 rgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 147 ALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDqeeamL-----MSDRIFLMNKGEIVQSDTAENL 221
Cdd:COG4172  170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD-----LgvvrrFADRVAVMRQGEIVEQGPTAEL 244


                 ....*
gi 738468658 222 YTQPA 226
Cdd:COG4172  245 FAAPQ 249
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 6-228 2.15e-44

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 152.88  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLepvND--------GRIYVNKQDITSS---PPQ- 73
Cdd:COG1117   14 VRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM---NDlipgarveGEILLDGEDIYDPdvdVVEl 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  74 QREIGMVFQSYALFPnMTTERNIAFGLKMQKVpeneqrKSVAEVIELV-------GL----KGKEQHLPHQLSGGQRQRV 142
Cdd:COG1117   91 RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGI------KSKSELDEIVeeslrkaALwdevKDRLKKSALGLSGGQQQRL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 143 ALARALVMKPRILLLDEPLSALD----AQIRKhLRQQIRQiqrelNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTA 218
Cdd:COG1117  164 CIARALAVEPEVLLMDEPTSALDpistAKIEE-LILELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPT 237

                        250
                 ....*....|
gi 738468658 219 ENLYTQPANE 228
Cdd:COG1117  238 EQIFTNPKDK 247
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 7-235 2.45e-44

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: 152.06  E-value: 2.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---IGMVFQS 83
Cdd:COG0410    7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVPEG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKMQKvPENEQRKSVAEVIEL--VgLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:COG0410   87 RRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 162 SALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPanEFVARFMG 235
Cdd:COG0410  165 LGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--EVREAYLG 235
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 22-222 3.82e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 152.60  E-value: 3.82e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQS-YALFPNMTTERNIAF 98
Cdd:PRK13648  28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklRKHIGIVFQNpDNQFVGSIVKYDVAF 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  99 GLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQ 178
Cdd:PRK13648 108 GLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738468658 179 IQRELNLTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAENLY 222
Cdd:PRK13648 188 VKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEIF 230
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
12-217 7.16e-44

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 158.79  E-value: 7.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  12 SFA---ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYAL 86
Cdd:COG1132  346 SFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFL 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FpNMTTERNIAFGLKmqKVPENEqrksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRIL 155
Cdd:COG1132  426 F-SGTIRENIRYGRP--DATDEE----VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPIL 498

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 156 LLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDqeeamL----MSDRIFLMNKGEIVQSDT 217
Cdd:COG1132  499 ILDEATSALDTETEALIQEALERLMK--GRTTIVIAHR-----LstirNADRILVLDDGRIVEQGT 557
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 6-213 7.53e-44

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 150.19  E-value: 7.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    6 AENLTKSFA----ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS------SPPQQR 75
Cdd:TIGR02211   4 CENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssnerAKLRNK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   76 EIGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRIL 155
Cdd:TIGR02211  84 KLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658  156 LLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMsDRIFLMNKGEIV 213
Cdd:TIGR02211 164 LADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-233 3.08e-43

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 149.41  E-value: 3.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---I 77
Cdd:COG1137    1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRArlgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLkgkeQHLPHQ----LSGGQRQRVALARALVMKPR 153
Cdd:COG1137   81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI----THLRKSkaysLSGGERRRVEIARALATNPK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 154 ILLLDEPLSALD----AQIRK---HLRQqiRQIqrelnltTIFVT-HDQEEAMLMSDRIFLMNKGEIVQSDTAENLYtqp 225
Cdd:COG1137  157 FILLDEPFAGVDpiavADIQKiirHLKE--RGI-------GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL--- 224


                 ....*...
gi 738468658 226 ANEFVARF 233
Cdd:COG1137  225 NNPLVRKV 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 7-221 1.53e-42

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 147.29  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---IGMVFQS 83
Cdd:TIGR03410   4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVPQG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   84 YALFPNMTTERNIAFGLKMQKVPEneqRKSVAEVIELVG-LKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:TIGR03410  84 REIFPRLTVEENLLTGLAALPRRS---RKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658  163 ALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 23-226 1.59e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 149.01  E-value: 1.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS------PPQQREIGMVFQsyalFPNM-----T 91
Cdd:PRK13634  27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkklKPLRKKVGIVFQ----FPEHqlfeeT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGK-EQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 171 HLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 14-226 3.21e-42

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: 154.15  E-value: 3.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFpNMT 91
Cdd:COG4987  346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTT 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLkmQKVPENEqrksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:COG4987  425 LRENLRLAR--PDATDEE----LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEP 498

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQEEAMLMsDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:COG4987  499 TEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNG 561
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 4-215 4.25e-42

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: 145.41  E-value: 4.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGeFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMVFQ 82
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03264   80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 163 ALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:cd03264  160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 6-220 4.27e-42

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 146.84  E-value: 4.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQS 83
Cdd:PRK13548   5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YAL-FPnMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV------MKPRILL 156
Cdd:PRK13548  85 SSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 157 LDEPLSALDaqirkhLRQQIR--QIQREL----NLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAEN 220
Cdd:PRK13548 164 LDEPTSALD------LAHQHHvlRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 17-221 2.16e-41

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: 145.33  E-value: 2.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMVFQ-SYALF-PN 89
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPSAVnPR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   90 MTTERNIAFGLK-MQKVPENEQRKSVAEVIELVGLKGKE-QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658  168 IRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV-QSDTAENL 221
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeECDVAQLL 239
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
7-245 4.22e-41

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 144.59  E-value: 4.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF-------------AATPVfsglNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ 73
Cdd:COG4167    8 RNLSKTFkyrtglfrrqqfeAVKPV----SFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  74 QR--EIGMVFQ--SYALFPNMTTERNIAFGLKMQ-KVPENEQRKSVAEVIELVGLKGKEQHL-PHQLSGGQRQRVALARA 147
Cdd:COG4167   84 YRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFyPHMLSSGQKQRVALARA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPAN 227
Cdd:COG4167  164 LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQH 243

                        250
                 ....*....|....*....
gi 738468658 228 EFVARF-MGHYNLVSAHNA 245
Cdd:COG4167  244 EVTKRLiESHFGEALTADA 262
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
3-224 4.59e-41

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 144.85  E-value: 4.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   3 YVIAENLTKSFAATPVfsglNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDiTSSPPQQREI----G 78
Cdd:PRK13633  14 YESNEESTEKLALDDV----NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDIrnkaG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  79 MVFQSyalfPN-----MTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPR 153
Cdd:PRK13633  89 MVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 154 ILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAmLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 21-225 5.55e-41

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 146.00  E-value: 5.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  21 GLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR-----EIGMVFQS--YALFPNMTTE 93
Cdd:PRK15079  39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIG 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFGLKM--QKVPENEQRKSVAEVIELVGLKGKE-QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 171 HLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 16-225 7.76e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 144.06  E-value: 7.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVN----KQDITSSPPQQREIGMVFQSY--ALFPN 89
Cdd:PRK13639  15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVGIVFQNPddQLFAP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 mTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQir 169
Cdd:PRK13639  95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM-- 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 170 khLRQQIRQIQRELN---LTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK13639 172 --GASQIMKLLYDLNkegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 7-215 1.07e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 143.59  E-value: 1.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA--TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS--PPQQREIGMVFQ 82
Cdd:PRK13632  11 ENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlKEIRKKIGIIFQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SY-ALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:PRK13632  91 NPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 162 SALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLmSDRIFLMNKGEIVQS 215
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQ 223
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
6-243 1.17e-40

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 142.95  E-value: 1.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:COG4559    4 AENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTP-SSGEVRLNGRPLAAWSPWElaRRRAVLPQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYAL-FPnMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV-------MKPRI 154
Cdd:COG4559   83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 155 LLLDEPLSALDaqirkhLRQQIR--QIQREL---NLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQpanEF 229
Cdd:COG4559  162 LFLDEPTSALD------LAHQHAvlRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTD---EL 232

                        250
                 ....*....|....
gi 738468658 230 VARFMGHYNLVSAH 243
Cdd:COG4559  233 LERVYGADLRVLAH 246
cbiO PRK13640
energy-coupling factor transporter ATPase;
17-225 1.43e-40

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 143.79  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGL---EPVNDGRIYVNKQDITSSPPQQ-RE-IGMVFQSY-ALFPNM 90
Cdd:PRK13640  21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiREkVGIVFQNPdNQFVGA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  91 TTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 171 HLRQQIRQIQRELNLTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK13640 181 QILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 7-213 1.70e-40

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: 141.20  E-value: 1.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYAL 86
Cdd:cd03268    4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKMQKVPENEqrksVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDA 166
Cdd:cd03268   84 YPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738468658 167 QIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03268  160 DGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 6-213 2.12e-40

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: 139.49  E-value: 2.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP---QQREIGMVfq 82
Cdd:cd03216    3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdaRRAGIAMV-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 syalfpnmtterniafglkmqkvpeneqrksvaevielvglkgkeqhlpHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03216   81 -------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTA 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738468658 163 ALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03216  112 ALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
6-221 2.72e-40

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 147.86  E-value: 2.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---IGMVFQ 82
Cdd:COG1129    7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQaagIAIIHQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQK---VPENEQRKSVAEVIELVGLkgkeqHL-PHQ----LSGGQRQRVALARALVMKPRI 154
Cdd:COG1129   87 ELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGL-----DIdPDTpvgdLSVAQQQLVEIARALSRDARV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 155 LLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:COG1129  162 LILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 6-213 1.99e-39

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: 138.65  E-value: 1.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATP----VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-QREIGMV 80
Cdd:cd03266    4 ADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLGFV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03266   84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 161 LSALDAQIRKHLRQQIRQiQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03266  164 TTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 4-207 6.41e-39

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: 144.35  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    4 VIAENLTKSFA-ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMV 80
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 FQSYALFPNMTTErNIAFGLKMQKVPEneqrksVAEVIELVGLKGKEQHLP-----------HQLSGGQRQRVALARALV 149
Cdd:TIGR02857 402 PQHPFLFAGTIAE-NIRLARPDASDAE------IREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFL 474

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658  150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQEEAMLMsDRIFLM 207
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 17-242 7.33e-39

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: 137.67  E-value: 7.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFpNMTTER 94
Cdd:cd03249   17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLF-DGTIAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NIAFGLKMQKVPENEQRKSVA---EVIE--------LVGLKGKeqhlphQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd03249   96 NIRYGKPDATDEEVEEAAKKAnihDFIMslpdgydtLVGERGS------QLSGGQKQRIAIARALLRNPKILLLDEATSA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 164 LDAQIRKhlrqqirQIQRELNL-----TTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPanefvarfmGHY- 237
Cdd:cd03249  170 LDAESEK-------LVQEALDRamkgrTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQK---------GVYa 232


                 ....*
gi 738468658 238 NLVSA 242
Cdd:cd03249  233 KLVKA 237
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
 16-197 1.18e-38

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 136.01  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP----QQREIGMVFQS--YALFpN 89
Cdd:TIGR01166   5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglleRRQRVGLVFQDpdDQLF-A 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   90 MTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:TIGR01166  84 ADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163

                         170       180
                  ....*....|....*....|....*...
gi 738468658  170 KHLRQQIRQIqRELNLTTIFVTHDQEEA 197
Cdd:TIGR01166 164 EQMLAILRRL-RAEGMTVVISTHDVDLA 190
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 6-213 1.25e-38

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: 136.23  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSF-AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDItSSPPQQREIGMVFQS- 83
Cdd:cd03226    2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 -YALFPNmTTERNIAFGLKmqKVPENEQRksVAEVIELVGLKG-KEQHlPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:cd03226   81 dYQLFTD-SVREELLLGLK--ELDAGNEQ--AETVLKDLDLYAlKERH-PLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 162 SALDaqiRKHLRQ---QIRQIQRELNlTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03226  155 SGLD---YKNMERvgeLIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 4-221 2.18e-38

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: 136.59  E-value: 2.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAAT-PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS--SPPQQREIGMV 80
Cdd:cd03253    1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFpNMTTERNIAFGlkMQKVPENEQRKS-----VAEVIE--------LVGLKGKeqhlphQLSGGQRQRVALARA 147
Cdd:cd03253   81 PQDTVLF-NDTIGYNIRYG--RPDATDEEVIEAakaaqIHDKIMrfpdgydtIVGERGL------KLSGGEKQRVAIARA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAENL 221
Cdd:cd03253  152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEEL 222
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 14-212 2.92e-38

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: 134.27  E-value: 2.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmt 91
Cdd:cd03246   13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 terniafglkmqkvpeneqrkSVAEVIelvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKH 171
Cdd:cd03246   91 ---------------------SIAENI---------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 738468658 172 LRQQIRQIqRELNLTTIFVTHdQEEAMLMSDRIFLMNKGEI 212
Cdd:cd03246  135 LNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 7-221 5.72e-38

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: 135.98  E-value: 5.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDG---------RIYVNKQDItssppqQREI 77
Cdd:COG1119    7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerRGGEDVWEL------RKRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVfqSYAL---FPNMTTERNI----AFG-LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV 149
Cdd:COG1119   81 GLV--SPALqlrFPRDETVLDVvlsgFFDsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSD------TAENL 221
Cdd:COG1119  159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGpkeevlTSENL 236
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 21-225 8.40e-38

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 137.40  E-value: 8.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  21 GLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMVFQS-YA-LFPNMTTE 93
Cdd:PRK11308  33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVG 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFGLKMQ-KVPENEQRKSVAEVIELVGLKGKE-QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKH 171
Cdd:PRK11308 113 QILEEPLLINtSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQ 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 172 LRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK11308 193 VLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 6-213 2.03e-37

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: 133.17  E-value: 2.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPpqQREIGMVFQSYA 85
Cdd:cd03269    3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEERG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:cd03269   81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738468658 166 AQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03269  161 PVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 4-211 6.47e-37

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: 131.82  E-value: 6.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLT-----KSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQditssppqqreIG 78
Cdd:cd03250    1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  79 MVFQSyALFPNMTTERNIAFGLkmqkvPENEQRksVAEVIELVGLKGKEQHLPHQ-----------LSGGQRQRVALARA 147
Cdd:cd03250   70 YVSQE-PWIQNGTIRENILFGK-----PFDEER--YEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIrqIQRELNL--TTIFVTHdQEEAMLMSDRIFLMNKGE 211
Cdd:cd03250  142 VYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLLNnkTRILVTH-QLQLLPHADQIVVLDNGR 204
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 14-213 1.00e-36

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: 131.56  E-value: 1.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFpNMT 91
Cdd:cd03245   15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGlkmqKVPENEQRksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03245   94 LRDNITLG----APLADDER--ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEP 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQeeAML-MSDRIFLMNKGEIV 213
Cdd:cd03245  168 TSAMDMNSEERLKERLRQLLGD--KTLIIITHRP--SLLdLVDRIIVMDSGRIV 217
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 1-234 1.11e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 132.73  E-value: 1.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGL-----EPVNDGRIYVNKQDITSSP--PQ 73
Cdd:PRK14247   1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDviEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  74 QREIGMVFQSYALFPNMTTERNIAFGLKMQKVPEN--EQRKSVAEVIELVGL----KGKEQHLPHQLSGGQRQRVALARA 147
Cdd:PRK14247  81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPAN 227
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238


                 ....*..
gi 738468658 228 EFVARFM 234
Cdd:PRK14247 239 ELTEKYV 245
cbiO PRK13642
energy-coupling factor transporter ATPase;
19-222 2.76e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 132.14  E-value: 2.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  19 FSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP--PQQREIGMVFQSY-ALFPNMTTERN 95
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwNLRRKIGMVFQNPdNQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  96 IAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQ 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738468658 176 IRQIQRELNLTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAENLY 222
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELF 228
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 14-219 2.97e-36

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: 137.57  E-value: 2.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmT 91
Cdd:COG4618  343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-T 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIA-FG-LKMQKVPENEQRKSVAEVIelvglkgkeQHLP-----------HQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:COG4618  422 IAENIArFGdADPEKVVAAAKLAGVHEMI---------LRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLD 492

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQeEAMLMSDRIFLMNKGEIVQSDTAE 219
Cdd:COG4618  493 EPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRD 551
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-217 3.04e-36

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 131.73  E-value: 3.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSF---------AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP 71
Cdd:PRK10419   1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  72 PQQ-----REIGMVFQSY--ALFPNMTTERNIAFGLK-MQKVPENEQRKSVAEVIELVGLK-GKEQHLPHQLSGGQRQRV 142
Cdd:PRK10419  81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 143 ALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDT 217
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 1-234 5.57e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 130.73  E-value: 5.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN-----DGRIYVNKQDITS---SP 71
Cdd:PRK14267   1 MKFAIeTVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdvDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  72 PQ-QREIGMVFQSYALFPNMTTERNIAFGLKMQKVPENeqRKSVAEVIELV--------GLKGKEQHLPHQLSGGQRQRV 142
Cdd:PRK14267  81 IEvRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKS--KKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 143 ALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLY 222
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236

                        250
                 ....*....|..
gi 738468658 223 TQPANEFVARFM 234
Cdd:PRK14267 237 ENPEHELTEKYV 248
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-210 7.84e-36

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: 129.48  E-value: 7.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSF-------AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQ----DIT 68
Cdd:COG4778    1 MTTLLeVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  69 SSPPQQ------REIGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHL-PHQLSGGQRQR 141
Cdd:COG4778   81 QASPREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 142 VALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDqEEAM-LMSDRIFLMNKG 210
Cdd:COG4778  161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPF 228
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 20-243 1.04e-35

nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 129.41  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   20 SGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVND----GRIYVNKQDITSSPPQQREIGMVFQS--YALFPNMTTE 93
Cdd:TIGR02770   3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLtqtsGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   94 RNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:TIGR02770  83 NHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658  171 HLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEfVARfmghyNLVSAH 243
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE-TTR-----KLLSAH 229
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
32-226 1.76e-35

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 131.92  E-value: 1.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  32 IT-LLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQ---DITSS---PPQQREIGMVFQSYALFPNMTTERNIAFGLKmqk 104
Cdd:PRK11144  26 ITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGiclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 105 vpeneqRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQR 181
Cdd:PRK11144 103 ------KSMVAQFDKIVALLGIEPLLdryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 738468658 182 ELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 1-225 2.01e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 129.92  E-value: 2.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAAT-PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REI 77
Cdd:PRK13652   1 MHLIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSY--ALFpNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRIL 155
Cdd:PRK13652  81 GLVFQNPddQIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 156 LLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 18-208 2.49e-35

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 128.36  E-value: 2.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR------EIGMVFQSYALFPNMT 91
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKH 171
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 738468658 172 LRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMN 208
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
cbiO PRK13644
energy-coupling factor transporter ATPase;
7-226 2.55e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 129.72  E-value: 2.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFA-ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYV---NKQDITSSPPQQREIGMVFQ 82
Cdd:PRK13644   5 ENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgiDTGDFSKLQGIRKLVGIVFQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 S-YALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:PRK13644  85 NpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 162 SALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEaMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
17-225 2.94e-35

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 129.50  E-value: 2.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMVFQSYALFPNMT 91
Cdd:PRK11831  21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMSMLFQSGALFTDMN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLKMQ-KVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:PRK11831 101 VFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 171 HLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-219 4.04e-35

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 133.61  E-value: 4.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-SSPPQQRE-- 76
Cdd:COG3845    2 MPPALeLRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIAlg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSYALFPNMT-TErNIAFGL---KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKP 152
Cdd:COG3845   82 IGMVHQHFMLVPNLTvAE-NIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS-DTAE 219
Cdd:COG3845  161 RILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTvDTAE 227
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 4-221 5.13e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 129.44  E-value: 5.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSF-AATP----VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRI---YVNKQ---------- 65
Cdd:PRK13651   3 IKVKNIVKIFnKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKnkkktkekek 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  66 ---DITSSPPQ----------QREIGMVFQ--SYALFPNmTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKgkEQHL 130
Cdd:PRK13651  83 vleKLVIQKTRfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLD--ESYL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 131 ---PHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKhlrqQIRQIQRELNL---TTIFVTHDQEEAMLMSDRI 204
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVK----EILEIFDNLNKqgkTIILVTHDLDNVLEWTKRT 235

                        250
                 ....*....|....*...
gi 738468658 205 FLMNKGEIVQ-SDTAENL 221
Cdd:PRK13651 236 IFFKDGKIIKdGDTYDIL 253
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 7-223 1.08e-34

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 127.12  E-value: 1.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSY 84
Cdd:COG4604    5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQEN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ALFPNMTTERNIAFG--------LKmqkvpeNEQRKSVAEVIELVGLKG-KEQHLpHQLSGGQRQRVALARALVMKPRIL 155
Cdd:COG4604   85 HINSRLTVRELVAFGrfpyskgrLT------AEDREIIDEAIAYLDLEDlADRYL-DELSGGQRQRAFIAMVLAQDTDYV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 156 LLDEPLSALDAqirKHLRQ---QIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYT 223
Cdd:COG4604  158 LLDEPLNNLDM---KHSVQmmkLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 14-213 1.20e-34

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 133.84  E-value: 1.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFpNMT 91
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGT 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   92 TERNIAFGlkmqkVPE-NEQRksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:TIGR03375 555 LRDNIALG-----APYaDDEE--ILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658  160 PLSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQeeAML-MSDRIFLMNKGEIV 213
Cdd:TIGR03375 628 PTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRT--SLLdLVDRIIVMDNGRIV 678
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
8-234 3.86e-34

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 126.24  E-value: 3.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-----------SSPPQQR- 75
Cdd:PRK10619  10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRl 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 ---EIGMVFQSYALFPNMTTERNIAFG-LKMQKVPENEQRKSVAEVIELVGLKGKEQ-HLPHQLSGGQRQRVALARALVM 150
Cdd:PRK10619  90 lrtRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 151 KPRILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFV 230
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248


                 ....
gi 738468658 231 ARFM 234
Cdd:PRK10619 249 QQFL 252
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 16-213 3.46e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 124.19  E-value: 3.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ----QREIGMVFQS--YALFpN 89
Cdd:PRK13636  19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQDpdNQLF-S 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:PRK13636  98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738468658 170 KHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 18-234 1.06e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 122.08  E-value: 1.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQ------DI--TSSPPQQREIGMVFQSYALFPN 89
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIfqIDAIKLRKEVGMVFQQPNPFPH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTERNIAFGLKMQKVPEN-EQRKSVAEVIELVGLkGKEQH-----LPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGL-WKEVYdrlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 164 LDAQIRKHLRQQIRQIQRElnLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFM 234
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 21-224 2.03e-32

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: 126.46  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   21 GLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYV----NKQDITSSPPQQR-----EIGMVFQSYALFPNMT 91
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRgrakrYIGILHQEYDLYPHRT 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   92 TERNI--AFGLKMQKvpENEQRKSVAeVIELVGLKGKE-----QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:TIGR03269 382 VLDNLteAIGLELPD--ELARMKAVI-TLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  165 DAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:TIGR03269 459 DPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 14-224 2.43e-32

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: 120.41  E-value: 2.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT--SSPPQQREIGMVFQSYALFpNMT 91
Cdd:cd03251   13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGLVSQDVFLF-NDT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLkmqkvpENEQRKSVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03251   92 VAENIAYGR------PGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:cd03251  166 TSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 6-213 2.84e-32

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 122.14  E-value: 2.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITssPPQQREIGmvfqsY- 84
Cdd:COG4152    4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIG-----Yl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ----ALFPNMTTERNIAF-----GLkmqkvPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRIL 155
Cdd:COG4152   77 peerGLYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 156 LLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:COG4152  152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKV 208
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
7-213 4.26e-32

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 119.59  E-value: 4.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF-AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-----SSPPQQREIGMV 80
Cdd:PRK10908   5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQIGMI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:PRK10908  85 FQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 161 LSALDAQIRKHLRQQIRQIQReLNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
6-178 4.34e-32

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 119.14  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITssppQQREigmVFQSYA 85
Cdd:PRK13538   4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LF--------PNMTTERNIAFGLKMQKVPENEQrksVAEVIELVGLKGKEqHLP-HQLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK13538  77 LYlghqpgikTELTALENLRFYQRLHGPGDDEA---LWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWI 152

                        170       180
                 ....*....|....*....|....*.
gi 738468658 157 LDEPLSALD----AQIRKHLRQQIRQ 178
Cdd:PRK13538 153 LDEPFTAIDkqgvARLEALLAQHAEQ 178
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 6-212 6.13e-32

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: 117.92  E-value: 6.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTksfaATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR-EIGMVF--- 81
Cdd:cd03215    7 VRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYvpe 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 --QSYALFPNMTTERNIAfglkmqkvpeneqrksvaevielvglkgkeqhLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:cd03215   83 drKREGLVLDLSVAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDE 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:cd03215  131 PTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 18-221 6.77e-32

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: 119.51  E-value: 6.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFpNMTTERN 95
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  96 IAF---GLKMQKVPENEQRKSVAEVIELVGLkGKEQHLPHQ---LSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:cd03252   96 IALadpGMSMERVIEAAKLAGAHDFISELPE-GYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738468658 170 KHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:cd03252  175 HAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
16-217 8.98e-32

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 119.15  E-value: 8.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS------SPPQQREIGMVFQSYALFPN 89
Cdd:PRK11629  22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakAELRNQKLGFIYQFHHLLPD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738468658 170 KHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSdRIFLMNKGEIVQSDT 217
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 15-227 1.13e-31

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 125.63  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   15 ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFpNMTT 92
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLF-SRSI 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   93 ERNIAFGlkmqkvpenEQRKSVAEVIELVGLKGKEQ---HLPH-----------QLSGGQRQRVALARALVMKPRILLLD 158
Cdd:TIGR01846 548 RDNIALC---------NPGAPFEHVIHAAKLAGAHDfisELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFD 618

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658  159 EPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPAN 227
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 24-221 1.25e-31

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 118.41  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   24 FSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVnkqDITSSPPQQREIGMVFQSYAL---FPnMTTERNIAFG- 99
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKV---AGASPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  100 ---LKMQKVPENEQRKSVAEVIELVGLkgkeQHLPH----QLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHL 172
Cdd:TIGR03771  77 tghIGWLRRPCVADFAAVRDALRRVGL----TELADrpvgELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 738468658  173 RQQIRQIQRELNlTTIFVTHDQEEAMLMSDRIFLMNkGEIVQSDTAENL 221
Cdd:TIGR03771 153 TELFIELAGAGT-AILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 1-213 2.05e-31

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: 116.88  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTK------SFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPVND-GRIYVNKQDITSSPP 72
Cdd:cd03213    1 GVTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLDKRSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  73 QqREIGMVFQSYALFPNMTTERNIAFGLKMQkvpeneqrksvaevielvglkgkeqhlphQLSGGQRQRVALARALVMKP 152
Cdd:cd03213   81 R-KIIGYVPQDDILHPTLTVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNP 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHD-QEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03213  131 SLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 6-235 2.91e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 119.05  E-value: 2.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCL-------AGLEPVND----GRIYVNKQDITSSppqQ 74
Cdd:PRK14271  24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSGDvllgGRSIFNYRDVLEF---R 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  75 REIGMVFQSYALFPnMTTERNIAFGLKMQK-VPENEQRKSVAEVIELVGL----KGKEQHLPHQLSGGQRQRVALARALV 149
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEF 229
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257


                 ....*.
gi 738468658 230 VARFMG 235
Cdd:PRK14271 258 TARYVA 263
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 17-234 4.55e-31

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 123.53  E-value: 4.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFPNmTTER 94
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGVVLQNGRLMSG-SIFE 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   95 NIAFGLKMqkVPENEQrksvaEVIELVGLKGKEQHLP---H--------QLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:TIGR03797 546 NIAGGAPL--TLDEAW-----EAARMAGLAEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEATSA 618

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658  164 LDAQIRKHLRQQIRQiqreLNLTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAENLYTQPAneFVARFM 234
Cdd:TIGR03797 619 LDNRTQAIVSESLER----LKVTRIVIAHRLSTIR-NADRIYVLDAGRVVQQGTYDELMAREG--LFAQLA 682
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 6-175 6.59e-31

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: 115.92  E-value: 6.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ-QREIGMVFQSY 84
Cdd:TIGR01189   3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   85 ALFPNMTTERNIAFglkMQKVPENEQRkSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:TIGR01189  83 GLKPELSALENLHF---WAAIHGGAQR-TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158

                         170
                  ....*....|....*....
gi 738468658  165 DAQ--------IRKHLRQQ 175
Cdd:TIGR01189 159 DKAgvallaglLRAHLARG 177
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 21-228 7.19e-31

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 117.18  E-value: 7.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  21 GLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN-----DGRIYVNKQDI----TSSPPQQREIGMVFQSYALFPnMT 91
Cdd:PRK14239  23 SVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTVDLRKEIGMVFQQPNPFP-MS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLKMQKVPENEQRKSVAEVielvGLKGK------EQHLpHQ----LSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:PRK14239 102 IYENVVYGLRLKGIKDKQVLDEAVEK----SLKGAsiwdevKDRL-HDsalgLSGGQQQRVCIARVLATSPKIILLDEPT 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 162 SALD----AQIRKHLrqqirqiqreLNL----TTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANE 228
Cdd:PRK14239 177 SALDpisaGKIEETL----------LGLkddyTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 18-216 1.12e-30

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: 115.71  E-value: 1.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDitSSPPqqrEIGMVFQsyalfPNMTTERNIA 97
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV--SSLL---GLGGGFN-----PELTGRENIY 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  98 FGLKMQKVPENEQRKSVAEVIELVGLkGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQI 176
Cdd:cd03220  107 LNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 738468658 177 RQIQRELNlTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSD 216
Cdd:cd03220  186 RELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
cbiO PRK13643
energy-coupling factor transporter ATPase;
13-224 1.18e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 117.53  E-value: 1.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  13 FAATPVFSgLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP------PQQREIGMVFQsyal 86
Cdd:PRK13643  17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQ---- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNM-----TTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKgKE--QHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PRK13643  92 FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA-DEfwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQrELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 17-221 1.31e-30

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: 115.79  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmTTER 94
Cdd:cd03254   17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIME 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NIAFGlkmqkvPENEQRKSVAEVIELVGL--------KGKEQHLPHQ---LSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd03254   96 NIRLG------RPNATDEEVIEAAKEAGAhdfimklpNGYDTVLGENggnLSQGERQLLAIARAMLRDPKILILDEATSN 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 164 LDAQIRKHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:cd03254  170 IDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 1-232 1.78e-30

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 115.76  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE---I 77
Cdd:PRK10895   1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVA-EVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK10895  81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAnELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYtqpANEFVAR 232
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL---QDEHVKR 232
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 18-229 1.82e-30

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 120.97  E-value: 1.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKST----LLRCLAglepvNDGRIYVNKQDITSSPPQQ-----REIGMVFQ--SYAL 86
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSL 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKM-QKVPENEQRKS-VAEVIELVGLKGKEQH-LPHQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhQPTLSAAQREQqVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEF 229
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 22-234 2.84e-30

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 121.12  E-value: 2.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----REIGMVFQS-YA-LFPNMTTER 94
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGD 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NIAFGLKMQKVPENEQ-RKSVAEVIELVGLKGKEQ-HLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHL 172
Cdd:PRK10261 423 SIMEPLRVHGLLPGKAaAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 173 RQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFM 234
Cdd:PRK10261 503 INLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
cbiO PRK13646
energy-coupling factor transporter ATPase;
22-224 3.15e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 116.42  E-value: 3.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP------PQQREIGMVFQ--SYALFPNmTTE 93
Cdd:PRK13646  26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirPVRKRIGMVFQfpESQLFED-TVE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFGLKMQKVP-ENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHL 172
Cdd:PRK13646 105 REIIFGPKNFKMNlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQV 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738468658 173 RQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK13646 185 MRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 17-213 4.41e-30

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: 120.31  E-value: 4.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFpNMTTER 94
Cdd:COG5265  372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAY 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NIAFGLkmqkvPENEQRKsVAEVIELVGLKGKEQHLPHQ-----------LSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:COG5265  451 NIAYGR-----PDASEEE-VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 164 LDAQIRKHLRQQIRQIQRelNLTTIFVTH------DqeeamlmSDRIFLMNKGEIV 213
Cdd:COG5265  525 LDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIV 571
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 14-196 5.04e-30

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 114.04  E-value: 5.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmT 91
Cdd:PRK10247  18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAF----------------GLKMQKVPENEQRKSVAEvielvglkgkeqhlphqLSGGQRQRVALARALVMKPRIL 155
Cdd:PRK10247  97 VYDNLIFpwqirnqqpdpaifldDLERFALPDTILTKNIAE-----------------LSGGEKQRISLIRNLQFMPKVL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 738468658 156 LLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEE 196
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-206 5.22e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 113.10  E-value: 5.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  12 SFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGmvfqsyALFPnMT 91
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGL----KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:NF040873  74 VRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 738468658 168 IRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFL 206
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 18-226 5.61e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 116.49  E-value: 5.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYV----NKQDI-----TSSPPQQ---------REIGM 79
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKnnhelITNPYSKkiknfkelrRRVSM 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQ--SYALFPNmTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKgkEQHL---PHQLSGGQRQRVALARALVMKPRI 154
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD--DSYLersPFGLSGGQKRRVAIAGILAIQPEI 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 155 LLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-219 5.64e-30

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 114.41  E-value: 5.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSF-----------------AATP-----VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVND 57
Cdd:COG1134    1 MSSMIeVENVSKSYrlyhepsrslkelllrrRRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  58 GRIYVNKQdiTSSPpqqREIGMVFQsyalfPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLkGKEQHLP-HQLSG 136
Cdd:COG1134   81 GRVEVNGR--VSAL---LELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL-GDFIDQPvKTYSS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 137 GQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSD 216
Cdd:COG1134  150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228


                 ...
gi 738468658 217 TAE 219
Cdd:COG1134  229 DPE 231
cbiO PRK13641
energy-coupling factor transporter ATPase;
22-225 1.57e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 114.54  E-value: 1.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ------REIGMVFQ--SYALFPNmTTE 93
Cdd:PRK13641  26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQfpEAQLFEN-TVL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFGLKMQKVPENEQRKSVAEVIELVGLKGK-EQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHL 172
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 173 RQQIRQIQRELNlTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK13641 185 MQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 1-213 2.01e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 114.06  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSFA-ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QRE 76
Cdd:PRK13647   1 MDNIIeVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSY--ALFpNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRI 154
Cdd:PRK13647  81 VGLVFQDPddQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 155 LLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 6-228 2.59e-29

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 113.34  E-value: 2.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPV-----NDGRIYVNKQDITSS---PPQ-QRE 76
Cdd:PRK14243  13 TENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPdvdPVEvRRR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSYALFPNMTTErNIAFGLK-------MQKVPENEQRKSVA--EVielvglKGKEQHLPHQLSGGQRQRVALARA 147
Cdd:PRK14243  93 IGMVFQKPNPFPKSIYD-NIAYGARingykgdMDELVERSLRQAALwdEV------KDKLKQSGLSLSGGQQQRLCIARA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 148 LVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElnLTTIFVTHDQEEAMLMSDRIFLMN---------KGEIVQSDTA 218
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRT 243

                        250
                 ....*....|
gi 738468658 219 ENLYTQPANE 228
Cdd:PRK14243 244 EKIFNSPQQQ 253
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-193 3.80e-29

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 117.09  E-value: 3.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKqDITssppqqreIGMVFQSYA 85
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR--------IGYLPQEPP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIAFGL---------------KMQKVPENEQRKS-----------------VAEVIELVGLKGKEQHLP-H 132
Cdd:COG0488   72 LDDDLTVLDTVLDGDaelraleaeleeleaKLAEPDEDLERLAelqeefealggweaearAEEILSGLGFPEEDLDRPvS 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 133 QLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQiqreLNLTTIFVTHD 193
Cdd:COG0488  152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHD 208
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 7-227 5.16e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 112.44  E-value: 5.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN-----DGRIYVNKQDITSSPPQ----QREI 77
Cdd:PRK14258  11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNlnrlRRQV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFPnMTTERNIAFGLKMQK-VPENEQRKSVAEVIELVGLKGKEQHLPHQ----LSGGQRQRVALARALVMKP 152
Cdd:PRK14258  91 SMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSD--RIFLMNK---GEIVQSDTAENLYTQPAN 227
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDftAFFKGNEnriGQLVEFGLTKKIFNSPHD 249
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 8-224 5.88e-29

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 112.23  E-value: 5.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRI-YVNK----QDITSSPPQQR------E 76
Cdd:TIGR02323   8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRsgaeLELYQLSEAERrrlmrtE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   77 IGMVFQSYALFPNMTT-------ERNIAFGLKMQKVPENEQRKSVAEV-IELvglkGKEQHLPHQLSGGQRQRVALARAL 148
Cdd:TIGR02323  88 WGFVHQNPRDGLRMRVsaganigERLMAIGARHYGNIRATAQDWLEEVeIDP----TRIDDLPRAFSGGMQQRLQIARNL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  149 VMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS-------DTAENL 221
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESgltdqvlDDPQHP 243


                  ...
gi 738468658  222 YTQ 224
Cdd:TIGR02323 244 YTQ 246
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 6-174 6.81e-29

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 110.73  E-value: 6.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQReIGMVFQSYA 85
Cdd:PRK13539   5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIAFGLKMQkvpeNEQRKSVAEVIELVGLKGKEqHLPHQ-LSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:PRK13539  84 MKPALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLA-HLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158

                        170
                 ....*....|....*...
gi 738468658 165 DAQ--------IRKHLRQ 174
Cdd:PRK13539 159 DAAavalfaelIRAHLAQ 176
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
4-224 1.54e-28

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 110.87  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVF 81
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTERNIAFGlkmqKVPEN--------EQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPR 153
Cdd:PRK11231  83 QHHLTPEGITVRELVAYG----RSPWLslwgrlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 154 ILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
6-213 2.55e-28

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: 2.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTksfaATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-SSPPQQREIGMVF--- 81
Cdd:COG1129  259 VEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYvpe 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 --QSYALFPNMTTERNIA---------FGLkmqkVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALV 149
Cdd:COG1129  335 drKGEGLVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLA 410

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 150 MKPRILLLDEPLSALD--AqirkhlRQQIRQIQREL---NLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:COG1129  411 TDPKVLILDEPTRGIDvgA------KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIV 473
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 16-192 3.72e-28

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 114.90  E-value: 3.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVnkqditssPPQQReigMVF---QSYalFPNMTT 92
Cdd:COG4178  376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VLFlpqRPY--LPLGTL 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  93 ERNIAFGLKMQKVPENEqrksVAEVIELVGLK------GKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDA 166
Cdd:COG4178  443 REALLYPATAEAFSDAE----LREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518

                        170       180
                 ....*....|....*....|....*.
gi 738468658 167 QIRKHLRQQIRqiQRELNLTTIFVTH 192
Cdd:COG4178  519 ENEAALYQLLR--EELPGTTVISVGH 542
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 17-225 4.77e-28

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 114.82  E-value: 4.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFpNMTTER 94
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLF-SGSVRE 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   95 NIAFGLkmQKVPENEQRKSVAE------VIEL-------VGLKGKeqhlphQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:TIGR00958 574 NIAYGL--TDTPDEEIMAAAKAanahdfIMEFpngydteVGEKGS------QLSGGQKQRIAIARALVRKPRVLILDEAT 645

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658  162 SALDAQIrKHLRQQIRQIQrelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:TIGR00958 646 SALDAEC-EQLLQESRSRA---SRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 14-212 7.33e-28

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 113.60  E-value: 7.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   92 TERNIA-FGlkmqkvpENEQRKSVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:TIGR01842 408 VAENIArFG-------ENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDE 480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 738468658  160 PLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHdQEEAMLMSDRIFLMNKGEI 212
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRI 531
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 7-234 8.39e-28

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: 113.36  E-value: 8.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLE--PVNDGRI-----------YVNKQDITSSP-- 71
Cdd:TIGR03269   4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVERPSKVGEPcp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   72 -------PQQ---------------REIGMVFQ-SYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQ 128
Cdd:TIGR03269  84 vcggtlePEEvdfwnlsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRIT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  129 HLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMN 208
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243

                         250       260
                  ....*....|....*....|....*.
gi 738468658  209 KGEIVQSDTAEnlytqpanEFVARFM 234
Cdd:TIGR03269 244 NGEIKEEGTPD--------EVVAVFM 261
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 7-212 8.44e-28

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: 108.33  E-value: 8.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSF---AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVF 81
Cdd:cd03248   15 QNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTErNIAFGLK---MQKVPENEQRKSVAEVIEL--------VGLKGKeqhlphQLSGGQRQRVALARALVM 150
Cdd:cd03248   95 QEPVLFARSLQD-NIAYGLQscsFECVKEAAQKAHAHSFISElasgydteVGEKGS------QLSGGQKQRVAIARALIR 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 151 KPRILLLDEPLSALDAQIRKHLRQQIRQIQRElnlTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:cd03248  168 NPQVLILDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 17-213 1.04e-27

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: 108.19  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDitssPPQQRE-----IGMVF-QSYALFPNM 90
Cdd:cd03267   35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKkflrrIGVVFgQKTQLWWDL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  91 TTERNIAFGLKMQKVPENEQRKSVAEVIELVGLkGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:cd03267  111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738468658 170 KHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03267  190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
cbiO PRK13649
energy-coupling factor transporter ATPase;
14-215 1.57e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.06  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATP----VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP------PQQREIGMVFQs 83
Cdd:PRK13649  14 AGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQ- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 yalFPNM-----TTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGK--EQHlPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK13649  93 ---FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILAMEPKILV 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQrELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 7-210 1.93e-27

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 108.15  E-value: 1.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-REIGMV--FQS 83
Cdd:PRK11300   9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARMGVVrtFQH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERN--IAFGLKMQ--------KVP-----ENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARAL 148
Cdd:PRK11300  89 VRLFREMTVIENllVAQHQQLKtglfsgllKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCM 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 149 VMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKG 210
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
7-210 2.24e-27

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 109.12  E-value: 2.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMVFQSYA 85
Cdd:PRK13537  11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQFDN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIA-----FGLKMQKVpeneqRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:PRK13537  91 LDPDFTVRENLLvfgryFGLSAAAA-----RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 161 LSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKG 210
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 15-193 2.38e-27

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: 112.07  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   15 ATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPnmTT 92
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLFD--TT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   93 ER-NIAFGLKmqKVPENEqrksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:TIGR02868 425 VReNLRLARP--DATDEE----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEP 498

                         170       180       190
                  ....*....|....*....|....*....|...
gi 738468658  161 LSALDAQIRKHLRQQIRQIQRElnLTTIFVTHD 193
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALSG--RTVVLITHH 529
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
8-210 2.48e-27

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 109.54  E-value: 2.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDItssPPQQR----EIGMVFQS 83
Cdd:PRK13536  46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARlaraRIGVVPQF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIA-----FGLKMQKVPEneqrkSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:PRK13536 123 DNLDLEFTVRENLLvfgryFGMSTREIEA-----VIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKG 210
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAG 248
cbiO PRK13645
energy-coupling factor transporter ATPase;
4-213 2.50e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 108.56  E-value: 2.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAA-TPV-FSGLN---FSVSKGEFITLLGPSGCGKSTLLRCLAGL-------EPVNDGRIYVNKQDITSSP 71
Cdd:PRK13645   7 IILDNVSYTYAKkTPFeFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgqTIVGDYAIPANLKKIKEVK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  72 PQQREIGMVFQ--SYALFPNmTTERNIAFGLKMQKVPENEQRKSVAEVIELVGL-KGKEQHLPHQLSGGQRQRVALARAL 148
Cdd:PRK13645  87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 149 VMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 18-213 2.56e-27

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: 106.97  E-value: 2.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVND---GRIYVNKQDitSSPPQ-QREIGMVFQSYALFPNMTTE 93
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP--RKPDQfQKCVAYVRQDDILLPGLTVR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  94 RNIAFG--LKMQKVPENEQRKSVAEVIEL--VGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:cd03234  100 ETLTYTaiLRLPRKSSDAIRKKRVEDVLLrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 738468658 170 KHLRQQIRQIQRElNLTTIFVTHD-QEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03234  180 LNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 6-224 2.57e-27

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 107.70  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQD------ITSSPPQQR---- 75
Cdd:PRK11701   9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERRrllr 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  76 -EIGMVFQSYA--LFPNMTTERNIafGLKMQKVPEN---EQRKSVAEVIELVGLKGKE-QHLPHQLSGGQRQRVALARAL 148
Cdd:PRK11701  89 tEWGFVHQHPRdgLRMQVSAGGNI--GERLMAVGARhygDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 149 VMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS-------DTAENL 221
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESgltdqvlDDPQHP 246


                 ...
gi 738468658 222 YTQ 224
Cdd:PRK11701 247 YTQ 249
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-236 2.80e-27

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 109.02  E-value: 2.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSF-----------AATPVFS----------GLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRIY 61
Cdd:COG4586    2 IEVENLSKTYrvyekepglkgALKGLFRreyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  62 VNKQDitsspPQQRE------IGMVF-QSYALFPNMTT-ErniAFGL--KMQKVPENEQRKSVAEVIELVGLKGKEQHLP 131
Cdd:COG4586   81 VLGYV-----PFKRRkefarrIGVVFgQRSQLWWDLPAiD---SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 132 HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNlTTIFVT-HDqeeamlMSD------RI 204
Cdd:COG4586  153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERG-TTILLTsHD------MDDiealcdRV 225

                        250       260       270
                 ....*....|....*....|....*....|..
gi 738468658 205 FLMNKGEIVqsdtaenlYTQPANEFVARFMGH 236
Cdd:COG4586  226 IVIDHGRII--------YDGSLEELKERFGPY 249
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 6-215 4.64e-27

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 111.30  E-value: 4.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP---QQREIGMVFQ 82
Cdd:PRK15439  14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLkmQKVPENEQRksVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PRK15439  94 EPLLFPNLSVKENILFGL--PKRQASMQK--MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 163 ALDAQIRKHLRQQIRQIQrELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:PRK15439 170 SLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
7-220 5.34e-27

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 111.74  E-value: 5.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA----TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-----RE- 76
Cdd:PRK10535   8 KDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREh 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK10535  88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAEN 220
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAA-QAERVIEIRDGEIVRNPPAQE 229
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-212 6.51e-27

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 107.02  E-value: 6.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVI-AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGL---EPVNDGRIYVNKQDITSSPPQQRE 76
Cdd:PRK09984   1 MQTIIrVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 I-------GMVFQSYALFPNMTTERNIAFGlKMQKVP---------ENEQRKSVAEVIELVGLKgkeqHLPHQ----LSG 136
Cdd:PRK09984  81 IrksrantGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMV----HFAHQrvstLSG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 137 GQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 17-234 7.36e-27

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 110.95  E-value: 7.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKS----TLLRCLAGlEPVN--DGRIYVNKQDITSSPPQQ------REIGMVFQS- 83
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS-PPVVypSGDIRFHGESLLHASEQTlrgvrgNKIAMIFQEp 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 -YALFPNMTTERNIAFGLKMQKVPENE-QRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:PRK15134 102 mVSLNPLHTLEKQLYEVLSLHRGMRREaARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIAD 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFM 234
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 5-178 7.36e-27

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: 105.27  E-value: 7.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   5 IAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQ-DITSSPPQQREIGMVFQS 83
Cdd:cd03231    2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFglkmqkVPENEQRKSVAEVIELVGLKGKEqHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03231   82 PGIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNGFE-DRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154

                        170
                 ....*....|....*.
gi 738468658 163 ALDAQIRKHLRQQIRQ 178
Cdd:cd03231  155 ALDKAGVARFAEAMAG 170
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 22-225 1.61e-26

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 109.93  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNdGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmTTERNIAFG 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQLPHG-TLRDNVLLG 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 100 ---LKMQKVPENEQRKSVAEVIELVglkgkEQHLPHQ-------LSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:PRK11174 447 npdASDEQLQQALENAWVSEFLPLL-----PQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 170 KHLRQQIRQIQRelNLTTIFVTH--DQEEAMlmsDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK11174 522 QLVMQALNAASR--RQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGDYAELSQAG 574
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 16-229 1.79e-26

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 109.94  E-value: 1.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKS----TLLRCL--AGLEpVNDGRIYV---NKQDI---TSSPPQQR-----EIG 78
Cdd:PRK10261  29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLrrrSRQVIelsEQSAAQMRhvrgaDMA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  79 MVFQS--YALFPNMTTERNIAFGLKM-QKVPENEQRKSVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMKP 152
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSCRP 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEF 229
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 17-217 2.38e-26

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: 104.11  E-value: 2.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNmTTER 94
Cdd:cd03244   18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NIAfglkmqkvPENEQRKS-VAEVIELVGLKGKEQHLPHQL-----------SGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03244   97 NLD--------PFGEYSDEeLWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATA 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 163 ALDAQIRKHLRQQIRqiqREL-NLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDT 217
Cdd:cd03244  169 SVDPETDALIQKTIR---EAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDS 220
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-221 3.15e-26

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 109.83  E-value: 3.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAA-TPVfSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIY-----VNKQDITSsppqQREIGM 79
Cdd:NF033858 269 ARGLTMRFGDfTAV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT----RRRVGY 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLtTIFV-THDQEEAMLmSDRIFLMNKGEIVQSDTAENL 221
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGV-TIFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 11-227 1.08e-25

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 103.00  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  11 KSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPvNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFP 88
Cdd:COG4138    4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  89 NMTTERNIAFGLKmQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVM-------KPRILLLDEPL 161
Cdd:COG4138   83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 162 SALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTqPAN 227
Cdd:COG4138  162 NSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN 225
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
6-248 1.18e-25

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 103.72  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSF-------------AATPVfsglNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT---S 69
Cdd:PRK15112   7 VRNLSKTFryrtgwfrrqtveAVKPL----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  70 SPPQQReIGMVFQ--SYALFPNMTTERNIAFGLKMQKVPENEQR-KSVAEVIELVGLKGKE-QHLPHQLSGGQRQRVALA 145
Cdd:PRK15112  83 SYRSQR-IRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQReKQIIETLRQVGLLPDHaSYYPHMLAPGQKQRLGLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 146 RALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVThdQEEAML--MSDRIFLMNKGEIVQSDTAENLYT 223
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLA 239

                        250       260
                 ....*....|....*....|....*
gi 738468658 224 QPANEFVARfmghynLVSAHNANSL 248
Cdd:PRK15112 240 SPLHELTKR------LIAGHFGEAL 258
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 22-225 1.92e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 104.05  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGL----EPVNDGRIYVNKQDITSSPPQQR------EIGMVFQS--YALFPN 89
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTERNIAFGLKMQKVPENEQRKSVA-EVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKKTRRQRAiDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 166 AQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 7-219 2.70e-25

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: 100.68  E-value: 2.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLE--PVNDGRIYVNKQDITSSPPQQRE---IGMVF 81
Cdd:cd03217    4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERArlgIFLAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTE---RNIAFGlkmqkvpeneqrksvaevielvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLD 158
Cdd:cd03217   84 QYPPEIPGVKNAdflRYVNEG----------------------------------FSGGEKKRNEILQLLLLEPDLAILD 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLM-SDRIFLMNKGEIVQSDTAE 219
Cdd:cd03217  130 EPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-213 2.76e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 106.30  E-value: 2.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREigmvfqs 83
Cdd:COG0488  316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE------- 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 yALFPNMTTERNiafglkMQKVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:COG0488  389 -ELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 163 ALDAQIRkhlrqqirqiqRELNL-------TTIFVTHDQEeamLMS---DRIFLMNKGEIV 213
Cdd:COG0488  462 HLDIETL-----------EALEEalddfpgTVLLVSHDRY---FLDrvaTRILEFEDGGVR 508
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
17-213 5.23e-25

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 102.01  E-value: 5.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSP----PQQREIGMVFQSyalfPNMTT 92
Cdd:PRK13638  15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllALRQQVATVFQD----PEQQI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  93 -----ERNIAFGLKMQKVPENEQRKSVAEVIELVglkgKEQHLPHQ----LSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:PRK13638  91 fytdiDSDIAFSLRNLGVPEAEITRRVDEALTLV----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIfVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQIL 215
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
7-235 7.09e-25

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 101.60  E-value: 7.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT--SSPPQQREIGMVFQSY 84
Cdd:PRK10253  11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ALFPNMTTERNIAFGlKMQKVP-----ENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PRK10253  91 TTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQpanEFVARFMG 235
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA---ELIERIYG 242
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-233 7.83e-25

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 100.96  E-value: 7.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIA-ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIyvnkqditSSPPQQReIGM 79
Cdd:PRK09544   1 MTSLVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGY 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNM--TTERNiafglkMQKVPeNEQRKSVAEVIELVglkgKEQHL---PHQ-LSGGQRQRVALARALVMKPR 153
Cdd:PRK09544  72 VPQKLYLDTTLplTVNRF------LRLRP-GTKKEDILPALKRV----QAGHLidaPMQkLSGGETQRVLLARALLNRPQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 154 ILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNkGEIVQSDTAENLYTQPanEFVARF 233
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 8-225 8.10e-25

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 103.77  E-value: 8.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDI--TSSPPQQREIGMVFQSYA 85
Cdd:PRK09536   8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeaLSARAASRRVASVPQDTS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIafglKMQKVP--------ENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLL 157
Cdd:PRK09536  88 LSFEFDVRQVV----EMGRTPhrsrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 158 DEPLSALDaqirkhLRQQIRQIQ--REL---NLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK09536 164 DEPTASLD------INHQVRTLElvRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 14-224 8.70e-25

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 104.91  E-value: 8.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-RE-IGMVFQSYALFpNMT 91
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISVVSQRVHLF-SAT 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNiafgLKMQKVPENEQRksVAEVIELVGLkgkEQHLPH-------------QLSGGQRQRVALARALVMKPRILLLD 158
Cdd:PRK11160 430 LRDN----LLLAAPNASDEA--LIEVLQQVGL---EKLLEDdkglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLD 500

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
7-226 1.17e-24

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 100.34  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--RE-IGMVFQS 83
Cdd:PRK11614   9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimREaVAIVPEG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKMQKVPENEQRksVAEVIELVG-LKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PRK11614  89 RRVFSRMTVEENLAMGGFFAERDQFQER--IKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 163 ALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 22-226 1.92e-24

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 101.72  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNdGRI----YVNKQDITSSPPQQ------REIGMVFQS--YALFPN 89
Cdd:PRK09473  35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNLPEKElnklraEQISMIFQDpmTSLNPY 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTERNIAFGLKMQKvpeneqRKSVAEVIE-----LVGLKGKEQH-----LPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PRK09473 114 MRVGEQLMEVLMLHK------GMSKAEAFEesvrmLDAVKMPEARkrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPA 226
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 3-225 2.20e-24

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: 103.87  E-value: 2.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    3 YVIAENLTKSFAAT--PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIG 78
Cdd:TIGR03796 477 YVELRNITFGYSPLepPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlANSVA 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   79 MVFQSYALFPNmTTERNIAfgLKMQKVPENE-----QRKSVAEVIelVGLKGK-EQHLPH---QLSGGQRQRVALARALV 149
Cdd:TIGR03796 557 MVDQDIFLFEG-TVRDNLT--LWDPTIPDADlvracKDAAIHDVI--TSRPGGyDAELAEggaNLSGGQRQRLEIARALV 631

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  150 MKPRILLLDEPLSALDAQIRKHLRQQIRqiQRelNLTTIFVTH------DqeeamlmSDRIFLMNKGEIVQSDTAENLYT 223
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLR--RR--GCTCIIVAHrlstirD-------CDEIIVLERGKVVQRGTHEELWA 700


                  ..
gi 738468658  224 QP 225
Cdd:TIGR03796 701 VG 702
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
7-225 2.52e-24

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 99.86  E-value: 2.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITS--SPPQQREIGMVFQSY 84
Cdd:PRK10575  15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  85 ALFPNMTTERNIAFGlkmqKVPEN--------EQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK10575  95 PAAEGMTVRELVAIG----RYPWHgalgrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV---------QSDTAENLYTQP 225
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIaqgtpaelmRGETLEQIYGIP 248
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 7-221 2.75e-24

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: 103.64  E-value: 2.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    7 ENLTKSFAAT--PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQ 82
Cdd:TIGR02203 334 RNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQ 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   83 SYALFpNMTTERNIAFGlKMQKVPENEQRKSV--AEVIELVGLKGKEQHLP-----HQLSGGQRQRVALARALVMKPRIL 155
Cdd:TIGR02203 414 DVVLF-NDTIANNIAYG-RTEQADRAEIERALaaAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALLKDAPIL 491

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658  156 LLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 4-195 8.98e-24

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: 95.21  E-value: 8.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIyvnkqditssppqqreigmvfqs 83
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 yalfpnmtterniafglkmqkvpeneQRKSVAEVielvglkgkeQHLPhQLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd03221   58 --------------------------TWGSTVKI----------GYFE-QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                        170       180       190
                 ....*....|....*....|....*....|..
gi 738468658 164 LDAQIRKHLRQQIRQIQRELnlttIFVTHDQE 195
Cdd:cd03221  101 LDLESIEALEEALKEYPGTV----ILVSHDRY 128
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
6-175 1.08e-23

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 96.84  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSpPQQREIGMVFQSYA 85
Cdd:PRK13543  14 AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRFMAYLGHLPG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 LFPNMTTERNIAF-----GLKMQKVPENeqrksvaeVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:PRK13543  93 LKADLSTLENLHFlcglhGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164

                        170       180
                 ....*....|....*....|...
gi 738468658 161 LSALDAQ--------IRKHLRQQ 175
Cdd:PRK13543 165 YANLDLEgitlvnrmISAHLRGG 187
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 7-219 1.35e-23

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 97.45  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLE--PVNDGRIYVNKQDITSSPPQQRE---IGMVF 81
Cdd:COG0396    4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAragIFLAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTER--NIAFGLKMQKVPENEQ-RKSVAEVIELVGLKGK--EQHLPHQLSGGQRQRVALARALVMKPRILL 156
Cdd:COG0396   84 QYPVEIPGVSVSNflRTALNARRGEELSAREfLKLLKEKMKELGLDEDflDRYVNEGFSGGEKKRNEILQMLLLEPKLAI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEeamLMS----DRIFLMNKGEIVQSDTAE 219
Cdd:COG0396  164 LDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQR---ILDyikpDFVHVLVDGRIVKSGGKE 226
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 7-217 2.63e-23

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: 95.56  E-value: 2.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAA--TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQ 82
Cdd:cd03369   10 ENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTIIPQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFpnMTTERNiafglkmQKVPENEQrkSVAEVIElvGLKGKEQHLphQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:cd03369   90 DPTLF--SGTIRS-------NLDPFDEY--SDEEIYG--ALRVSEGGL--NLSQGQRQLLCLARALLKRPRVLVLDEATA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 163 ALDAQIRKHLRQQIRQiqrELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDT 217
Cdd:cd03369  155 SIDYATDALIQKTIRE---EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 29-233 3.40e-23

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 100.51  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   29 GEFITLLGPSGCGKSTLLRCLAGLEPVN---DGRIYVNKQDITSspPQQREI-GMVFQSYALFPNMTTERNIAFG--LKM 102
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA--KEMRAIsAYVQQDDLFIPTLTVREHLMFQahLRM 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  103 QK-VPENEQRKSVAEVIELVGLKgKEQHL----PHQ---LSGGQRQRVALARALVMKPRILLLDEPLSALDA-------Q 167
Cdd:TIGR00955 129 PRrVTKKEKRERVDEVLQALGLR-KCANTrigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSfmaysvvQ 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658  168 IRKHLRQQIRqiqrelnltTIFVTHDQEEAMLMS--DRIFLMNKGEIVQSDTAENL--------YTQPANEFVARF 233
Cdd:TIGR00955 208 VLKGLAQKGK---------TIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENYNPADF 274
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
4-221 6.02e-23

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 99.65  E-value: 6.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAAT-PVFSGLNFSVSKGEFITLLGPSGCGKSTLLrclAGLEPVND---GRIYVNKQDITSSPPQ--QREI 77
Cdd:PRK13657 335 VEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRVFDpqsGRILIDGTDIRTVTRAslRRNI 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 GMVFQSYALFpNMTTERNIAFG---LKMQKVPENEQRKSVAEVIE--------LVGLKGKeqhlphQLSGGQRQRVALAR 146
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIRVGrpdATDEEMRAAAERAQAHDFIErkpdgydtVVGERGR------QLSGGERQRLAIAR 484

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 147 ALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTH---DQEEAmlmsDRIFLMNKGEIVQSDTAENL 221
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHrlsTVRNA----DRILVFDNGRVVESGSFDEL 556
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 17-210 6.37e-23

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: 95.09  E-value: 6.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIY-VNKQDITSSPPQQREIGMVFQSYA----LFPNMT 91
Cdd:cd03290   15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwSNKNESEPSFEATRSRNRYSVAYAaqkpWLLNAT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGlkmqkVPENEQRKSVaeVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:cd03290   95 VEENITFG-----SPFNKQRYKA--VTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDP 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738468658 161 LSALDAQIRKHLRQQ-IRQIQRELNLTTIFVTHdQEEAMLMSDRIFLMNKG 210
Cdd:cd03290  168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 7-213 8.66e-23

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 98.95  E-value: 8.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLT-KSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ-REIGMVF--- 81
Cdd:COG3845  261 ENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYipe 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 --QSYALFPNMTTERNIAFG------------LKMQKVpeneqRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALAR 146
Cdd:COG3845  341 drLGRGLVPDMSVAENLILGryrrppfsrggfLDRKAI-----RAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILAR 415

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 147 ALVMKPRILLLDEPLSALD----AQIRKHLRQqirqiQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:COG3845  416 ELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 4-217 2.60e-22

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: 98.55  E-value: 2.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658     4 VIAENLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMV 80
Cdd:TIGR01257  929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQsLGMC 1008

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    81 FQSYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658   161 LSALDAQIRKHLRQQIrqIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDT 217
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
23-225 2.72e-22

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 95.74  E-value: 2.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEP----VNDGRIYVNKQDITSSPPQQR------EIGMVFQ--SYALFPNM 90
Cdd:COG4170   27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPSA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  91 TTERNIafglkMQKVPENE------QRK--SVAEVIEL---VGLKGKEQHL---PHQLSGGQRQRVALARALVMKPRILL 156
Cdd:COG4170  107 KIGDQL-----IEAIPSWTfkgkwwQRFkwRKKRAIELlhrVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQPRLLI 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 157 LDEPLSALD----AQIRKhLRQQIRQIQrelNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:COG4170  182 ADEPTNAMEsttqAQIFR-LLARLNQLQ---GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 8-221 3.98e-22

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: 96.82  E-value: 3.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN--DGRIYVNKQDITSSPPQQRE---IGMVFQ 82
Cdd:TIGR02633   6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTEragIVIIHQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   83 SYALFPNMTTERNIAFG----LKMQKVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLL 157
Cdd:TIGR02633  86 ELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLIL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658  158 DEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 16-215 5.17e-22

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: 91.22  E-value: 5.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQRE-IGMVFQSYALFPnmTTER 94
Cdd:cd03247   15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQRPYLFD--TTLR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NiafglkmqkvpeneqrksvaevielvglkgkeqHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDaqiRKHLRQ 174
Cdd:cd03247   93 N---------------------------------NLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD---PITERQ 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 738468658 175 QIRQIQREL-NLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:cd03247  137 LLSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQ 177
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 19-215 9.39e-22

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 95.89  E-value: 9.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  19 FSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR-EIGMVF-----QSYALFPNMTT 92
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPL 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  93 ERNIAfGLKMQKVPENEQRKSVAEVIE----LVGLK--GKEQHLpHQLSGGQRQRVALARALVMKPRILLLDEPLSALDA 166
Cdd:PRK15439 359 AWNVC-ALTHNRRGFWIKPARENAVLEryrrALNIKfnHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738468658 167 QIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 6-255 1.36e-21

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 92.07  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSfAATPVFSGLNFSVSKGEFITLLGPSGCGKStlLRCLAGLE--P----VNDGRIYVNKQDITSSPPQQREIGM 79
Cdd:PRK10418   7 LRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilPagvrQTAGRVLLDGKPVAPCALRGRKIAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQS--YALFPNMTTERNIAFGLKMQKVPENEQRksVAEVIELVGLKGKEQHL---PHQLSGGQRQRVALARALVMKPRI 154
Cdd:PRK10418  84 IMQNprSAFNPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 155 LLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEfVARfm 234
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA-VTR-- 238

                        250       260
                 ....*....|....*....|.
gi 738468658 235 ghyNLVSAHNAnsLLGLNLSG 255
Cdd:PRK10418 239 ---SLVSAHLA--LYGMELAS 254
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 8-221 2.22e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 94.61  E-value: 2.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN--DGRIYVNKQDITSSPPQQRE---IGMVFQ 82
Cdd:PRK13549  10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTEragIAIIHQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQK---VPENEQRKSVAEVIELVGLkGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLD 158
Cdd:PRK13549  90 ELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNKQARLLILD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 4-192 2.97e-21

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 88.75  E-value: 2.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLT-KSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVnkqditsspPQQREIGMVFQ 82
Cdd:cd03223    1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 -SYalFPNMTTERNIAFglkmqkvpeneqrksvaevielvglkgkeqhlP--HQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:cd03223   72 rPY--LPLGTLREQLIY--------------------------------PwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117

                        170       180       190
                 ....*....|....*....|....*....|...
gi 738468658 160 PLSALDAQIRKHLRQQIrqiqRELNLTTIFVTH 192
Cdd:cd03223  118 ATSALDEESEDRLYQLL----KELGITVISVGH 146
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 17-212 3.08e-21

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: 95.01  E-value: 3.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQdiTSSPPQQreigmvfqsyALFPNMTTERNI 96
Cdd:TIGR00957  652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ----------AWIQNDSLRENI 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    97 AFGLKMQKvpeneqrKSVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:TIGR00957  720 LFGKALNE-------KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 738468658   166 AQIRKHLRQQIRQIQREL-NLTTIFVTHDQeEAMLMSDRIFLMNKGEI 212
Cdd:TIGR00957  793 AHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKI 839
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
3-215 5.28e-21

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 93.70  E-value: 5.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   3 YVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ---QREIGM 79
Cdd:PRK09700   5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  80 VFQSYALFPNMTTERNIAFGLKMQK-------VPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKP 152
Cdd:PRK09700  85 IYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 153 RILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS 215
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 22-225 8.62e-21

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 89.61  E-value: 8.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPvNDGRIYVNKQDITSSPP------------QQRE-IGM-VFQSYALF 87
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAaelarhraylsqQQTPpFAMpVFQYLTLH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  88 pnmtterniafglKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARA-LVMKPRI------LLLDEP 160
Cdd:PRK03695  94 -------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 161 LSALDAQIRKHLRQQIRQIQReLNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 4-213 2.44e-20

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: 87.32  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN---DGRI-YVNKQ-DITSSPPqQREIG 78
Cdd:cd03233    8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIhYNGIPyKEFAEKY-PGEII 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  79 MVFQSYALFPNMTTERNIAFGLKMQKvpeNEQrksvaevielvgLKGkeqhlphqLSGGQRQRVALARALVMKPRILLLD 158
Cdd:cd03233   87 YVSEEDVHFPTLTVRETLDFALRCKG---NEF------------VRG--------ISGGERKRVSIAEALVSRASVLCWD 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 159 EPLSALDAQIRKHLRQQIRQIQRELNLTTIF-VTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:cd03233  144 NSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 12-212 2.57e-20

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 91.57  E-value: 2.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  12 SFAATPVfsglNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFPN 89
Cdd:PRK10522 336 GFSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQ 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTerniafglkmqkvPENEQRKS--VAEVIELVGLKGKEQHLPH-----QLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PRK10522 412 LLG-------------PEGKPANPalVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAA 478

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 163 ALDAQIRKHLRQQIRQIQRELNLTTIFVTHDqEEAMLMSDRIFLMNKGEI 212
Cdd:PRK10522 479 DQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 23-212 2.89e-20

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 91.22  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQR-EIGMVFQSY-----ALFPNMTTERNI 96
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSVKENM 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  97 A------FGLKMQKVPENEQRKSVAEVIELVGLK--GKEQHLpHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQI 168
Cdd:PRK10762 352 SltalryFSRAGGSLKHADEQQAVSDFIRLFNIKtpSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738468658 169 RKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PRK10762 431 KKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
14-225 4.80e-20

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 90.93  E-value: 4.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  14 AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDItsspPQQR------EIGMVFQSYALF 87
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQldswrsRLAVVSQTPFLF 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  88 PNmTTERNIAFGLKMQKVPENEQRKSVAEVIE-----------LVGLKGKeqhlphQLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK10789 402 SD-TVANNIALGRPDATQQEIEHVARLASVHDdilrlpqgydtEVGERGV------MLSGGQKQRISIARALLLNAEILI 474

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658 157 LDEPLSALDAQIRKHLRQQIRQIQRElnlTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQP 225
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
PLN03211 PLN03211
ABC transporter G-25; Provisional
 10-166 7.80e-20

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 90.32  E-value: 7.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  10 TKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVND--GRIYVNKQDITSspPQQREIGMVFQSYALF 87
Cdd:PLN03211  75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  88 PNMTTERNIAFG--LKMQKVPENEQRKSVAE-VIELVGLKGKEQHLPHQ-----LSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PLN03211 153 PHLTVRETLVFCslLRLPKSLTKQEKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232


                 ....*..
gi 738468658 160 PLSALDA 166
Cdd:PLN03211 233 PTSGLDA 239
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
22-224 7.09e-19

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 87.15  E-value: 7.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-SSPPQQREIGMVF-----QSYALFPNMTTERN 95
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYitesrRDNGFFPNFSIAQN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  96 IA---------FGLKMQKVPENEQRKSVAEVIELVGLK--GKEQHLpHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:PRK09700 362 MAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKchSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 165 DAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 16-214 1.38e-18

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 83.08  E-value: 1.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPpqqreigmvfqsyalfpnmttERN 95
Cdd:COG2401   43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR---------------------EAS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  96 IafglkMQKVPENEQRKSVAEVIELVGLKGKEQHL--PHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLR 173
Cdd:COG2401  102 L-----IDAIGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 738468658 174 QQIRQIQRELNLTTIFVTHDQE-EAMLMSDRIFLMNKGEIVQ 214
Cdd:COG2401  177 RNLQKLARRAGITLVVATHHYDvIDDLQPDLLIFVGYGGVPE 218
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
16-224 1.94e-18

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 86.23  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  16 TPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT----SSPPQQreIGMVFQSYALFpNMT 91
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytlASLRNQ--VALVSQNVHLF-NDT 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  92 TERNIAFGLKMQKVPEN-EQRKSVAEVIELVglkgkeQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PRK11176 433 IANNIAYARTEQYSREQiEEAARMAYAMDFI------NKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDE 506

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 160 PLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHDQ---EEAmlmsDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQK--NRTSLVIAHRLstiEKA----DEILVVEDGEIVERGTHAELLAQ 568
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
17-224 3.19e-18

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 85.54  E-value: 3.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQ-----SYALFPN 89
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQdpvvlADTFLAN 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  90 MTTERNIAfglkmqkvpeNEQRKSVAEVIELVGL-----KGKEQHLPHQ---LSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:PRK10790 435 VTLGRDIS----------EEQVWQALETVQLAELarslpDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEAT 504

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 162 SALDAQIRKHLRQQIRQIQRElnlTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
PLN03232 PLN03232
ABC transporter C family member; Provisional
 17-229 3.77e-18

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 85.80  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS--PPQQREIGMVFQSYALFPNMT--- 91
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFglTDLRRVLSIIPQSPVLFSGTVrfn 1329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   92 ----TERNIAfglkmqKVPENEQRKSVAEVIEL--VGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:PLN03232 1330 idpfSEHNDA------DLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658  166 AQIRKHLRQQIRQiqrELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEF 229
Cdd:PLN03232 1404 VRTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 25-204 4.05e-18

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: 82.46  E-value: 4.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  25 SVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDItSSPPQQREigmvfqsyALFPnmTTERNIAFGlKMQK 104
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIK--------ADYE--GTVRDLLSS-ITKD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 105 VPENEQRKSvaEVIELVGLKG-KEQHLPhQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQREL 183
Cdd:cd03237   89 FYTHPYFKT--EIAKPLQIEQiLDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165

                        170       180
                 ....*....|....*....|.
gi 738468658 184 NLTTIFVTHDQEEAMLMSDRI 204
Cdd:cd03237  166 EKTAFVVEHDIIMIDYLADRL 186
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 1-213 4.47e-18

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 85.00  E-value: 4.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   1 MSYVIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNkQDITSSPPQQ---REI 77
Cdd:PRK11147   1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQdppRNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 -GMVF---------------QSYALFPNMTT---ERNIAfglKMQKVPEN---------EQRksVAEVIELVGLKGkEQH 129
Cdd:PRK11147  80 eGTVYdfvaegieeqaeylkRYHDISHLVETdpsEKNLN---ELAKLQEQldhhnlwqlENR--INEVLAQLGLDP-DAA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 130 LpHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELnlttIFVTHDQEEAMLMSDRIFLMNK 209
Cdd:PRK11147 154 L-SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRIVDLDR 228


                 ....
gi 738468658 210 GEIV 213
Cdd:PRK11147 229 GKLV 232
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 17-236 4.93e-18

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: 85.18  E-value: 4.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFPNMTTEr 94
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYLPQEPYIFSGSILE- 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   95 NIAFGLKmqkvpENEQRKSVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:TIGR01193 567 NLLLGAK-----ENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDESTSN 641

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658  164 LDAQIRKHLRQQIRQIQRElnlTTIFVTHDQEEAMlMSDRIFLMNKGEIVQSDTAENLYTQpaNEFVARFMGH 236
Cdd:TIGR01193 642 LDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLIHN 708
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 4-197 6.36e-18

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 84.30  E-value: 6.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEP---VND----GR-------IYvnkqDIts 69
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgySNDltlfGRrrgsgetIW----DI-- 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  70 sppqQREIGMVFQSYAL-FPNMTTERNI-------AFGLkMQKVPEnEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQrQ 140
Cdd:PRK10938 335 ----KKHIGYVSSSLHLdYRVSTSVRNVilsgffdSIGI-YQAVSD-RQQKLAQQWLDILGIDKRTADAPfHSLSWGQ-Q 407

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 141 RVAL-ARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEA 197
Cdd:PRK10938 408 RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
8-292 9.29e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 83.81  E-value: 9.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQditsspPQQ----RE-----IG 78
Cdd:PRK11288   9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRfastTAalaagVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  79 MVFQSYALFPNMTTERNIAFGLKMQK---VPENEQRKSVAEVIELVGLK-GKEQHLPHqLSGGQRQRVALARALVMKPRI 154
Cdd:PRK11288  83 IIYQELHLVPEMTVAENLYLGQLPHKggiVNRRLLNYEAREQLEHLGVDiDPDTPLKY-LSIGQRQMVEIAKALARNARV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 155 LLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQS-DTAENLytqpanefvarf 233
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV------------ 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 234 mGHYNLVSAhnansLLGLNLSGIVAIRPESI-YVR-EAGRQYGEHISHPVSGTIRDSQLLG 292
Cdd:PRK11288 229 -DRDQLVQA-----MVGREIGDIYGYRPRPLgEVRlRLDGLKGPGLREPISFSVRAGEIVG 283
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 4-165 9.72e-18

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: 83.83  E-value: 9.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    4 VI-AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREigmvfq 82
Cdd:TIGR03719 322 VIeAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD------ 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   83 syALFPNMTTERNIAFGLKMQKVpENEQRKSVAEViELVGLKGKEQH-LPHQLSGGQRQRVALARALVMKPRILLLDEPL 161
Cdd:TIGR03719 396 --ALDPNKTVWEEISGGLDIIKL-GKREIPSRAYV-GRFNFKGSDQQkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471


                  ....
gi 738468658  162 SALD 165
Cdd:TIGR03719 472 NDLD 475
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 9-210 3.27e-17

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: 83.14  E-value: 3.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658     9 LTKSFAAT--PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYV-NKQDITSSPPQQREIGMVFQSYA 85
Cdd:TIGR01257 1943 LTKVYSGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMGYCPQFDA 2022

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    86 LFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 738468658   166 AQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKG 210
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 22-224 3.31e-17

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: 82.18  E-value: 3.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEP-VNDGRIYVNKQDITSSPPQQ---REIGMVFQS---YALFPNMTTER 94
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGK 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   95 NIAFGL-----KMQKVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQI 168
Cdd:TIGR02633 359 NITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658  169 RKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEiVQSDTAENLYTQ 224
Cdd:TIGR02633 439 KYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK-LKGDFVNHALTQ 492
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 26-210 5.70e-17

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 82.08  E-value: 5.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    26 VSKGEFITLLGPSGCGKSTLLRCLAGLEP---VNDGRIYVNKQDITSSppQQREIGMVFQSYALFPNMTTERNIAFGLKM 102
Cdd:TIGR00956  786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSS--FQRSIGYVQQQDLHLPTSTVRESLRFSAYL 863

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   103 ---QKVPENEQRKSVAEVIEL----------VGLKGKeqhlphQLSGGQRQRVALARALVMKPRILL-LDEPLSALDAQ- 167
Cdd:TIGR00956  864 rqpKSVSKSEKMEYVEEVIKLlemesyadavVGVPGE------GLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQt 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 738468658   168 ---IRKHLRQQIRQIQrelnltTIFVTHDQEEAMLMS--DRIFLMNKG 210
Cdd:TIGR00956  938 awsICKLMRKLADHGQ------AILCTIHQPSAILFEefDRLLLLQKG 979
PLN03130 PLN03130
ABC transporter C family member; Provisional
 12-221 1.41e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 80.94  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   12 SFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPVNDGRIYVnkqditssppqQREIGMVFQSYALFpNM 90
Cdd:PLN03130  626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI-----------RGTVAYVPQVSWIF-NA 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   91 TTERNIAFGLKMQkvPENEQRksvaeVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PLN03130  694 TVRDNILFGSPFD--PERYER-----AIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDD 766

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658  160 PLSALDAqirkHLRQQI--RQIQREL-NLTTIFVThDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:PLN03130  767 PLSALDA----HVGRQVfdKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
hmuV PRK13547
heme ABC transporter ATP-binding protein;
6-213 2.53e-16

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 77.94  E-value: 2.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG--LEPVND------GRIYVNKQDITSSPPQQrei 77
Cdd:PRK13547   4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAAIDAPR--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  78 gmVFQSYALFPNmTTERNIAFGLK----MQKVP--------ENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALA 145
Cdd:PRK13547  81 --LARLRAVLPQ-AAQPAFAFSAReivlLGRYPharragalTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 146 RAL---------VMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 7-219 1.35e-15

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 75.45  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGlEP---VNDGRIYVNKQDITSSPPQQRE---IGMV 80
Cdd:CHL00131  11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESILDLEPEERAhlgIFLA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTER--NIAFG--LKMQKVPEN---EQRKSVAEVIELVGLKGK--EQHLPHQLSGGQRQRVALARALVMK 151
Cdd:CHL00131  90 FQYPIEIPGVSNADflRLAYNskRKFQGLPELdplEFLEIINEKLKLVGMDPSflSRNVNEGFSGGEKKRNEILQMALLD 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 152 PRILLLDEPLSALDAQIRKHLRQQIRQIQRELNlTTIFVTHDQEeamLMS----DRIFLMNKGEIVQSDTAE 219
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQR---LLDyikpDYVHVMQNGKIIKTGDAE 237
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 17-221 1.41e-15

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 78.15  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQ----DITSSPPQQ----REIGMV-------- 80
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNehtnDMTNEQDYQgdeeQNVGMKnvnefslt 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   81 -----FQSYALFPN----------------------------------MTTERNIAFGlkmqkvPENEQRKSVAEVIELV 121
Cdd:PTZ00265 1262 keggsGEDSTVFKNsgkilldgvdicdynlkdlrnlfsivsqepmlfnMSIYENIKFG------KEDATREDVKRACKFA 1335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  122 GLKGKEQHLPHQ-----------LSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFV 190
Cdd:PTZ00265 1336 AIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 738468658  191 THdQEEAMLMSDRIFLMNK----GEIVQSD-TAENL 221
Cdd:PTZ00265 1416 AH-RIASIKRSDKIVVFNNpdrtGSFVQAHgTHEEL 1450
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 26-210 1.54e-15

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: 73.82  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  26 VSKGEFITLLGPSGCGKSTLLRCLAGLEP--VNDGRIYVNKQDITSSppQQREIGMVFQSYALFPNMTterniafglkmq 103
Cdd:cd03232   30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN--FQRSTGYVEQQDVHSPNLT------------ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 104 kvpeneqrksVAEVIELVG-LKGkeqhlphqLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRE 182
Cdd:cd03232   96 ----------VREALRFSAlLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 738468658 183 LNltTIFVTHDQEEAMLMS--DRIFLMNKG 210
Cdd:cd03232  158 GQ--AILCTIHQPSASIFEkfDRLLLLKRG 185
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 8-224 1.55e-15

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 75.66  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLagLEPVN-DGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:cd03289    7 DLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF--LRLLNtEGDIQIDGVSWNSVPLQKwrKAFGVIPQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPnmtterniafGLKMQKVPENEQRK--SVAEVIELVGLKGKEQHLPHQL-----------SGGQRQRVALARALV 149
Cdd:cd03289   85 KVFIFS----------GTFRKNLDPYGKWSdeEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQiqrELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:cd03289  155 SKAKILLLDEPSAHLDPITYQVIRKTLKQ---AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
8-225 1.96e-15

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 75.99  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSF--AATPV--FSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEP----VNDGRIYVNKQDITSSPPQQRE--- 76
Cdd:PRK15093   8 NLTIEFktSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRklv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 ---IGMVFQ--SYALFPNMTTERNIafglkMQKVPE-----------NEQRKSVAEVIELVGLKGKE---QHLPHQLSGG 137
Cdd:PRK15093  88 ghnVSMIFQepQSCLDPSERVGRQL-----MQNIPGwtykgrwwqrfGWRKRRAIELLHRVGIKDHKdamRSFPYELTEG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 138 QRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDT 217
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242


                 ....*...
gi 738468658 218 AENLYTQP 225
Cdd:PRK15093 243 SKELVTTP 250
GguA NF040905
sugar ABC transporter ATP-binding protein;
8-204 2.11e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 76.75  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVN--DGRIYVNKQ-----DITSSppQQREIGMV 80
Cdd:NF040905   6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEvcrfkDIRDS--EALGIVII 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  81 FQSYALFPNMTTERNIAFGlkmqkvpeNEQRKS-----------VAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALV 149
Cdd:NF040905  84 HQELALIPYLSIAENIFLG--------NERAKRgvidwnetnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRI 204
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSI 209
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 23-212 2.34e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 76.89  E-value: 2.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEP-VNDGRIYVNKQDITSSPPQQ---REIGMVFQS---YALFPNMTTERN 95
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  96 IAFGL-----KMQKVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLSALD---- 165
Cdd:PRK13549 362 ITLAAldrftGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgak 441

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738468658 166 AQIRKHLRQQIRQiqrelNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PRK13549 442 YEIYKLINQLVQQ-----GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 8-165 2.67e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 73.45  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS-PPQQREIGMVFQSYAL 86
Cdd:PRK13540   6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlCTYQKQLCFVGHRSGI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  87 FPNMTTERNIAFGLKMQkvpeneqrKSVAEVIELVGLKGKEQHLPHQ---LSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:PRK13540  86 NPYLTLRENCLYDIHFS--------PGAVGITELCRLFSLEHLIDYPcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157


                 ..
gi 738468658 164 LD 165
Cdd:PRK13540 158 LD 159
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
24-223 3.39e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 74.53  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  24 FSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDiTSSPPQQREIGMVFQSYAL---FPnMTTERNIAFG- 99
Cdd:PRK15056  28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYVPQSEEVdwsFP-VLVEDVVMMGr 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 100 ---LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQI 176
Cdd:PRK15056 106 yghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738468658 177 RQIQRElNLTTIFVTHDQEEAMLMSDRIfLMNKGEIVQSDTAENLYT 223
Cdd:PRK15056 186 RELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFT 230
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 12-249 5.21e-15

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 76.10  E-value: 5.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    12 SFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRIYvNKQDITSSPpqqreigmvfQSYALFPNm 90
Cdd:TIGR01271  435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP-SEGKIK-HSGRISFSP----------QTSWIMPG- 501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    91 TTERNIAFGLKMqkvpeNEQRKSvaEVIELVGLKGKEQHLPHQ-----------LSGGQRQRVALARALVMKPRILLLDE 159
Cdd:TIGR01271  502 TIKDNIIFGLSY-----DEYRYT--SVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   160 PLSALDAQIRKHLRQQIrQIQRELNLTTIFVThDQEEAMLMSDRIFLMNKGEIVQSDTAENLYT-QPanEFVARFMG--H 236
Cdd:TIGR01271  575 PFTHLDVVTEKEIFESC-LCKLMSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAkRP--DFSSLLLGleA 650

                          250
                   ....*....|...
gi 738468658   237 YNLVSAHNANSLL 249
Cdd:TIGR01271  651 FDNFSAERRNSIL 663
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 4-165 5.30e-15

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 75.93  E-value: 5.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VI-AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRI---------YVNkqditssppQ 73
Cdd:PRK11819 324 VIeAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkigetvklaYVD---------Q 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  74 QREigmvfqsyALFPNMTTERNIAFGLKMQKVPENE--QRKSVAEvielVGLKGKEQHLP-HQLSGGQRQRVALARALVM 150
Cdd:PRK11819 395 SRD--------ALDPNKTVWEEISGGLDIIKVGNREipSRAYVGR----FNFKGGDQQKKvGVLSGGERNRLHLAKTLKQ 462

                        170
                 ....*....|....*
gi 738468658 151 KPRILLLDEPLSALD 165
Cdd:PRK11819 463 GGNVLLLDEPTNDLD 477
PLN03130 PLN03130
ABC transporter C family member; Provisional
 17-221 1.19e-14

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 75.16  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSS--PPQQREIGMVFQSYALFPNmtter 94
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDLRKVLGIIPQAPVLFSG----- 1327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   95 NIAFGLKmqkvPENE----------QRKSVAEVIEL--VGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PLN03130 1328 TVRFNLD----PFNEhndadlweslERAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658  163 AL----DAQIRKHLRQQIRQ-----IQRELNltTIfvthdqeeamLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:PLN03130 1404 AVdvrtDALIQKTIREEFKSctmliIAHRLN--TI----------IDCDRILVLDAGRVVEFDTPENL 1459
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 8-208 1.87e-14

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: 74.20  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    8 NLTKSFAAT-PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYvnkqditssPPQQREIGMVFQSYAL 86
Cdd:TIGR03719   9 RVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPGIKVGYLPQEPQL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   87 FPNMTTERNIAFGLK----------------------MQKVPEnEQRKsVAEVIELVGLKGKEQHL---------P---- 131
Cdd:TIGR03719  80 DPTKTVRENVEEGVAeikdaldrfneisakyaepdadFDKLAA-EQAE-LQEIIDAADAWDLDSQLeiamdalrcPpwda 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  132 --HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ----IRKHLrqqirqiqRELNLTTIFVTHdqeeamlmsDRIF 205
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHL--------QEYPGTVVAVTH---------DRYF 220


                  ...
gi 738468658  206 LMN 208
Cdd:TIGR03719 221 LDN 223
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 12-249 2.48e-14

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: 72.20  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  12 SFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRIYvNKQDITSSPpqqreigmvfQSYALFPNm 90
Cdd:cd03291   46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEP-SEGKIK-HSGRISFSS----------QFSWIMPG- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  91 TTERNIAFGlkmqkVPENEQR-KSVaevIELVGLKGKEQHLPHQ-----------LSGGQRQRVALARALVMKPRILLLD 158
Cdd:cd03291  113 TIKENIIFG-----VSYDEYRyKSV---VKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 159 EPLSALDAQIRKHLRQQIrQIQRELNLTTIFVTHDQEEaMLMSDRIFLMNKGEIVQSDTAENLYTQPAnEFVARFMG--H 236
Cdd:cd03291  185 SPFGYLDVFTEKEIFESC-VCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRP-DFSSKLMGydT 261

                        250
                 ....*....|...
gi 738468658 237 YNLVSAHNANSLL 249
Cdd:cd03291  262 FDQFSAERRNSIL 274
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 7-247 2.85e-14

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 74.18  E-value: 2.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658     7 ENLTKSF--AATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVnDGRIYVNKQDITSSPPQQ--REIGMVFQ 82
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTwrKAFGVIPQ 1299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    83 SYALFPNmTTERNIAfglkmqkvP-ENEQRKSVAEVIELVGLKGKEQHLPHQL-----------SGGQRQRVALARALVM 150
Cdd:TIGR01271 1300 KVFIFSG-TFRKNLD--------PyEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILS 1370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   151 KPRILLLDEPLSALDAQIRKHLRQQIRQIQRelNLTTIFVTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPAneFV 230
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEH-RVEALLECQQFLVIEGSSVKQYDSIQKLLNETS--LF 1445

                          250       260
                   ....*....|....*....|
gi 738468658   231 ARFMGHYN---LVSAHNANS 247
Cdd:TIGR01271 1446 KQAMSAADrlkLFPLHRRNS 1465
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 7-221 2.91e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 73.23  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDI---TSSPPQQREIGMVFQS 83
Cdd:PRK10982   2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFG---LKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEP 160
Cdd:PRK10982  82 LNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 161 LSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENL 221
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
PTZ00243 PTZ00243
ABC transporter; Provisional
 22-176 4.61e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 73.27  E-value: 4.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVnkqditssppqQREIGMVFQSyALFPNMTTERNIAFglk 101
Cdd:PTZ00243  679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQ-AWIMNATVRGNILF--- 743

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  102 mqKVPENEQRksVAEVIELVGLKGKEQHLPH-----------QLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRK 170
Cdd:PTZ00243  744 --FDEEDAAR--LADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819


                  ....*.
gi 738468658  171 HLRQQI 176
Cdd:PTZ00243  820 RVVEEC 825
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-195 4.66e-14

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 73.00  E-value: 4.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNkqditssppQQREIGMVFQ- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------ENANIGYYAQd 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPN-MTTERNIAfglKMQKVPENEQ----------------RKSVaevielvglkgkeqhlpHQLSGGQRQRVALA 145
Cdd:PRK15064 391 HAYDFENdLTLFDWMS---QWRQEGDDEQavrgtlgrllfsqddiKKSV-----------------KVLSGGEKGRMLFG 450

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738468658 146 RALVMKPRILLLDEPLSALDAqirkhlrQQIRQIQRELNL---TTIFVTHDQE 195
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDM-------ESIESLNMALEKyegTLIFVSHDRE 496
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 17-236 5.43e-14

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: 70.71  E-value: 5.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFPNmtter 94
Cdd:cd03288   35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSIILQDPILFSG----- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 NIAFGLKMQKVPENEQrksVAEVIELVGLKGKEQHLPHQL-----------SGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:cd03288  110 SIRFNLDPECKCTDDR---LWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATAS 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738468658 164 LDAQIRKHLRQQIRQIQRELNLTTIfvTHdQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQPANEFVARFMGH 236
Cdd:cd03288  187 IDMATENILQKVVMTAFADRTVVTI--AH-RVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 28-211 6.96e-14

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: 68.17  E-value: 6.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    28 KGEFITLLGPSGCGKSTLLRCLAG-LEPVNDGRIYVNKQDITSSPPQQREIGMVFQSYalfpnmtterniafglkmqkvp 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   107 eneqrksvaevielvglkgkeqhlpHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIR-----QIQR 181
Cdd:smart00382  59 -------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKS 113

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 738468658   182 ELNLTTIFVTHDQE-----EAMLMSDRIFLMNKGE 211
Cdd:smart00382 114 EKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 18-228 7.71e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 72.75  E-value: 7.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNK----QDITSSPPQQReIGMVFQSYALFPNmTTE 93
Cdd:PTZ00265  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSK-IGVVSQDPLLFSN-SIK 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   94 RNIAFGL---------------------------------------------------KMQKVPENEQRKSVAEVIELVG 122
Cdd:PTZ00265  478 NNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIKDSEVVDVSKKVL 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  123 LKGKEQHLP-----------HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNLTTIFVT 191
Cdd:PTZ00265  558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 738468658  192 HdQEEAMLMSDRIFLMN---KGEIVQSDTAENLYTQPANE 228
Cdd:PTZ00265  638 H-RLSTIRYANTIFVLSnreRGSTVDVDIIGEDPTKDNKE 676
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 7-219 8.88e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 71.96  E-value: 8.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP---QQREIGMVFQS 83
Cdd:PRK10762   8 KGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGL----KMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDE 159
Cdd:PRK10762  88 LNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 160 PLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQEEAMLMSDRIFLMNKGE-IVQSDTAE 219
Cdd:PRK10762 168 PTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIAEREVAD 227
PLN03232 PLN03232
ABC transporter C family member; Provisional
 17-222 1.41e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.93  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   17 PVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPVNDGRIyvnkqDITSSPPQQREIGMVFqsyalfpNMTTERN 95
Cdd:PLN03232  631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSV-----VIRGSVAYVPQVSWIF-------NATVREN 698

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   96 IAFGLKMQkvPENEQRksvaeVIELVGLKGKEQHLPHQ-----------LSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:PLN03232  699 ILFGSDFE--SERYWR-----AIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  165 DAqirkHLRQQIRQ--IQRELNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLY 222
Cdd:PLN03232  772 DA----HVAHQVFDscMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 18-224 5.03e-13

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: 70.36  E-value: 5.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQ--QREIGMVFQSYALFPNmttern 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdlRFKITIIPQDPVLFSG------ 1374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    96 iafGLKMQKVPENE-QRKSVAEVIELVGLKGKEQHLP----HQ-------LSGGQRQRVALARALVMKPRILLLDEPLSA 163
Cdd:TIGR00957 1375 ---SLRMNLDPFSQySDEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1451

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658   164 LDAQIRKHLRQQIRQiQRElNLTTIFVTHDQEEAMLMSdRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:TIGR00957 1452 VDLETDNLIQSTIRT-QFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 22-192 6.69e-13

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 69.39  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   22 LNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIGM-VFQSYALFPnMTTERNIAFGL 100
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSSEDMKRRGL 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  101 KMQKVpeneqrKSVAEVIELVGLKGKE------QHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIrkhlRQ 174
Cdd:TIGR00954 550 SDKDL------EQILDNVQLTHILEREggwsavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV----EG 619

                         170
                  ....*....|....*...
gi 738468658  175 QIRQIQRELNLTTIFVTH 192
Cdd:TIGR00954 620 YMYRLCREFGITLFSVSH 637
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 29-204 1.89e-12

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: 66.24  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  29 GEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIyvnkqditSSPPQQREI-----GMVFQSY-----------ALFPNMTT 92
Cdd:cd03236   26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEIldefrGSELQNYftkllegdvkvIVKPQYVD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  93 ERNIAF----GLKMQKVPENEQRKSVAEVIELVGLkgKEQHLpHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQI 168
Cdd:cd03236   98 LIPKAVkgkvGELLKKKDERGKLDELVDQLELRHV--LDRNI-DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 738468658 169 RKHLRQQIRQIQRELNlTTIFVTHDQEEAMLMSDRI 204
Cdd:cd03236  175 RLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYI 209
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 26-204 1.91e-12

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: 64.90  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  26 VSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPpqqreigmvfqsyalfpnmtterniafglkmQKV 105
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------------------------QYI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 106 peneqrksvaevielvglkgkeqhlphQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNL 185
Cdd:cd03222   71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123

                        170
                 ....*....|....*....
gi 738468658 186 TTIFVTHDQEEAMLMSDRI 204
Cdd:cd03222  124 TALVVEHDLAVLDYLSDRI 142
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-204 3.02e-12

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 67.53  E-value: 3.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  26 VSKGEFITLLGPSGCGKSTLLRCLAG-LEPVN-----DGRIYVNKQDITSSPPQQ-----REIGMVFQSYALFPNmtter 94
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDEgevdpELKISYKPQYIKPDYDGTvedllRSITDDLGSSYYKSE----- 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 nIAFGLKMQKVPEneqrKSVAEvielvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQ 174
Cdd:PRK13409 437 -IIKPLQLERLLD----KNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494

                        170       180       190
                 ....*....|....*....|....*....|..
gi 738468658 175 QIRQIQRELNLTTIFVTHDQeeAM--LMSDRI 204
Cdd:PRK13409 495 AIRRIAEEREATALVVDHDI--YMidYISDRL 524
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 32-208 5.72e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 66.68  E-value: 5.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  32 ITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKqDITssppqqreIGMVFQSYALFPNMTTERNI--AFGLKMQKVPE-N 108
Cdd:PRK11819  36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-GIK--------VGYLPQEPQLDPEKTVRENVeeGVAEVKAALDRfN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 109 EQRKSVAEVI----ELVGLKGKEQ----------------------HLPH------QLSGGQRQRVALARALVMKPRILL 156
Cdd:PRK11819 107 EIYAAYAEPDadfdALAAEQGELQeiidaadawdldsqleiamdalRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLL 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 157 LDEPLSALDAQ----IRKHLrqqirqiqRELNLTTIFVTHdqeeamlmsDRIFLMN 208
Cdd:PRK11819 187 LDEPTNHLDAEsvawLEQFL--------HDYPGTVVAVTH---------DRYFLDN 225
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
23-213 6.70e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 66.09  E-value: 6.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT-SSPPQQREIGMVF-----QSYALFPNMTTERNI 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLcpedrKAEGIIPVHSVADNI 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  97 AFGLKMQKVP-----ENEQRKSVAEV-IELVGLK--GKEQhLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQI 168
Cdd:PRK11288 353 NISARRHHLRagcliNNRWEAENADRfIRSLNIKtpSREQ-LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738468658 169 rkhlRQQIRQIQREL---NLTTIFVTHDQEEAMLMSDRIFLMNKGEIV 213
Cdd:PRK11288 432 ----KHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 6-195 8.41e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 66.13  E-value: 8.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   6 AENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRIYV-NKQDITSSpPQQREigmvfqs 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQA-DSGRIHCgTKLEVAYF-DQHRA------- 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 yALFPNMTTERNIAFGlkMQKVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARaLVMKPRILL-LDEPL 161
Cdd:PRK11147 393 -ELDPEKTVMDNLAEG--KQEVMVNGRPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLAR-LFLKPSNLLiLDEPT 468

                        170       180       190
                 ....*....|....*....|....*....|....
gi 738468658 162 SALDAQIRKHLRQQIRQIQRelnlTTIFVTHDQE 195
Cdd:PRK11147 469 NDLDVETLELLEELLDSYQG----TVLLVSHDRQ 498
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 28-207 2.34e-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: 64.81  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  28 KGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRIyvnkqditSSPPQQREI-----GMVFQSYalFpNMTTERNIAFGLK 101
Cdd:COG1245   98 KGKVTGILGPNGIGKSTALKILSGeLKP-NLGDY--------DEEPSWDEVlkrfrGTELQDY--F-KKLANGEIKVAHK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 102 MQ---KVPE------------NEQRKSVAEVIELVGLKGK-EQHLpHQLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:COG1245  166 PQyvdLIPKvfkgtvrellekVDERGKLDELAEKLGLENIlDRDI-SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 738468658 166 aqIRKHLR--QQIRQIQRElNLTTIFVTHDQeeAML--MSDRIFLM 207
Cdd:COG1245  245 --IYQRLNvaRLIRELAEE-GKYVLVVEHDL--AILdyLADYVHIL 285
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 25-204 2.61e-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: 64.42  E-value: 2.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  25 SVSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGriYVNKQDITSSPPQ--QREIGMVFQSY---ALFPNMTT---ERN 95
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGvLKP-DEG--EVDEDLKISYKPQyiSPDYDGTVEEFlrsANTDDFGSsyyKTE 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  96 IAFGLKMQKVPEneqrKSVAEvielvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQ 175
Cdd:COG1245  439 IIKPLGLEKLLD----KNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497

                        170       180       190
                 ....*....|....*....|....*....|...
gi 738468658 176 IRQIQRELNLTTIFVTHDqeeaMLM----SDRI 204
Cdd:COG1245  498 IRRFAENRGKTAMVVDHD----IYLidyiSDRL 526
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 7-215 3.40e-11

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 62.50  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLE--PVNDGRIYVNKQDITSSPPQQRE---IGMVF 81
Cdd:PRK09580   5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegIFMAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  82 QSYALFPNMTTERNIAFGLK-MQKVPENE--QRKSVAEVIElvgLKGKEQHLPHQL---------SGGQRQRVALARALV 149
Cdd:PRK09580  85 QYPVEIPGVSNQFFLQTALNaVRSYRGQEplDRFDFQDLME---EKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 150 MKPRILLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDQE-EAMLMSDRIFLMNKGEIVQS 215
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKS 227
PLN03073 PLN03073
ABC transporter F family; Provisional
 18-212 3.57e-11

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 64.11  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAG-LEPVNDG-------RIYVNKQ------DITSSPpqqreigMVFQS 83
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTvfrsakvRMAVFSQhhvdglDLSSNP-------LLYMM 596

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YAlFPNmtterniafglkmqkVPENEQRKSVAEVielvGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PLN03073 597 RC-FPG---------------VPEQKLRAHLGSF----GVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 738468658 163 ALDAQIRKHLRQQIRQIQRELnlttIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PLN03073 657 HLDLDAVEALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 22-213 5.41e-11

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


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 63.66  E-value: 5.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  22 LNFSVSKGE--FITllGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITsspPQQRE-----IGMVFQSYALFPNMtter 94
Cdd:COG4615  351 IDLTIRRGElvFIV--GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREayrqlFSAVFSDFHLFDRL---- 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  95 niafgLKMQKVPENEQrksVAEVIELVGLKGKEQH-----LPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIR 169
Cdd:COG4615  422 -----LGLDGEADPAR---ARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR 493

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738468658 170 KHLRQQIRQIQRELNLTTIFVTHDQ---EEAmlmsDRIFLMNKGEIV 213
Cdd:COG4615  494 RVFYTELLPELKARGKTVIAISHDDryfDLA----DRVLKMDYGKLV 536
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
9-224 9.48e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.06  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   9 LTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGK------STLLRCLAGLEPVNDGRIYVNKQDITSSPPQQREIgmvfq 82
Cdd:NF000106  19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**rgalpAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPV----- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  83 SYALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:NF000106  94 R*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738468658 163 ALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEIVQSDTAENLYTQ 224
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 29-213 2.19e-10

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.05  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658    29 GEFITLLGPSGCGKSTLLRCLA----GLEPVNDGRIYVNKQDITSSPPQQR-EIGMVFQSYALFPNMTTERNIAFGLKMQ 103
Cdd:TIGR00956   87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAARCK 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   104 K-------VPENEQRKSVAEVIELV-GLK-------GKEqhLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQI 168
Cdd:TIGR00956  167 TpqnrpdgVSREEYAKHIADVYMATyGLShtrntkvGND--FVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 738468658   169 RKHLRQQIRQIQRELNlTTIFVTHDQ--EEAMLMSDRIFLMNKGEIV 213
Cdd:TIGR00956  245 ALEFIRALKTSANILD-TTPLVAIYQcsQDAYELFDKVIVLYEGYQI 290
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-193 9.50e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.82  E-value: 9.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  26 VSKGEFITLLGPSGCGKSTLLRCLAG-LEPvNDGRiyvnkqdiTSSPPQQREI-----GMVFQSYalFPNMTtERNIAFG 99
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILSGeLIP-NLGD--------YEEEPSWDEVlkrfrGTELQNY--FKKLY-NGEIKVV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 100 LKMQ-----------KVPE----NEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSAL 164
Cdd:PRK13409 164 HKPQyvdlipkvfkgKVREllkkVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243

                        170       180       190
                 ....*....|....*....|....*....|...
gi 738468658 165 DaqirkhLRQQIR--QIQREL--NLTTIFVTHD 193
Cdd:PRK13409 244 D------IRQRLNvaRLIRELaeGKYVLVVEHD 270
PLN03140 PLN03140
ABC transporter G family member; Provisional
 29-167 2.64e-09

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 58.70  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   29 GEFITLLGPSGCGKSTLLRCLAGLEP----VNDGRI---------------YVNKQDITSSPPQQREiGMVFQSYALFPN 89
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAGRKTggyiEGDIRIsgfpkkqetfarisgYCEQNDIHSPQVTVRE-SLIYSAFLRLPK 984

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   90 MTTERNiafglKMQKVPEneqrksVAEVIELVGLKGKEQHLP--HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQ 167
Cdd:PLN03140  985 EVSKEE-----KMMFVDE------VMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 32-195 3.97e-09

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 55.69  E-value: 3.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  32 ITLL-GPSGCGKSTLLRC----LAGLEPvNDGRIYVNKQDITSSPPQQREIGMVFQSyALFPNMTTERNIAFGLKMQKVP 106
Cdd:cd03240   24 LTLIvGQNGAGKTTIIEAlkyaLTGELP-PNSKGGAHDPKLIREGEVRAQVKLAFEN-ANGKKYTITRSLAILENVIFCH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 107 ENEQRKSVAEVIElvglkgkeqhlphQLSGGQRQ------RVALARALVMKPRILLLDEPLSALDA-QIRKHLRQQIRQI 179
Cdd:cd03240  102 QGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEER 168

                        170
                 ....*....|....*.
gi 738468658 180 QRELNLTTIFVTHDQE 195
Cdd:cd03240  169 KSQKNFQLIVITHDEE 184
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 8-193 8.22e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.82  E-value: 8.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   8 NLTKSFAATPVFSglNFSV--SKGEFITLLGPSGCGKSTLLRCLAG-LEP--------VNDgRIYVNKQDiTSSPPQQRE 76
Cdd:PRK15064   6 NITMQFGAKPLFE--NISVkfGGGNRYGLIGANGCGKSTFMKILGGdLEPsagnvsldPNE-RLGKLRQD-QFAFEEFTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  77 IGMVFQS--------------YALfPNMTTERNIafglkmqKVPENEQR---------KSVAEVIEL-VGLkGKEQH--L 130
Cdd:PRK15064  82 LDTVIMGhtelwevkqerdriYAL-PEMSEEDGM-------KVADLEVKfaemdgytaEARAGELLLgVGI-PEEQHygL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738468658 131 PHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAqirkhlrQQIRQIQRELN---LTTIFVTHD 193
Cdd:PRK15064 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------NTIRWLEDVLNernSTMIIISHD 211
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-224 3.00e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 55.13  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKSFAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSppQQREigMVFQSYA- 85
Cdd:NF033858   5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRR--AVCPRIAy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  86 --------LFPNMTTERNIAF-----GlkmQKVPENEQRksVAEVIELVGLK-------GKeqhlphqLSGGQRQRVALA 145
Cdd:NF033858  81 mpqglgknLYPTLSVFENLDFfgrlfG---QDAAERRRR--IDELLRATGLApfadrpaGK-------LSGGMKQKLGLC 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 146 RALVMKPRILLLDE------PLSaldaqirkhlRQQ----IRQIQREL-NLTTIFVTHDQEEAMLMsDRIFLMNKGEIVQ 214
Cdd:NF033858 149 CALIHDPDLLILDEpttgvdPLS----------RRQfwelIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217

                        250
                 ....*....|
gi 738468658 215 SDTAENLYTQ 224
Cdd:NF033858 218 TGTPAELLAR 227
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 20-192 6.13e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 54.13  E-value: 6.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  20 SGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIyvnkqDITSSPpqqreiGMVFQSYALFPNMTTERNIAFG 99
Cdd:PRK13545  41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA------ALIAISSGLNGQLTGIENIELK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 100 LKMQKVPENEQRKSVAEVIELVGLkGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQIRQ 178
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADI-GKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188

                        170
                 ....*....|....
gi 738468658 179 IqRELNLTTIFVTH 192
Cdd:PRK13545 189 F-KEQGKTIFFISH 201
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 21-210 1.03e-07

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: 51.17  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  21 GLNFSVSKGEFITLLGPSGCGKSTLlrCLAGLEPVNDGRIyvnkQDITSSPPQQREIgMVFQSYALfpnmtternIAFGL 100
Cdd:cd03238   13 NLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARL----ISFLPKFSRNKLI-FIDQLQFL---------IDVGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 101 kmqkvpeneqrksvaevielvGLKGKEQHLPhQLSGGQRQRVALARALV--MKPRILLLDEPLSALDAQIRKHLRQQIRQ 178
Cdd:cd03238   77 ---------------------GYLTLGQKLS-TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKG 134

                        170       180       190
                 ....*....|....*....|....*....|..
gi 738468658 179 IqRELNLTTIFVTHDqEEAMLMSDRIFLMNKG 210
Cdd:cd03238  135 L-IDLGNTVILIEHN-LDVLSSADWIIDFGPG 164
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 23-182 1.33e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 53.09  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  23 NFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDIT--SSPPQQREIGMVFQsyalfpnmtteRNiafGL 100
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlSFEQLQKLVSDEWQ-----------RN---NT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 101 KMQKVPENEQRKSVAEVI-----------ELVGLKGKEQHLPH---QLSGGQRQRVALARALVMKPRILLLDEPLSALDA 166
Cdd:PRK10938  89 DMLSPGEDDTGRTTAEIIqdevkdparceQLAQQFGITALLDRrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168

                        170
                 ....*....|....*.
gi 738468658 167 QIRKHLRQQIRQIQRE 182
Cdd:PRK10938 169 ASRQQLAELLASLHQS 184
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 257-330 1.74e-07

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 48.00  E-value: 1.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658  257 VAIRPESIYVREAGrqygehisHPVSGTIRDSQLLGNIIRYQVDTGLGALTVDLLNRSSERLFEQGTQLELMFN 330
Cdd:pfam08402   1 LAIRPEKIRLAAAA--------NGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPAPGDRVGLGWD 66
PTZ00243 PTZ00243
ABC transporter; Provisional
 18-169 2.71e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.47  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   18 VFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPPQQ--REIGMVFQSYALFpNMTTERN 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLF-DGTVRQN 1403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   96 IAFGLKmqkvpeneqrKSVAEV---IELVGLKGK-----EQHLPHQLSG------GQRQRVALARALVMKPR-ILLLDEP 160
Cdd:PTZ00243 1404 VDPFLE----------ASSAEVwaaLELVGLRERvasesEGIDSRVLEGgsnysvGQRQLMCMARALLKKGSgFILMDEA 1473

                         170
                  ....*....|...
gi 738468658  161 LS----ALDAQIR 169
Cdd:PTZ00243 1474 TAnidpALDRQIQ 1486
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 7-212 3.15e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.65  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   7 ENLTKsfAATPVFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSPP-------------Q 73
Cdd:PRK10982 254 RNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvteE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  74 QREIGMV------FQSyaLFPNMTTERNiAFGLKmqkvpENEQRKSVAE-VIELVGLKGKEQHLP-HQLSGGQRQRVALA 145
Cdd:PRK10982 332 RRSTGIYayldigFNS--LISNIRNYKN-KVGLL-----DNSRMKSDTQwVIDSMRVKTPGHRTQiGSLSGGNQQKVIIG 403

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738468658 146 RALVMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRElNLTTIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
4-193 3.38e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 50.97  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   4 VIAENLTKSFAAtpvFSGLNFSVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRIYVNKqditssppqqrEIGMVFQS 83
Cdd:PRK13546  28 LIPKHKNKTFFA---LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAIS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  84 YALFPNMTTERNIAFGLKMQKVPENEQRKSVAEVIELVGLkGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PRK13546  94 AGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALS 172

                        170       180       190
                 ....*....|....*....|....*....|.
gi 738468658 163 ALDAQIRKHLRQQIRQIqRELNLTTIFVTHD 193
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEF-KEQNKTIFFVSHN 202
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 27-205 7.12e-07

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 48.51  E-value: 7.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  27 SKGEFITLLGPSGCGKSTLLRCL---AGLEPVNDGRIYVNKQDITSSppqqreigmvfqsyalfpnmtterniafglkmq 103
Cdd:cd03227   19 GEGSLTIITGPNGSGKSTILDAIglaLGGAQSATRRRSGVKAGCIVA--------------------------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 104 kvpeneqrksvAEVIELVGLKgkeqhlpHQLSGGQRQRVALARALV---MKPRIL-LLDEPLSALDAQIRKHLRQQIRQi 179
Cdd:cd03227   66 -----------AVSAELIFTR-------LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILE- 126

                        170       180
                 ....*....|....*....|....*.
gi 738468658 180 QRELNLTTIFVTHDqEEAMLMSDRIF 205
Cdd:cd03227  127 HLVKGAQVIVITHL-PELAELADKLI 151
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 29-212 7.13e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 50.94  E-value: 7.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  29 GEFITLLGPSGCGKSTLLRCLAG-LEPVNdGRIYVNKqDITSSPPQQREIGMV------FQSYALFPNMTTERNI----- 96
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGeLAPVS-GEIGLAK-GIKLGYFAQHQLEFLradespLQHLARLAPQELEQKLrdylg 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  97 AFGLKMQKVPENEQRksvaevielvglkgkeqhlphqLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQI 176
Cdd:PRK10636 416 GFGFQGDKVTEETRR----------------------FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 738468658 177 RQIQRELnlttIFVTHDQEEAMLMSDRIFLMNKGEI 212
Cdd:PRK10636 474 IDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 36-176 3.09e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.17  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  36 GPSGCGKSTLLRCLAGLEPVNDGRIYVNKQDITSSppQQREIGMVFQSYALFPNMTTERNIAFGLKMQKVPEneqrkSVA 115
Cdd:PRK13541  33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAE-----TLY 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738468658 116 EVIELVGLKGKEQHLPHQLSGGQRQRVALARALVMKPRILLLDEPLSALDAQIRKHLRQQI 176
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
PLN03073 PLN03073
ABC transporter F family; Provisional
 133-165 5.75e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.93  E-value: 5.75e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 738468658 133 QLSGGQRQRVALARALVMKPRILLLDEPLSALD 165
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 134-255 3.06e-05

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 45.77  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  134 LSGGQRQRVALARAL------VMkpriLLLDEPlsaldaQIRKHLRQQIRQIQ-----RELNLTTIFVTHDqEEAMLMSD 202
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgVL----YVLDEP------SIGLHQRDNRRLINtlkrlRDLGNTLIVVEHD-EDTIRAAD 557

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 738468658  203 RIFLMNK------GEIVQSDTAENLytqpanefvarfmghynlvsAHNANSLLGLNLSG 255
Cdd:TIGR00630 558 YVIDIGPgagehgGEVVASGTPEEI--------------------LANPDSLTGQYLSG 596
GguA NF040905
sugar ABC transporter ATP-binding protein;
134-213 9.81e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.01  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 134 LSGGQRQRVALARALVMKPRILLLDEPLSALD--AqirkhlRQQIRQIQRELNLT---TIFVTHDQEEAMLMSDRIFLMN 208
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgA------KYEIYTIINELAAEgkgVIVISSELPELLGMCDRIYVMN 478


                 ....*
gi 738468658 209 KGEIV 213
Cdd:NF040905 479 EGRIT 483
PLN03140 PLN03140
ABC transporter G family member; Provisional
 34-213 1.83e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 43.30  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   34 LLGPSGCGKSTLLRCLAG-LEPVND--GRIYVNKQDITSSPPQQREiGMVFQSYALFPNMTTERNIAFGLKMQKV----- 105
Cdd:PLN03140  196 LLGPPSSGKTTLLLALAGkLDPSLKvsGEITYNGYRLNEFVPRKTS-AYISQNDVHVGVMTVKETLDFSARCQGVgtryd 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  106 ---------------PENE----QRKSVAEVIE----------LVGLK-------GKEqhLPHQLSGGQRQRVALARALV 149
Cdd:PLN03140  275 llselarrekdagifPEAEvdlfMKATAMEGVKsslitdytlkILGLDickdtivGDE--MIRGISGGQKKRVTTGEMIV 352

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  150 MKPRILLLDEPLSALDA----QIRKHLRQQIRqiqreLNLTTIFVTHDQ--EEAMLMSDRIFLMNKGEIV 213
Cdd:PLN03140  353 GPTKTLFMDEISTGLDSsttyQIVKCLQQIVH-----LTEATVLMSLLQpaPETFDLFDDIILLSEGQIV 417
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 117-179 4.73e-04

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 41.09  E-value: 4.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658 117 VIELVGLKGKEQHLPHQLSGGQRQRVALARALVMK-----PrILLLDEPLSALDAQIRKHLRQQIRQI 179
Cdd:cd03272  142 INSLTNMKQDEQQEMQQLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALDAQYRTAVANMIKEL 208
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 134-213 1.46e-03

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: 39.55  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 134 LSGGQRQRVALARALVMKPR--ILLLDEPLSALDAQIRKHLRQQIRQIqRELNLTTIFVTHDqEEAMLMSDRIFLM---- 207
Cdd:cd03270  138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIgpga 215


                 ....*...
gi 738468658 208 --NKGEIV 213
Cdd:cd03270  216 gvHGGEIV 223
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 25-195 1.93e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 40.15  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  25 SVSKGEFITLLGPSGCGKSTLLRCLAGLEPVNDGRI---------YVNKQDITSSPPQ-------QREigmvFQSYALFP 88
Cdd:PRK10636  23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQETPALPQPAleyvidgDRE----YRQLEAQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658  89 NMTTERNIAFGL-----KMQKVPENEQRKSVAEVIELVGLKGKEQHLP-HQLSGGQRQRVALARALVMKPRILLLDEPLS 162
Cdd:PRK10636  99 HDANERNDGHAIatihgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 738468658 163 ALDAQIRKHLRQQIRQIQRelnlTTIFVTHDQE 195
Cdd:PRK10636 179 HLDLDAVIWLEKWLKSYQG----TLILISHDRD 207
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 82-204 2.51e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.81  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   82 QSYALFPNMTTERNIAFglkMQKVPENEQrkSVAEVIElvGLKGK-----EQHLPH--------QLSGGQRQRVALARAL 148
Cdd:PRK00635  419 KTFAEFQQMSLQELFIF---LSQLPSKSL--SIEEVLQ--GLKSRlsiliDLGLPYltperalaTLSGGEQERTALAKHL 491

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 738468658  149 --VMKPRILLLDEPLSALDAQIRKHLRQQIRQIQRELNlTTIFVTHDqEEAMLMSDRI 204
Cdd:PRK00635  492 gaELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRI 547
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
125-195 3.97e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658 125 GKEQHLPHqLSGGQRQ------RVALARALVMKPRILLLDEPLSALDAQIRKHL----RQQIRQIQRelnltTIFVTHDQ 194
Cdd:PRK03918 781 GKERPLTF-LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRKIPQ-----VIIVSHDE 854


                 .
gi 738468658 195 E 195
Cdd:PRK03918 855 E 855
recF PRK00064
recombination protein F; Reviewed
 154-214 6.35e-03

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 38.22  E-value: 6.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738468658 154 ILLLDEPLSALDAQIRKHLRQQIRQIQrelnlTTIFVT---HDQEEAMLMSDRIFLMNKGEIVQ 214
Cdd:PRK00064 303 ILLLDDVASELDDGRRAALLERLKGLG-----AQVFITttdLEDLADLLENAKIFHVEQGKITD 361
AAA_23 pfam13476
AAA domain;
19-189 7.39e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 37.09  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   19 FSGLNFSVSKGefITLL-GPSGCGKSTLLRCLA----GLEP--VNDGRIYVNKQDIT----SSPPQQREIGMVFQSYALF 87
Cdd:pfam13476   9 FRDQTIDFSKG--LTLItGPNGSGKTTILDAIKlalyGKTSrlKRKSGGGFVKGDIRigleGKGKAYVEITFENNDGRYT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738468658   88 PNMTTERNIAfglkmqkvpENEQRKSVAEVIELVGLKGKEQHLPHQLSGGQRQrvalaralvmKPRILLLDEplSALDAQ 167
Cdd:pfam13476  87 YAIERSRELS---------KKKGKTKKKEILEILEIDELQQFISELLKSDKII----------LPLLVFLGQ--EREEEF 145

                         170       180
                  ....*....|....*....|..
gi 738468658  168 IRKHLRQQIRQIQRELNLTTIF 189
Cdd:pfam13476 146 ERKEKKERLEELEKALEEKEDE 167
PrkA COG2766
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
34-71 9.33e-03

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 442049 [Multi-domain]  Cd Length: 675  Bit Score: 37.89  E-value: 9.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 738468658  34 LLGPSGCGKSTLLRCL-AGLE---PVNDGRIYV-------NKQDITSSP 71
Cdd:COG2766  113 LHGPVGSGKSTLARCLkRGLEeysRTDEGALYTfewnfpsADDDIKGSP 161
 
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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