NCBI Conserved Domain Search

Conserved domains on [gi|90111106|ref|NP_414796|]

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ABC transporter ATP-binding protein AfuC [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

ferric ABC transporter ATP-binding protein( domain architecture ID 11485344)

ferric ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex FbpABC and is responsible for coupling the energy of ATP hydrolysis to the import of Fe(3+) ions

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

1-348

0e+00

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 775.82 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI 80
Cdd:PRK11432   1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK11432  81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA 240
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  241 NLFPATFSDGYVDIYGYHLPRPLHF---GTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILL 317
Cdd:PRK11432 241 NIFPATLSGDYVDIYGYRLPRPAAFafnLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQELLL 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 90111106  318 QVNATRLQPDVGEQYYLEIHPYGMFVLADAA 348
Cdd:PRK11432 321 QVNATQLQPDLGEHYYLEIHPYGMFLLADAA 351

Name

Accession

Description

Interval

E-value

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

1-348

0e+00

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 775.82 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI 80
Cdd:PRK11432   1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK11432  81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA 240
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  241 NLFPATFSDGYVDIYGYHLPRPLHF---GTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILL 317
Cdd:PRK11432 241 NIFPATLSGDYVDIYGYRLPRPAAFafnLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQELLL 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 90111106  318 QVNATRLQPDVGEQYYLEIHPYGMFVLADAA 348
Cdd:PRK11432 321 QVNATQLQPDLGEHYYLEIHPYGMFLLADAA 351

PotA

COG3842

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

3-346

0e+00

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 508.48 E-value: 0e+00

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   3 QKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICM 82
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANL 242
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 243 FPATFSD---GYVDIYGYHL--PRPLHFGTQGEGMVGVRPEAITLSDRGEESQ-RCVIRHVAYMGPQYEVTVEW-HGQEI 315
Cdd:COG3842 242 LPGTVLGdegGGVRTGGRTLevPADAGLAAGGPVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLgDGQEL 321

                       330       340       350
                ....*....|....*....|....*....|..
gi 90111106 316 LLQV-NATRLQPDVGEQYYLEIHPYGMFVLAD 346
Cdd:COG3842 322 VVRVpNRAALPLEPGDRVGLSWDPEDVVVLPA 353

ABC_PotA_N

cd03300

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

7-238

2.65e-126

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: 361.55 E-value: 2.65e-126

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03300  81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMG 238
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

6-345

4.91e-123

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: 357.81 E-value: 4.91e-123

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQ 85
Cdd:TIGR03265   4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:TIGR03265  84 SYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPA 245
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   246 TF-SDGYVDIYGYHLPRPLHFGTQGEGM-VGVRPEAITLSDRGEESQR--CVIRHVAYMGPQYEVTVEWH---GQEILLQ 318
Cdd:TIGR03265 244 TRgGGSRARVGGLTLACAPGLAQPGASVrLAVRPEDIRVSPAGNAANLllARVEDMEFLGAFYRLRLRLEglpGQALVAD 323

                         330       340       350
                  ....*....|....*....|....*....|
gi 90111106   319 V--NATRLQPDV-GEQYYLEIHPYGMFVLA 345
Cdd:TIGR03265 324 VsaSEVERLGIRaGQPIWIELPAERLRAFA 353

ABC_arch_GlcV

NF040933

glucose ABC transporter ATP-binding protein GlcV;

7-338

3.70e-96

glucose ABC transporter ATP-binding protein GlcV;

Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 289.59 E-value: 3.70e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT--HRSI---QQ 77
Cdd:NF040933   3 VRVENVTKIFKKGKkevvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVAspGKIIvppED 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:NF040933  83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFM 237
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  238 GDANLFPATFS-DGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGE-------ESQRCVIRHVAYMGPQYEVTVE 309
Cdd:NF040933 243 GDINLLEGKVEeEGLVDGNDLKIPLPNPKLEAGEVIIGIRPEDIDISESDMrlppgfvEVGKGRVKVSSYAGGVFRVVVS 322

                        330       340       350
                 ....*....|....*....|....*....|
gi 90111106  310 W-HGQEILLQVNATRlQPDVGEQYYLEIHP 338
Cdd:NF040933 323 PiDDDSIEIIVNSDR-PIEEGEEVNLYVRP 351

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

22-308

3.59e-82

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 253.46 E-value: 3.59e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGY 101
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  102 GLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRE 181
Cdd:NF040840  96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  182 LQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGY----VDIYGY 257
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGegtiLDTGNI 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106  258 HLPRPLHFgtQGEGMVGVRPEAITLS-DRGEESQRCV----IRHVAYMGPQYEVTV 308
Cdd:NF040840 256 KIELPEEK--KGKVRIGIRPEDITIStEKVKTSARNEfkgkVEEIEDLGPLVKLTL 309

ABC_tran

pfam00005

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

22-165

5.00e-55

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: 177.07 E-value: 5.00e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHMSLGENV 99
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   100 GYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVD----QISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

9-215

3.21e-46

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 156.42 E-value: 3.21e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNT----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD----- 79
Cdd:NF038007   4 MQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrre 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   80 -ICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:NF038007  84 lIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  159 LFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQsEAFAVSDTVLVMNKGHI 215
Cdd:NF038007 164 LADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

15-208

1.03e-30

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.02 E-value: 1.03e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   15 RFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGqifidgeDVTHRSiqQRDICMVFQSYAL---FP 91
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAG--GARVAYVPQRSEVpdsLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   92 hMSLGENVGYGL----KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:NF040873  72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 90111106  168 DANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVL 208
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

7-227

3.69e-25

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 106.75 E-value: 3.69e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQQRDIcmv 83
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarHRRAVCPRI--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 fqSYA-------LFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:NF033858  79 --AYMpqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTH---DQSEAFavsDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATaymEEAERF---DWLVAMDAGRVLATGTPAELLAR 227

GguA

NF040905

sugar ABC transporter ATP-binding protein;

8-213

8.56e-24

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 101.79 E-value: 8.56e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLeKPS---EGQIFIDGEDVTHRSI---QQRDIC 81
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDIrdsEALGIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSYALFPHMSLGENVgyglkMLGVPRA--------ELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALIL 153
Cdd:NF040905  82 IIHQELALIPYLSIAENI-----FLGNERAkrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

7-227

1.24e-22

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 1.24e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD-ICMVFQ 85
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRrVGYMSQ 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAA 487

40850658_otr

NF000106

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

4-231

2.61e-14

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.85 E-value: 2.61e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTiLRLVAGLEKPSEGQ------IFIDGEDVTHRSIQQ 77
Cdd:NF000106  11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRrpwrf*TWCANRRALRRTIG* 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALfphmSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:NF000106  90 HRPVR*GRRESF----SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR 238

AAA

smart00382

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

31-214

6.01e-11

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

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 6.01e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     31 QGQMVTLLGPSGCGKTTILRLVAG-LEKPSEGQIFIDGEDVTHRSIQQRdicmvfqsyalfphmslgenvgyglkmlgvp 109
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL------------------------------- 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    110 raelkarvkealamvdLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQ---- 185
Cdd:smart00382  50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllks 113

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 90111106    186 ------FDITSLYVTHDQSEAFAVSDTVLVMNKGH 214
Cdd:smart00382 114 eknltvILTTNDEKDLGPALLRRRFDRRIVLLLIL 148

GguA

NF040905

sugar ABC transporter ATP-binding protein;

21-163

2.91e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 2.91e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLE--KPSEGQIFIDGEDVTHRSIQQ---RDICMVFQ---SYALFPH 92
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDaidAGLAYVTEdrkGYGLNLI 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   93 MSLGENV-GYGLKmlGVPRAELKARVKEALAMvdlEGFEDRF------VDQI----SGGQQQRVALARALILKPKVLLFD 161
Cdd:NF040905 355 DDIKRNItLANLG--KVSRRGVIDENEEIKVA---EEYRKKMniktpsVFQKvgnlSGGNQQKVVLSKWLFTDPDVLILD 429


                 ..
gi 90111106  162 EP 163
Cdd:NF040905 430 EP 431

Name

Accession

Description

Interval

E-value

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

1-348

0e+00

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 775.82 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI 80
Cdd:PRK11432   1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK11432  81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA 240
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  241 NLFPATFSDGYVDIYGYHLPRPLHF---GTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILL 317
Cdd:PRK11432 241 NIFPATLSGDYVDIYGYRLPRPAAFafnLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQELLL 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 90111106  318 QVNATRLQPDVGEQYYLEIHPYGMFVLADAA 348
Cdd:PRK11432 321 QVNATQLQPDLGEHYYLEIHPYGMFLLADAA 351

PotA

COG3842

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

3-346

0e+00

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 508.48 E-value: 0e+00

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   3 QKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICM 82
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANL 242
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 243 FPATFSD---GYVDIYGYHL--PRPLHFGTQGEGMVGVRPEAITLSDRGEESQ-RCVIRHVAYMGPQYEVTVEW-HGQEI 315
Cdd:COG3842 242 LPGTVLGdegGGVRTGGRTLevPADAGLAAGGPVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLgDGQEL 321

                       330       340       350
                ....*....|....*....|....*....|..
gi 90111106 316 LLQV-NATRLQPDVGEQYYLEIHPYGMFVLAD 346
Cdd:COG3842 322 VVRVpNRAALPLEPGDRVGLSWDPEDVVVLPA 353

MalK

COG3839

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

7-343

2.44e-165

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 464.93 E-value: 2.44e-165

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:COG3839   4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:COG3839  84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGD--ANLFP 244
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 245 ATFSDGYVDIYGYHLPRPLHFGTQGEG--MVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQVNAt 322
Cdd:COG3839 244 GTVEGGGVRLGGVRLPLPAALAAAAGGevTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLGGQELVARVPG- 322

                       330       340
                ....*....|....*....|.
gi 90111106 323 RLQPDVGEQYYLEIHPYGMFV 343
Cdd:COG3839 323 DTRLRPGDTVRLAFDPERLHL 343

CysA

COG1118

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

7-343

2.06e-146

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 416.86 E-value: 2.06e-146

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV-THRSIQQRDICMVFQ 85
Cdd:COG1118   3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG1118  83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPA 245
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 246 TFSDGYVDIYGYHLPrPLHFGTQGEGMVGVRPEAITLSDRGEESQ--RCVIRHVAYMGPQYEVTVE---WHGQEILLQVN 320
Cdd:COG1118 243 RVIGGQLEADGLTLP-VAEPLPDGPAVAGVRPHDIEVSREPEGENtfPATVARVSELGPEVRVELKledGEGQPLEAEVT 321

                       330       340
                ....*....|....*....|....*.
gi 90111106 321 ATR---LQPDVGEQYYLEIHPYGMFV 343
Cdd:COG1118 322 KEAwaeLGLAPGDPVYLRPRPARVFL 347

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

1-309

1.39e-131

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 380.45 E-value: 1.39e-131

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI 80
Cdd:PRK09452   9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK09452  89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA 240
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  241 NLFPATF----SDGYVDIYGYHLPRPLHFG---TQGEG-MVGVRPEAITLSDRGEESQR-CVIRHVA---YMGPQYEVTV 308
Cdd:PRK09452 249 NIFDATVierlDEQRVRANVEGRECNIYVNfavEPGQKlHVLLRPEDLRVEEINDDEHAeGLIGYVRernYKGMTLDSVV 328


                 .
gi 90111106  309 E 309
Cdd:PRK09452 329 E 329

ABC_PotA_N

cd03300

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

7-238

2.65e-126

Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 361.55 E-value: 2.65e-126

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03300  81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMG 238
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

ABC_Carb_Solutes_like

cd03259

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

7-219

1.06e-125

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: 359.14 E-value: 1.06e-125

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03259  81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111106 167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

6-345

4.91e-123

Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 357.81 E-value: 4.91e-123

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQ 85
Cdd:TIGR03265   4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:TIGR03265  84 SYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPA 245
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   246 TF-SDGYVDIYGYHLPRPLHFGTQGEGM-VGVRPEAITLSDRGEESQR--CVIRHVAYMGPQYEVTVEWH---GQEILLQ 318
Cdd:TIGR03265 244 TRgGGSRARVGGLTLACAPGLAQPGASVrLAVRPEDIRVSPAGNAANLllARVEDMEFLGAFYRLRLRLEglpGQALVAD 323

                         330       340       350
                  ....*....|....*....|....*....|
gi 90111106   319 V--NATRLQPDV-GEQYYLEIHPYGMFVLA 345
Cdd:TIGR03265 324 VsaSEVERLGIRaGQPIWIELPAERLRAFA 353

ugpC

PRK11650

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

7-338

1.58e-120

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 351.45 E-value: 1.58e-120

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQ 85
Cdd:PRK11650   4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK11650  84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA--NLF 243
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPamNLL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  244 PATFS-DGYVDIYGYH----LPRPLHFGTQGEGMVGVRPEAITLSDrGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQ 318
Cdd:PRK11650 244 DGRVSaDGAAFELAGGialpLGGGYRQYAGRKLTLGIRPEHIALSS-AEGGVPLTVDTVELLGADNLAHGRWGGQPLVVR 322

                        330       340
                 ....*....|....*....|
gi 90111106  319 VnATRLQPDVGEQyyLEIHP 338
Cdd:PRK11650 323 L-PHQERPAAGST--LWLHL 339

ABC_CysA_sulfate_importer

cd03296

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

7-239

4.08e-111

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: 323.14 E-value: 4.08e-111

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03296   3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKM----LGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03296  83 YALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGD 239
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239

ABC_MalK_N

cd03301

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

7-219

2.15e-106

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: 310.34 E-value: 2.15e-106

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03301  81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111106 167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213

potA

TIGR01187

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

37-344

1.19e-105

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: 312.51 E-value: 1.19e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    37 LLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKAR 116
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   117 VKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHD 196
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   197 QSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATF----SDGYVDIYGYHLPRPLHFGTQGEG- 271
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVierkSEQVVLAGVEGRRCDIYTDVPVEKd 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   272 ---MVGVRPEAITL----SDRGEESQRCVIRHVAYMGPQYEVTVEW-HGQEILLQV----NATRLQPDVGEQYYLEIHPY 339
Cdd:TIGR01187 241 qplHVVLRPEKIVIeeedEANSSNAIIGHVIDITYLGMTLEVHVRLeTGQKVLVSEffneDDPHMSPSIGDRVGLTWHPG 320


                  ....*
gi 90111106   340 GMFVL 344
Cdd:TIGR01187 321 SEVVL 325

3a0106s01

TIGR00968

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

7-241

5.30e-105

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

Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 307.88 E-value: 5.30e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106   167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDAN 241
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

7-334

8.80e-105

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 311.25 E-value: 8.80e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   87 YALFPHMSLGENVGYGLKMLgvPR------AELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK10851  83 YALFRHMTVFDNIAFGLTVL--PRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA 240
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  241 NLFPATFSDGYVDIYGYHLP---RPLHfgtQGEGMVGVRPEAITLSDRGeeSQRC----VIRHVAYMGPQYEVTVE---W 310
Cdd:PRK10851 241 NRLQGTIRGGQFHVGAHRWPlgyTPAY---QGPVDLFLRPWEVDISRRT--SLDSplpvQVLEVSPKGHYWQLVVQplgW 315

                        330       340
                 ....*....|....*....|....
gi 90111106  311 HGQEILLQVNATRLQPDVGEQYYL 334
Cdd:PRK10851 316 YNEPLTVVMHGDIDAPQRGERLFV 339

TauB

COG1116

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

1-213

3.86e-101

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 298.54 E-value: 3.86e-101

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   1 MTQ-KNFVELRNVTKRF----GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSi 75
Cdd:COG1116   1 MSAaAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  76 qqRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:COG1116  80 --PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215

ABC_arch_GlcV

NF040933

glucose ABC transporter ATP-binding protein GlcV;

7-338

3.70e-96

glucose ABC transporter ATP-binding protein GlcV;

Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 289.59 E-value: 3.70e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT--HRSI---QQ 77
Cdd:NF040933   3 VRVENVTKIFKKGKkevvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVAspGKIIvppED 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:NF040933  83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFM 237
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  238 GDANLFPATFS-DGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGE-------ESQRCVIRHVAYMGPQYEVTVE 309
Cdd:NF040933 243 GDINLLEGKVEeEGLVDGNDLKIPLPNPKLEAGEVIIGIRPEDIDISESDMrlppgfvEVGKGRVKVSSYAGGVFRVVVS 322

                        330       340       350
                 ....*....|....*....|....*....|
gi 90111106  310 W-HGQEILLQVNATRlQPDVGEQYYLEIHP 338
Cdd:NF040933 323 PiDDDSIEIIVNSDR-PIEEGEEVNLYVRP 351

ABC_NrtD_SsuB_transporters

cd03293

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

7-215

2.93e-94

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: 279.74 E-value: 2.93e-94

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiqqRDICM 82
Cdd:cd03293   1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03293  78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNK--GHI 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

7-334

9.65e-93

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 281.72 E-value: 9.65e-93

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:PRK11607  20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPAT 246
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  247 F---SDGYVDIYGYHLPRPLHFGTQG---EG---MVGVRPEAITLSDR----GEESQRCVIRHVAYMG--PQYEVTVEwH 311
Cdd:PRK11607 260 LkerQEDGLVIDSPGLVHPLKVDADAsvvDNvpvHVALRPEKIMLCEEppadGCNFAVGEVIHIAYLGdlSIYHVRLK-S 338

                        330       340
                 ....*....|....*....|....*..
gi 90111106  312 GQEILLQV-NATRL---QPDVGEQYYL 334
Cdd:PRK11607 339 GQMISAQLqNAHRYrkgLPTWGDEVRL 365

OpuBA

COG1125

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

8-238

1.76e-90

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

Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 273.12 E-value: 1.76e-90

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVF 84
Cdd:COG1125   3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDL--EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:COG1125  83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMG 238
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

7-328

2.95e-89

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 272.29 E-value: 2.95e-89

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:PRK11000   4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PRK11000  84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDA--NLFP 244
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmNFLP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  245 ATFSDGYVDIYGYHLPRPLHF-----GTQ---GEGM-VGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGqei 315
Cdd:PRK11000 244 VKVTATAIEQVQVELPNRQQVwlpveGRGvqvGANMsLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIPA--- 320

                        330
                 ....*....|...
gi 90111106  316 lLQVNATRLQPDV 328
Cdd:PRK11000 321 -IRQNLVYRQNDV 332

MlaF

COG1127

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

2-224

3.10e-89

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: 267.62 E-value: 3.10e-89

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   2 TQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD-- 79
Cdd:COG1127   1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ---ICMVFQSYALFPHMSLGENVGYGLKML-GVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:COG1127  81 rrrIGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229

GlnQ

COG1126

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

7-230

2.68e-84

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 254.92 E-value: 2.68e-84

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ----QRDICM 82
Cdd:COG1126   2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENVGYGL-KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:COG1126  82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 162 EPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPAS 230
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229

ABC_OpuCA_Osmoprotection

cd03295

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

7-238

1.81e-83

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: 252.99 E-value: 1.81e-83

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMV 83
Cdd:cd03295   1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLE--GFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03295  81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 162 EPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMG 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237

ABC_ModC_like

cd03299

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

7-242

6.69e-83

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: 251.49 E-value: 6.69e-83

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGsNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03299   1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03299  80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 167 LDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANL 242
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

22-308

3.59e-82

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 253.46 E-value: 3.59e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGY 101
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  102 GLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRE 181
Cdd:NF040840  96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  182 LQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGY----VDIYGY 257
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGegtiLDTGNI 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106  258 HLPRPLHFgtQGEGMVGVRPEAITLS-DRGEESQRCV----IRHVAYMGPQYEVTV 308
Cdd:NF040840 256 KIELPEEK--KGKVRIGIRPEDITIStEKVKTSARNEfkgkVEEIEDLGPLVKLTL 309

ABC_Org_Solvent_Resistant

cd03261

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

7-224

8.42e-81

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: 245.87 E-value: 8.42e-81

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ-----RDIC 81
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFPHMSLGENVGYGLKMLGV-PRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03261  81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224

ProV

COG4175

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

7-241

5.59e-80

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

Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 249.25 E-value: 5.59e-80

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN-----------------------TV-IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQ 62
Cdd:COG4175   4 IEVRNLYKIFGKRperalklldqgkskdeilektgqTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  63 IFIDGEDVTH------RSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQ 136
Cdd:COG4175  84 VLIDGEDITKlskkelRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIM 216
Cdd:COG4175 164 LSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243

                       250       260
                ....*....|....*....|....*
gi 90111106 217 QIGSPQDLYRQPASRFMASFMGDAN 241
Cdd:COG4175 244 QIGTPEEILTNPANDYVADFVEDVD 268

GsiA

COG1123

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

7-228

1.54e-79

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: 251.75 E-value: 1.54e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN-----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ---- 77
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 -RDICMVFQ--SYALFPHMSLGENVGYGLKMLGV-PRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALI 152
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496

ABC_Class3

cd03229

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

7-214

2.20e-79

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: 240.17 E-value: 2.20e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT----HRSIQQRDICM 82
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENVGYGLkmlgvpraelkarvkealamvdlegfedrfvdqiSGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03229  81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGH 214
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178

CcmA

COG1131

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

7-227

3.25e-79

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 241.89 E-value: 3.25e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVFQ 85
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG1131  81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 166 NLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221

ABC_Pro_Gly_Betaine

cd03294

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

12-239

1.04e-77

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: 239.47 E-value: 1.04e-77

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  12 VTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH------RSIQQRDICMVFQ 85
Cdd:cd03294  30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelRELRRKKISMVFQ 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGD 239
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263

EcfA2

COG1122

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

7-228

4.00e-77

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: 236.46 E-value: 4.00e-77

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMV 83
Cdd:COG1122   1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQS--YALFpHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:COG1122  81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 162 EPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225

ABC_MJ0796_LolCDE_FtsE

cd03255

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

7-215

4.79e-76

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: 233.15 E-value: 4.79e-76

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD--- 79
Cdd:cd03255   1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ---ICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:cd03255  81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAvSDTVLVMNKGHI 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218

LolD

COG1136

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

7-215

3.61e-75

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 231.09 E-value: 3.61e-75

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD--- 79
Cdd:COG1136   5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ---ICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:COG1136  85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQsEAFAVSDTVLVMNKGHI 215
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222

ThiQ

COG3840

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

8-238

4.33e-75

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 231.18 E-value: 4.33e-75

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVidNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSY 87
Cdd:COG3840   3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  88 ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:COG3840  81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 168 DANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMG 238
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231

ABC_HisP_GlnQ

cd03262

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

7-215

3.69e-73

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: 225.49 E-value: 3.69e-73

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ----QRDICM 82
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENVGYGL-KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03262  81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 162 EPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213

DppF

COG1124

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

7-230

2.52e-72

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: 224.68 E-value: 2.52e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGS----NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDI 80
Cdd:COG1124   2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  81 CMVFQSY--ALFPHMSLGENVGYGLKMLGVPRAElkARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG1124  82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPAS 230
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232

ABC_cobalt_CbiO_domain1

cd03225

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

8-214

4.77e-70

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: 217.72 E-value: 4.77e-70

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMV 83
Cdd:cd03225   1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQsyalFP-HMSLGENVG----YGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:cd03225  81 FQ----NPdDQFFGPTVEeevaFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 159 LFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGH 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

7-237

2.96e-69

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 216.50 E-value: 2.96e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI----CM 82
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQSYALFPHMSLGENVGYG-LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK09493  82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  162 EPLSNLDANLR----RSMRDKIRElqkqfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFM 237
Cdd:PRK09493 162 EPTSALDPELRhevlKVMQDLAEE-----GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236

ABC_MetN_methionine_transporter

cd03258

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

7-228

6.77e-69

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: 215.52 E-value: 6.77e-69

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS-----IQQ 77
Cdd:cd03258   2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:cd03258  82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232

FepC

COG1120

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

7-224

2.40e-68

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: 214.91 E-value: 2.40e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVF 84
Cdd:COG1120   2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENVGYG----LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG1120  82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225

ABC_ModC_molybdenum_transporter

cd03297

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

14-219

9.06e-68

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: 211.77 E-value: 9.06e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  14 KRFGSNTVidNINLTIPqGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDG------EDVTHRSIQQRDICMVFQSY 87
Cdd:cd03297   8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  88 ALFPHMSLGENVGYGLKmlGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd03297  85 ALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 90111106 168 DANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214

ModC

COG4148

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

11-246

2.48e-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: 215.73 E-value: 2.48e-67

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  11 NVTKRFGSNTVidNINLTIPqGQMVT-LLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV--THRSI----QQRDICMV 83
Cdd:COG4148   6 DFRLRRGGFTL--DVDFTLP-GRGVTaLFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIflppHRRRIGYV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFPHMSLGENVGYGLKMlgVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:COG4148  83 FQEARLFPHLSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 164 LSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLF 243
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVL 240


                ...
gi 90111106 244 PAT 246
Cdd:COG4148 241 EAT 243

AbcC

COG1135

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

7-236

2.99e-67

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 214.94 E-value: 2.99e-67

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ----- 77
Cdd:COG1135   2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG1135  82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASF 236
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240

NatA

COG4555

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

8-227

8.92e-67

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: 210.48 E-value: 8.92e-67

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVFQS 86
Cdd:COG4555   3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:COG4555  83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 167 LDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222

ABC_NikE_OppD_transporters

cd03257

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

7-219

1.12e-66

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: 209.67 E-value: 1.12e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF----GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH-----RSIQQ 77
Cdd:cd03257   2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlRKIRR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 RDICMVFQSY--ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDL---EGFEDRFVDQISGGQQQRVALARALI 152
Cdd:cd03257  82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228

FtsE

COG2884

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

7-215

1.94e-66

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 208.75 E-value: 1.94e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQQ--RDI 80
Cdd:COG2884   2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkRREIPYlrRRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG2884  82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRL 215

ABC_PstB_phosphate_transporter

cd03260

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

7-224

1.31e-65

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: 206.65 E-value: 1.31e-65

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEK-----PSEGQIFIDGEDVTHRSIQ----Q 77
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlelR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 RDICMVFQSYALFPhMSLGENVGYGLKMLGV-PRAELKARVKEALAMVDL-EGFEDR-FVDQISGGQQQRVALARALILK 154
Cdd:cd03260  81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 155 PKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227

PhnC

COG3638

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

7-224

3.06e-65

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.45 E-value: 3.06e-65

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQQ--RDI 80
Cdd:COG3638   3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrGRALRRlrRRI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  81 CMVFQSYALFPHMSLGENV-----GY--GLK-MLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALI 152
Cdd:COG3638  83 GMIFQQFNLVPRLSVLTNVlagrlGRtsTWRsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 153 LKPKVLLFDEPLSNLD-ANLRRSMRDkIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG3638 163 QEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

8-204

5.30e-65

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 204.64 E-value: 5.30e-65

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKP---SEGQIFIDGEDVTHRSIQQRDICMVF 84
Cdd:COG4136   3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGILF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENVGYGLKMlGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:COG4136  83 QDDLLFPHLSVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 90111106 165 SNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVS 204
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG 201

TauB

COG4525

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

8-210

2.75e-63

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 202.01 E-value: 2.75e-63

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIqqrDICMV 83
Cdd:COG4525   5 TVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---DRGVV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:COG4525  82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 90111106 164 LSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVM 210
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208

ectoine_ehuA

TIGR03005

ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...

7-237

1.19e-62

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: 200.06 E-value: 1.19e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH-------------- 72
Cdd:TIGR03005   1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpadek 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    73 --RSIQQRdICMVFQSYALFPHMSLGENVGYG-LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALAR 149
Cdd:TIGR03005  81 hlRQMRNK-IGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   150 ALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239


                  ....*...
gi 90111106   230 SRFMASFM 237
Cdd:TIGR03005 240 EERTREFL 247

ECF_ATPase_1

TIGR04520

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

7-227

2.22e-62

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: 199.96 E-value: 2.22e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS----IQQRdI 80
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweIRKK-V 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    81 CMVFQSyalfPH-----MSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:TIGR04520  80 GMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106   156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226

GsiA

COG1123

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

7-230

2.62e-61

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: 204.37 E-value: 2.62e-61

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS---EGQIFIDGEDVTHRSIQQR--D 79
Cdd:COG1123   5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ICMVFQS--YALFPhMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG1123  85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPAS 230
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

9-215

1.21e-60

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 195.28 E-value: 1.21e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHrsiQQRDICMVFQSYA 88
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTRLMFQDAR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   89 LFPHMSLGENVGYGLKmlgvprAELKARVKEALAMVdleGFEDRFVD---QISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK11247  92 LLPWKKVIDNVGLGLK------GQWRDAALQALAAV---GLADRANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLG 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212

ABC_DR_subfamily_A

cd03230

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

7-215

1.43e-60

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: 191.84 E-value: 1.43e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVFQ 85
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYglkmlgvpraelkarvkealamvdlegfedrfvdqiSGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03230  81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 90111106 166 NLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173

ECF_ATPase_2

TIGR04521

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

7-228

2.99e-60

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: 194.59 E-value: 2.99e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNT-----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH------RSI 75
Cdd:TIGR04521   1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkklKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    76 QQRdICMVFQsyalFPHMSLGEN-----VGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDR--FvdQISGGQQQRVAL 147
Cdd:TIGR04521  81 RKK-VGLVFQ----FPEHQLFEEtvykdIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERspF--ELSGGQMRRVAI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   148 ARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233


                  .
gi 90111106   228 P 228
Cdd:TIGR04521 234 V 234

AppF

COG4608

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

1-229

3.97e-60

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 196.11 E-value: 3.97e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   1 MTQKNFVELRNVTKRF---------GSNTV--IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGED 69
Cdd:COG4608   2 AMAEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  70 VTHRSIQQ-----RDICMVFQ-SYA-LFPHMSLGENVGYGLKMLGV-PRAELKARVKEALAMVDL-EGFEDRFVDQISGG 140
Cdd:COG4608  82 ITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 141 QQQRVALARALILKPKVLLFDEPLSNLDA-------NLrrsmrdkIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVsiqaqvlNL-------LEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLG 234

                       250
                ....*....|....*.
gi 90111106 214 HIMQIGSPQDLYRQPA 229
Cdd:COG4608 235 KIVEIAPRDELYARPL 250

LivG

COG0411

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

8-229

4.43e-60

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: 193.72 E-value: 4.43e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS---IQQRDICMVF 84
Cdd:COG0411   6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphrIARLGIARTF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENV----------GYGLKMLGVPR-----AELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALAR 149
Cdd:COG0411  86 QNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 150 ALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245

ZnuC

COG1121

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

1-229

4.99e-60

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 193.00 E-value: 4.99e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ---- 76
Cdd:COG1121   1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyv 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  77 -QRdicmvFQSYALFPhMSLGENVGYGL----KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARAL 151
Cdd:COG1121  81 pQR-----AEVDWDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQiGSPQDLYRQPA 229
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

7-237

1.66e-59

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 191.77 E-value: 1.66e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDG------EDVTHRSIQQ--R 78
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRElrR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 DICMVFQSYALFPHMSLGEN-VGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK11124  83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQkQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSpQDLYRQPASRFMASFM 237
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYL 240

ABC_PhnC_transporter

cd03256

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

8-224

1.01e-58

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: 189.70 E-value: 1.01e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQQ--RDIC 81
Cdd:cd03256   2 EVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQlrRQIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFPHMSLGENVGYGlkMLG-----------VPRAElKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARA 150
Cdd:cd03256  82 MIFQQFNLIERLSVLENVLSG--RLGrrstwrslfglFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232

FetA

COG4619

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

8-215

5.53e-58

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.56 E-value: 5.53e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVFQ 85
Cdd:COG4619   2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPhMSLGENVGYGLKMLGVPRAElkARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:COG4619  82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111106 165 SNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209

ABC_Mj1267_LivG_branched

cd03219

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

8-229

9.26e-58

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: 186.87 E-value: 9.26e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMVF 84
Cdd:cd03219   2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENV--------GYGLKMLGVPR--AELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILK 154
Cdd:cd03219  82 QIPRLFPELTVLENVmvaaqartGSGLLLARARReeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 155 PKVLLFDEPLSNLDANLRRSMRDKIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235

DppD

COG0444

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

7-229

1.69e-57

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: 189.11 E-value: 1.69e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKP---SEGQIFIDGEDVTH------R 73
Cdd:COG0444   2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  74 SIQQRDICMVFQ-SY-ALFPHMSLGENVGYGLKM-LGVPRAELKARVKEALAMVDL---EGFEDRFVDQISGGQQQRVAL 147
Cdd:COG0444  82 KIRGREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 148 ARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241


                ..
gi 90111106 228 PA 229
Cdd:COG0444 242 PR 243

ABC_Iron-Siderophores_B12_Hemin

cd03214

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

8-219

1.78e-57

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: 184.18 E-value: 1.78e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQrdicmvfqsy 87
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  88 alfphmslgenvgyglkmlgvpRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd03214  71 ----------------------LARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 90111106 168 DANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

7-235

5.92e-57

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 188.47 E-value: 5.92e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF--GSNTVI--DNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ----- 77
Cdd:PRK11153   2 IELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP----ASRFM 233
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREFI 241


                 ..
gi 90111106  234 AS 235
Cdd:PRK11153 242 QS 243

ArtP

COG4161

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

7-237

5.99e-57

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 185.22 E-value: 5.99e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE------DVTHRSIQQ--R 78
Cdd:COG4161   3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLlrQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  79 DICMVFQSYALFPHMSLGEN-VGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG4161  83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQkQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSpQDLYRQPASRFMASFM 237
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240

ABC_DrrA

cd03265

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

7-224

1.31e-56

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: 183.34 E-value: 1.31e-56

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVFQ 85
Cdd:cd03265   1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03265  81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219

HisP

COG4598

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

7-235

1.32e-55

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

Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 182.31 E-value: 1.32e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVthRSIQQRD------- 79
Cdd:COG4598   9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI--RLKPDRDgelvpad 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ----------ICMVFQSYALFPHMSLGENVGYG-LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALA 148
Cdd:COG4598  87 rrqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 149 RALILKPKVLLFDEPLSNLDANLR----RSMRDKIRELQkqfdiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVgevlKVMRDLAEEGR-----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241

                       250
                ....*....|....*
gi 90111106 225 YRQPAS----RFMAS 235
Cdd:COG4598 242 FGNPKSerlrQFLSS 256

ABC_subfamily_A

cd03263

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

7-224

3.53e-55

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: 179.62 E-value: 3.53e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGS--NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV-THRSIQQRDICMV 83
Cdd:cd03263   1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:cd03263  81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 164 LSNLDANLRRSMRDKIRELQKQFDItsLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219

ABC_tran

pfam00005

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

22-165

5.00e-55

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 177.07 E-value: 5.00e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHMSLGENV 99
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   100 GYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVD----QISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

FtsE

TIGR02673

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...

7-213

5.02e-55

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: 179.37 E-value: 5.02e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVI-DNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH---RSIQQ--RDI 80
Cdd:TIGR02673   2 IEFHNVSKAYPGGVAAlHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgRQLPLlrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90111106   161 DEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213

ABC_ThiQ_thiamine_transporter

cd03298

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

7-219

1.51e-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: 175.37 E-value: 1.51e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVidNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03298   1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLkmlgVPRAELKA----RVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03298  79 NNLFAHLTVEQNVGLGL----SPGLKLTAedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

7-217

1.55e-53

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: 176.09 E-value: 1.55e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---- 78
Cdd:COG4181   9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  79 --DICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARvkEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:COG4181  89 arHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQ 217
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226

SunT

COG2274

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

7-224

1.96e-53

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: 186.96 E-value: 1.96e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICM 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFpHMSLGENVgyglkMLGVPRAELkARVKEALAMVDLEGFEDRFVD-----------QISGGQQQRVALARAL 151
Cdd:COG2274 554 VLQDVFLF-SGTIRENI-----TLGDPDATD-EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEEL 696

ABC_ATPase

cd00267

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

8-214

2.25e-53

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: 172.81 E-value: 2.25e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQrdicmvfqsy 87
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  88 alfphmsLGENVGYglkmlgvpraelkarvkealamvdlegfedrfVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd00267  71 -------LRRRIGY--------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 90111106 168 DANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGH 214
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157

ABC_phnC

TIGR02315

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...

7-225

3.89e-53

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: 175.18 E-value: 3.89e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH---RSIQQ--RDI 80
Cdd:TIGR02315   2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgKKLRKlrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    81 CMVFQSYALFPHMSLGENVGYGL--------KMLG-VPRAElKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARAL 151
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGrFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106   152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234

3a0107s01c2

TIGR00972

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

7-231

4.53e-53

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]

Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 175.18 E-value: 4.53e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILR-------LVAGLEkpSEGQIFIDGEDVTHRSIQ--- 76
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVR--IEGKVLFDGQDIYDKKIDvve 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    77 -QRDICMVFQSYALFPhMSLGENVGYGLKMLGV-PRAELKARVKEALAMVDL-EGFEDRFVDQ---ISGGQQQRVALARA 150
Cdd:TIGR00972  80 lRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEVKDRLHDSalgLSGGQQQRLCIARA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFdiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPAS 230
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKE 236


                  .
gi 90111106   231 R 231
Cdd:TIGR00972 237 K 237

PRK11264

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

7-239

6.36e-53

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 174.94 E-value: 6.36e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFI-DGEDVTHRSI--QQRDI--- 80
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIDTARSLsqQKGLIrql 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 ----CMVFQSYALFPHMSLGENVGYG-LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK11264  84 rqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLY---RQPASR- 231
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFadpQQPRTRq 242


                 ....*...
gi 90111106  232 FMASFMGD 239
Cdd:PRK11264 243 FLEKFLLQ 250

nickel_nikE

TIGR02769

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

7-235

1.70e-52

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: 174.22 E-value: 1.70e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSN---------TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH----- 72
Cdd:TIGR02769   3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrkq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    73 RSIQQRDICMVFQ-SYALF-PHMSLGENVGYGLK-MLGVPRAELKARVKEALAMVDLEG-FEDRFVDQISGGQQQRVALA 148
Cdd:TIGR02769  83 RRAFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   149 RALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIM-QIGSPQDL-YR 226
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeECDVAQLLsFK 242


                  ....*....
gi 90111106   227 QPASRFMAS 235
Cdd:TIGR02769 243 HPAGRNLQS 251

ABC_FtsE

cd03292

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

7-215

2.04e-52

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: 172.59 E-value: 2.04e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTV-IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH---RSIQ--QRDI 80
Cdd:cd03292   1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPylRRKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03292  81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 161 DEPLSNLDANLRRsmrdKIRELQKQFD---ITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03292 161 DEPTGNLDPDTTW----EIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

8-217

3.00e-52

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 173.35 E-value: 3.00e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRdicMVFQSY 87
Cdd:PRK11248   3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG---VVFQNE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   88 ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:PRK11248  80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90111106  168 DANLRRSMRDKIRELQKQFDITSLYVTHDQSEA-FAVSDTVLVM-NKGHIMQ 217
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAvFMATELVLLSpGPGRVVE 211

PstB

COG1117

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

7-228

4.81e-52

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 172.91 E-value: 4.81e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILR-------LVAGLEkpSEGQIFIDGEDVTHRSIQQ-- 77
Cdd:COG1117  12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYDPDVDVve 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 --RDICMVFQSYALFPhMSLGENVGYGLKMLGV-PRAELKARVKEALAMVDL-EGFEDRFVDQ---ISGGQQQRVALARA 150
Cdd:COG1117  90 lrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKDRLKKSalgLSGGQQQRLCIARA 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 151 LILKPKVLLFDEPLSNLD--ANLRrsMRDKIRELQKQFDItsLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpiSTAK--IEELILELKKDYTI--VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

22-219

1.17e-51

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: 171.11 E-value: 1.17e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiqqRDICMVFQSYALFPHMSLGENVGY 101
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG---PDRMVVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   102 GLK--MLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKI 179
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 90111106   180 RELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197

modC_ABC

TIGR02142

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

11-234

1.32e-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: 1.32e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    11 NVTKRFGSNTVidNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE---DVTHR---SIQQRDICMVF 84
Cdd:TIGR02142   4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGiflPPEKRRIGYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    85 QSYALFPHMSLGENVGYGLKMLGVPraELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:TIGR02142  82 QEARLFPHLSVRGNLRYGMKRARPS--ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   165 SNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMA 234
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229

PRK10070

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

12-236

5.54e-51

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 174.45 E-value: 5.54e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   12 VTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH------RSIQQRDICMVFQ 85
Cdd:PRK10070  34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASF 236
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264

ABC_Metallic_Cations

cd03235

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

8-213

5.62e-51

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: 168.87 E-value: 5.62e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHrsiQQRDICMVFQSY 87
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  88 AL---FPhMSLGENVGYGL----KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03235  78 SIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208

CcmA

COG4133

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

7-203

1.05e-50

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: 167.66 E-value: 1.05e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVFQ 85
Cdd:COG4133   3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAElkARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG4133  83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 90111106 166 NLDANLRRSMRDKIRELQKQFDITsLYVTHDQSEAFAV 203
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAV-LLTTHQPLELAAA 197

ABC_BcrA_bacitracin_resist

cd03268

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

7-215

1.71e-50

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: 167.39 E-value: 1.71e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQS 86
Cdd:cd03268   1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPraelKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03268  81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 90111106 167 LDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204

cbiO

PRK13637

energy-coupling factor transporter ATPase;

22-227

2.13e-49

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 167.15 E-value: 2.13e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI----CMVFQ--SYALFPHmSL 95
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-TI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   96 GENVGYGLKMLGVPRAELKARVKEALAMV--DLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90111106  174 SMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235

ABC_NatA_sodium_exporter

cd03266

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

7-219

2.34e-49

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: 164.85 E-value: 2.34e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNT----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDIC 81
Cdd:cd03266   2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03266  82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 162 EPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218

cbiO

PRK13650

energy-coupling factor transporter ATPase;

4-225

2.47e-49

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 166.45 E-value: 2.47e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNT---VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSI--QQR 78
Cdd:PRK13650   2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdIRH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 DICMVFQSY-ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13650  82 KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELF 228

YejF

COG4172

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

23-228

4.25e-49

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: 172.18 E-value: 4.25e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  23 DNINLTIPQGQMVTLLGPSGCGKTT----ILRLVaglekPSEGQIFIDGEDVTHRSIQQ-----RDICMVFQS-YA-LFP 91
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSP 377

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  92 HMSLGENVGYGLKMLGVP--RAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:COG4172 378 RMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 169 ANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:COG4172 458 VSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

17-237

5.42e-49

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 165.25 E-value: 5.42e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   17 GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT--HRSIQ---QRDICMVFQSY--AL 89
Cdd:PRK10419  23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRkafRRDIQMVFQDSisAV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   90 FPHMSLGENVGYGLK-MLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:PRK10419 103 NPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  168 DANLRRSMRDKIRELQKQFDITSLYVTHDQS--EAFAvsDTVLVMNKGHIM--QIGSPQDLYRQPASRFMASFM 237
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRlvERFC--QRVMVMDNGQIVetQPVGDKLTFSSPAGRVLQNAV 254

MdlB

COG1132

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

7-227

1.49e-48

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.50 E-value: 1.49e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTkrF---GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDIC 81
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIG 417

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFpHMSLGENVGYGLKmlGVPRAElkarVKEALAMVDLEGFEDRFVD-----------QISGGQQQRVALARA 150
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGRP--DATDEE----VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 151 LILKPKVLLFDEPLSNLDA--------NLRRSMRDKirelqkqfdiTSLYVTHDQS---EAfavsDTVLVMNKGHIMQIG 219
Cdd:COG1132 491 LLKDPPILILDEATSALDTetealiqeALERLMKGR----------TTIVIAHRLStirNA----DRILVLDDGRIVEQG 556


                ....*...
gi 90111106 220 SPQDLYRQ 227
Cdd:COG1132 557 THEELLAR 564

ABCC_MRP_Like

cd03228

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

7-214

1.50e-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: 161.01 E-value: 1.50e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVthRSIQQRDIC--- 81
Cdd:cd03228   1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRkni 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 -MVFQSYALFpHMSLGENVgyglkmlgvpraelkarvkealamvdlegfedrfvdqISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03228  79 aYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAfAVSDTVLVMNKGH 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171

MglA

COG1129

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

6-210

4.38e-48

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 169.04 E-value: 4.38e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSI---QQRDICM 82
Cdd:COG1129   4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHMSLGENV--GYGLKMLG-VPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG1129  84 IHQELNLVPNLSVAENIflGREPRRGGlIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111106 160 FDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVM 210
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213

ABC_TM1139_LivF_branched

cd03224

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

8-224

5.91e-48

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: 161.06 E-value: 5.91e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMVF 84
Cdd:cd03224   2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENvgygLKM--LGVPRAELKARVKEALAMV-DLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03224  82 EGRRIFPELTVEEN----LLLgaYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 162 EPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219

L_ocin_972_ABC

TIGR03608

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...

9-197

2.95e-47

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: 158.93 E-value: 2.95e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     9 LRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH------RSIQQRDICM 82
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnskkaSKFRREKLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    83 VFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 90111106   163 PLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQ 197
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP 194

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

26-230

3.05e-47

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 159.75 E-value: 3.05e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   26 NLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYG--- 102
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  103 -LKMLGVPRAELKARVKEalamVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRE 181
Cdd:PRK10771  99 gLKLNAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 90111106  182 LQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPAS 230
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223

CydD

COG4988

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

7-227

3.52e-47

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: 167.63 E-value: 3.52e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICMV 83
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFpHMSLGENVgyglkMLGVPRAElKARVKEALAMVDLEGFEDRFVDQI-----------SGGQQQRVALARALI 152
Cdd:COG4988 417 PQNPYLF-AGTIRENL-----RLGRPDAS-DEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALL 489

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

7-224

3.65e-47

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 160.54 E-value: 3.65e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFG--SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICM 82
Cdd:PRK13632   8 IKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQSY-ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK13632  88 IFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106  162 EPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFaVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229

thiQ

TIGR01277

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

26-219

5.27e-47

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: 158.49 E-value: 5.27e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    26 NLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKM 105
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   106 LGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQ 185
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 90111106   186 FDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

7-231

6.91e-47

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: 158.86 E-value: 6.91e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMV 83
Cdd:cd03218   1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:cd03218  81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 164 LSNLDANLRRSMRDKIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227

YhaQ

COG4152

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

7-227

1.44e-46

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.89 E-value: 1.44e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ-------Rd 79
Cdd:COG4152   2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 icmvfqsyALFPHMSLGENVGY--GLKmlGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG4152  81 --------GLYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 158 LLFDEPLSNLD---ANLrrsMRDKIRELQKQfDITSLYVTH--DQSEAFAvsDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:COG4152 151 LILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEELC--DRIVIINKGRKVLSGSVDEIRRQ 219

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

9-215

3.21e-46

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 156.42 E-value: 3.21e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNT----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD----- 79
Cdd:NF038007   4 MQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrre 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   80 -ICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:NF038007  84 lIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  159 LFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQsEAFAVSDTVLVMNKGHI 215
Cdd:NF038007 164 LADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

4-228

4.85e-46

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 157.38 E-value: 4.85e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-----EKPSEGQIFIDGEDVTHRSIQQ- 77
Cdd:PRK14247   1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 -RDICMVFQSYALFPHMSLGENVGYGLKM--LGVPRAELKARVKEALAMVDL-EGFEDRF---VDQISGGQQQRVALARA 150
Cdd:PRK14247  81 rRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

7-213

4.89e-46

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: 155.90 E-value: 4.89e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiqQRDICMVFQS 86
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03269  79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 90111106 167 LDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204

ABC_drug_resistance_like

cd03264

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

7-219

5.71e-46

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: 155.81 E-value: 5.71e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGqMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT-HRSIQQRDICMVFQ 85
Cdd:cd03264   1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkQPQKLRRRIGYLPQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03264  80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 166 NLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

3-227

1.57e-45

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 156.71 E-value: 1.57e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    3 QKNFVELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--R 78
Cdd:PRK13635   2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 DICMVFQSY-ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13635  82 QVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKS 230

ABC_Carb_Monos_I

cd03216

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

7-215

2.27e-45

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: 152.58 E-value: 2.27e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiqqrdicmvfqs 86
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 yalfphmslgenvgyglkmlgvPRAELKARVkealamvdlegfedRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03216  69 ----------------------PRDARRAGI--------------AMVYQLSVGERQMVEIARALARNARLLILDEPTAA 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 90111106 167 LDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160

CydC

COG4987

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

7-229

3.12e-45

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: 162.63 E-value: 3.12e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICM 82
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFpHMSLGENVgyglkMLGVPRAElKARVKEALAMVDLEGFEDRFVD-----------QISGGQQQRVALARAL 151
Cdd:COG4987 414 VPQRPHLF-DTTLRENL-----RLARPDAT-DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARAL 486

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAFAVsDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNG 561

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

4-228

4.91e-45

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 154.61 E-value: 4.91e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-----EKPSEGQIFIDGEDVTHRSIQ-- 76
Cdd:PRK14267   2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpi 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   77 --QRDICMVFQSYALFPHMSLGENVGYGLKMLGV--PRAELKARVKEALAMVDL-EGFEDRFVD---QISGGQQQRVALA 148
Cdd:PRK14267  82 evRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRLVIA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  149 RALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDItsLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

1-225

2.26e-44

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 153.37 E-value: 2.26e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-- 76
Cdd:PRK13648   2 EDKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   77 QRDICMVFQS-YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK13648  82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIF 230

LivF

COG0410

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

8-229

2.75e-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: 2.75e-44

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMVF 84
Cdd:COG0410   5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENVgyglkMLGVPRAELKARVKEALAMV-----DLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG0410  85 EGRRIFPSLTVEENL-----LLGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 160 FDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

1-231

4.10e-44

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 152.61 E-value: 4.10e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--- 77
Cdd:PRK11831   2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 --RDICMVFQSYALFPHMSLGENVGYGLK-MLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILK 154
Cdd:PRK11831  82 vrKRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  155 PKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238

SapF

COG4167

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

8-228

1.08e-43

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 151.53 E-value: 1.08e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNT---------VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR 78
Cdd:COG4167   6 EVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  79 --DICMVFQ--SYALFPHMSLGenvgyglKMLGVP--------RAELKARVKEALAMVDLEGFEDRFVDQ-ISGGQQQRV 145
Cdd:COG4167  86 ckHIRMIFQdpNTSLNPRLNIG-------QILEEPlrlntdltAEEREERIFATLRLVGLLPEHANFYPHmLSSGQKQRV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 146 ALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238


                ...
gi 90111106 226 RQP 228
Cdd:COG4167 239 ANP 241

CeuD

COG4604

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

7-224

1.20e-43

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 151.00 E-value: 1.20e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVF 84
Cdd:COG4604   2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QSYALFPHMSLGENVGYGL----KmlGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG4604  82 QENHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223

COG4559

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

8-223

2.10e-42

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 147.95 E-value: 2.10e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICM-VF-Q 85
Cdd:COG4559   3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRaVLpQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYAL-FPhMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALI-------LKPKV 157
Cdd:COG4559  83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 158 LLFDEPLSNLD-ANLRRSMRdKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:COG4559 162 LFLDEPTSALDlAHQHAVLR-LARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

22-228

4.92e-42

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 149.09 E-value: 4.92e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR-----DICMVFQS--YALFPHMS 94
Cdd:PRK15079  37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   95 LGENVGYGLKML--GVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK15079 117 IGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  172 RRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253

ABC_cobalt_CbiO_domain2

cd03226

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

8-215

5.59e-42

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: 145.09 E-value: 5.59e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVtHRSIQQRDICMVFQS 86
Cdd:cd03226   1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 --YALFPHmSLGENVGYGLKMLGvpraELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:cd03226  80 vdYQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 165 SNLDanlRRSMR---DKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03226 155 SGLD---YKNMErvgELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204

heterocyst_DevA

TIGR02982

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...

7-215

8.99e-42

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: 145.16 E-value: 8.99e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNT----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ----- 77
Cdd:TIGR02982   2 ISIRNLNHYYGHGSlrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    78 RDICMVFQSYALFPHMSLGENVGYGLKML-GVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:TIGR02982  82 RRIGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106   157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDqSEAFAVSDTVLVMNKGHI 215
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219

ABCC_MsbA

cd03251

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

7-227

1.68e-41

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: 144.68 E-value: 1.68e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGS--NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICM 82
Cdd:cd03251   1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFpHMSLGENVGYGLkmLGVPRAELKARVKEALAMVDLEGFEDRFVDQI-------SGGQQQRVALARALILKP 155
Cdd:cd03251  81 VSQDVFLF-NDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIgergvklSGGQRQRIAIARALLKDP 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 156 KVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQ 226

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

8-231

2.01e-41

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 144.79 E-value: 2.01e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DIcmvf 84
Cdd:COG1137   5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI---- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 qSY-----ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG1137  81 -GYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 160 FDEPLSNLD----ANLRRSmrdkIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:COG1137 160 LDEPFAGVDpiavADIQKI----IRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230

PRK10619

histidine ABC transporter ATP-binding protein HisP;

2-240

2.49e-41

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.11 E-value: 2.49e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    2 TQKNFVELRnvtKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH--------- 72
Cdd:PRK10619   4 NKLNVIDLH---KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   73 -------RSIQQRdICMVFQSYALFPHMSLGENVGYG-LKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQ 143
Cdd:PRK10619  81 vadknqlRLLRTR-LTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  144 RVALARALILKPKVLLFDEPLSNLDANLrrsMRDKIRELQK--QFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSP 221
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPEL---VGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236

                        250
                 ....*....|....*....
gi 90111106  222 QDLYRQPASRFMASFMGDA 240
Cdd:PRK10619 237 EQLFGNPQSPRLQQFLKGS 255

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

8-223

2.51e-41

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 144.91 E-value: 2.51e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDicmvfQSY 87
Cdd:PRK13548   4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA-----RRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   88 ALFP-HMSLG------ENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALI------LK 154
Cdd:PRK13548  79 AVLPqHSSLSfpftveEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  155 PKVLLFDEPLSNLDanLR---RSMRdKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:PRK13548 159 PRWLLLDEPTSALD--LAhqhHVLR-LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227

ModF

COG1119

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

6-224

4.39e-41

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: 144.07 E-value: 4.39e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQ---IF---IDGEDVthRSIQQRd 79
Cdd:COG1119   3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDV--WELRKR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ICMVfqSYAL---FPHMSLGENV----GYGlkMLGVPR---AELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALAR 149
Cdd:COG1119  80 IGLV--SPALqlrFPRDETVLDVvlsgFFD--SIGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 150 ALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

2-213

6.45e-41

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.79 E-value: 6.45e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   2 TQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiqQRD-- 79
Cdd:COG3845   1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS--PRDai 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ---ICMVFQSYALFPHMSLGENVGYGL---KMLGVPRAELKARVKEALAM----VDLegfeDRFVDQISGGQQQRVALAR 149
Cdd:COG3845  79 algIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERygldVDP----DAKVEDLSVGEQQRVEILK 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 150 ALILKPKVLLFDEPLSNLD--------ANLRRsMRDKirelqkqfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:COG3845 155 ALYRGARILILDEPTAVLTpqeadelfEILRR-LAAE--------GKSIIFITHKLREVMAIADRVTVLRRG 217

cbiO

PRK13640

energy-coupling factor transporter ATPase;

5-228

1.13e-40

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 144.17 E-value: 1.13e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    5 NFVELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKP---SEGQIFIDGEDVTHRSIQQ-R 78
Cdd:PRK13640   4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDiR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 D-ICMVFQSY-ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:PRK13640  84 EkVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234

ABCC_ATM1_transporter

cd03253

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

7-224

1.93e-40

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: 141.98 E-value: 1.93e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTkrFGSNT---VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVthRSIQQ----RD 79
Cdd:cd03253   1 IEFENVT--FAYDPgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLdslrRA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ICMVFQSYALFpHMSLGENVGYGlkMLGVPRAELKARVKEALAMVDLEGFEDRFVDQ-------ISGGQQQRVALARALI 152
Cdd:cd03253  77 IGVVPQDTVLF-NDTIGYNIRYG--RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAIL 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

24-229

2.54e-40

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.24 E-value: 2.54e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   24 NINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIdGEDVTHRSIQQRD-------ICMVFQsyalFPHMSLG 96
Cdd:PRK13634  25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlkplrkkVGIVFQ----FPEHQLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   97 E-----NVGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
Cdd:PRK13634 100 EetvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  171 LRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

22-228

3.17e-40

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 143.95 E-value: 3.17e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH-----RSIQQRDICMVFQSyalfPHMSLG 96
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaQKLLRQKIQIVFQN----PYGSLN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   97 --ENVGYglkMLGVP--------RAELKARVKEALAMVDLEG-FEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK11308 107 prKKVGQ---ILEEPllintslsAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246

LolD_lipo_ex

TIGR02211

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

10-215

5.59e-40

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: 140.56 E-value: 5.59e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    10 RNVTKRF--GSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS------IQQRD 79
Cdd:TIGR02211   5 ENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSsnerakLRNKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:TIGR02211  85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106   160 FDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHI 215
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEMKDGQL 219

PRK13633

energy-coupling factor transporter ATPase;

4-227

2.30e-39

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 140.61 E-value: 2.30e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSN------TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS--- 74
Cdd:PRK13633   2 NEMIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlw 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   75 -IQQRdICMVFQSyalfPHMSL-----GENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALA 148
Cdd:PRK13633  82 dIRNK-AGMVFQN----PDNQIvativEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  149 RALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

7-228

5.44e-39

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 139.44 E-value: 5.44e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS---IQQRD-IC 81
Cdd:PRK13639   2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKtVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSY--ALFPHmSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK13639  82 IVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228

cbiO

PRK13642

energy-coupling factor transporter ATPase;

7-225

5.46e-39

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 139.46 E-value: 5.46e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNIN---LTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDIC 81
Cdd:PRK13642   5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSY-ALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK13642  85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228

ABC_MTABC3_MDL1_MDL2

cd03249

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

7-227

1.17e-38

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: 137.29 E-value: 1.17e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGS---NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDIC 81
Cdd:cd03249   1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFPhMSLGENVGYGLKmlGVPRAELKARVKEALAMVDLEGFEDRFvD--------QISGGQQQRVALARALIL 153
Cdd:cd03249  81 LVSQEPVLFD-GTIAENIRYGKP--DATDEEVEEAAKKANIHDFIMSLPDGY-DtlvgergsQLSGGQKQRIAIARALLR 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQ 227

YejF

COG4172

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

1-229

3.28e-38

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: 142.90 E-value: 3.28e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   1 MTQKNFVELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKT----TILRLVAGLEKPSEGQIFIDGEDVTH 72
Cdd:COG4172   1 MMSMPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  73 ------RSIQQRDICMVFQ--SYALFPHMSLGENVGYGLKM-LGVPRAELKARVKEALAMVDLEGFEDRFVD---QISGG 140
Cdd:COG4172  81 lserelRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDqseaFAV----SDTVLVMNKGHIM 216
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIV 236

                       250
                ....*....|...
gi 90111106 217 QIGSPQDLYRQPA 229
Cdd:COG4172 237 EQGPTAELFAAPQ 249

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

8-234

3.51e-38

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: 136.12 E-value: 3.51e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMVF 84
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    85 QSYALFPHMSLGENVGYGLKmlGVPRAElKARVKEALAMVD-LEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:TIGR03410  82 QGREIFPRLTVEENLLTGLA--ALPRRS-RKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106   164 LSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMA 234
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229

ABCC_Protease_Secretion

cd03246

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

8-215

1.14e-37

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: 132.73 E-value: 1.14e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVThrsiqqrdicmvfq 85
Cdd:cd03246   2 EVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALfphMSLGENVGYglkmlgVPRaelkarvkealamvDLEGFEDRFVDQI-SGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:cd03246  68 QWDP---NELGDHVGY------LPQ--------------DDELFSGSIAENIlSGGQRQRLGLARALYGNPRILVLDEPN 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111106 165 SNLDANLRRSMRDKIRELQKQfDITSLYVTHdQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173

fecE

PRK11231

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

11-223

9.70e-37

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 132.83 E-value: 9.70e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQrdicmVFQSYALF 90
Cdd:PRK11231   7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARRLALL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   91 P--HM-----SLGENVGYG----LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK11231  82 PqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQFDiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

7-228

1.02e-36

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.39 E-value: 1.02e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMV 83
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 FQSY--ALFPhMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK13652  84 FQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  162 EPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

11-231

1.25e-36

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 135.00 E-value: 1.25e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVidNINLTIPqGQMVT-LLGPSGCGKTTILRLVAGLEKPSEGQI------FIDGEDVTHRSIQQRDICMV 83
Cdd:PRK11144   5 NFKQQLGDLCL--TVNLTLP-AQGITaIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPEKRRIGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 FQSYALFPHMSLGENVGYGLKmlgvpraelKARVKEALAMVDLEGFE---DRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK11144  82 FQDARLFPHYKVRGNLRYGMA---------KSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223

ABC_NatA_like

cd03267

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

9-216

2.00e-36

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: 131.69 E-value: 2.00e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   9 LRNVTKR-FGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVF-Q 85
Cdd:cd03267  23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFgQ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111106 166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIM 216
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233

nickel_nikD

TIGR02770

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

22-230

2.37e-36

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: 131.34 E-value: 2.37e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKP----SEGQIFIDGEDVTHRSIQQRDICMVFQS--YALFPHMSL 95
Cdd:TIGR02770   2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    96 GENVGYGLKMLGVPRAELKARVKEALAMVDLEGFE---DRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:TIGR02770  82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106   173 RSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPAS 230
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

5-225

1.08e-35

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 131.12 E-value: 1.08e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    5 NFVELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE--DVTHRSIQQ--RD 79
Cdd:PRK13636   4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKlrES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   80 ICMVFQS--YALFPhMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13636  84 VGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

1-199

1.48e-35

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 129.06 E-value: 1.48e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT----HRSIQ 76
Cdd:PRK10247   2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIYRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   77 QRDICmvFQSYALFphmslGENVGYGLKMlgvPRAELKARVKEALAMVDLEGFE------DRFVDQISGGQQQRVALARA 150
Cdd:PRK10247  82 QVSYC--AQTPTLF-----GDTVYDNLIF---PWQIRNQQPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRN 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 90111106  151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSE 199
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200

livG

PRK11300

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

1-240

3.40e-35

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 128.95 E-value: 3.40e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKnFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS---IQQ 77
Cdd:PRK11300   1 MSQP-LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqIAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPHMSLGEN--------VGYGL-----KMLGVPRAELKA--RVKEALAMVDLEGFEDRFVDQISGGQQ 142
Cdd:PRK11300  80 MGVVRTFQHVRLFREMTVIENllvaqhqqLKTGLfsgllKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQ 222
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239

                        250
                 ....*....|....*...
gi 90111106  223 DLYRQPasRFMASFMGDA 240
Cdd:PRK11300 240 EIRNNP--DVIKAYLGEA 255

ABCC_bacteriocin_exporters

cd03245

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

7-215

3.46e-35

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: 127.71 E-value: 3.46e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT--HRSIQQRDICM 82
Cdd:cd03245   3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFpHMSLGENVgyglkMLGVPRAElKARVKEALAMVDLEGFE-------DRFV----DQISGGQQQRVALARAL 151
Cdd:cd03245  83 VPQDVTLF-YGTLRDNI-----TLGAPLAD-DERILRAAELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARAL 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106 152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHI 215
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216

type_I_sec_LssB

TIGR03375

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...

6-222

4.71e-35

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: 135.38 E-value: 4.71e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     6 FVELRNVTKRF-GSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT--HRSIQQRDIC 81
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPADLRRNIG 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    82 MVFQSYALFpHMSLGENVgyglkMLGVPRAElKARVKEALAMVDLEGFEDR----FVDQI-------SGGQQQRVALARA 150
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNI-----ALGAPYAD-DEEILRAAELAGVTEFVRRhpdgLDMQIgergrslSGGQRQAVALARA 615

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106   151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQ 222
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKD 684

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

7-224

6.33e-35

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.54 E-value: 6.33e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD-ICMVFQ 85
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK13537  88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225

CydD

TIGR02857

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

7-210

2.32e-34

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: 132.03 E-value: 2.32e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH--RSIQQRDICMV 83
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADadADSWRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    84 FQSYALFPHmSLGENVGYGLKmlGVPRAElkarVKEALAMVDLEGFE-------DRFVDQ----ISGGQQQRVALARALI 152
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARP--DASDAE----IREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLALARAFL 474

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106   153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSEAfAVSDTVLVM 210
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

21-237

3.14e-34

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 126.32 E-value: 3.14e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE------DVTH-RSIQQR-DICMVFQSYALFPH 92
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQiDAIKLRkEVGMVFQQPNPFPH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   93 MSLGENVGYGLKMLGVP-RAELKARVKEALAMVDL-EGFEDRF---VDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  168 DANLRRSMRDKIRELQKQfdITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFM 237
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

6-224

5.84e-34

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 129.19 E-value: 5.84e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMV 83
Cdd:PRK09536   3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 FQSYALFPHMSLGENVGYG----LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK09536  83 PQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226

LPS_export_lptB

TIGR04406

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...

10-231

9.87e-34

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]

Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 124.69 E-value: 9.87e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    10 RNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMVFQS 86
Cdd:TIGR04406   5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    87 YALFPHMSLGENVGYGLKMLG-VPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:TIGR04406  85 ASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106   166 NLDANLRRSMRDKIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVR 229

cbiO

PRK13644

energy-coupling factor transporter ATPase;

7-233

1.02e-33

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 125.48 E-value: 1.02e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ---RDICM 82
Cdd:PRK13644   2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQS-YALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK13644  82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  162 EPLSNLDANLRRSMRDKIRELQKQFDiTSLYVTHDQSEaFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFM 233
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

7-227

1.78e-33

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 124.04 E-value: 1.78e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF----------------------GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIF 64
Cdd:COG1134   5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  65 IDGEdVThrsiqqrdicmvfqsyALF-------PHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQI 137
Cdd:COG1134  85 VNGR-VS----------------ALLelgagfhPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTY 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQ 217
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226

                       250
                ....*....|...
gi 90111106 218 IGSPQD---LYRQ 227
Cdd:COG1134 227 DGDPEEviaAYEA 239

PRK10908

cell division ATP-binding protein FtsE;

7-215

5.19e-33

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 122.29 E-value: 5.19e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQ--QRDI 80
Cdd:PRK10908   2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPflRRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK10908  82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  161 DEPLSNLDANLrrsmRDKIRELQKQFD---ITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:PRK10908 162 DEPTGNLDDAL----SEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215

ABCC_Glucan_exporter_like

cd03254

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

6-224

6.05e-33

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: 122.33 E-value: 6.05e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   6 FVELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDG---EDVTHRSIQQRdIC 81
Cdd:cd03254   2 EIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRSM-IG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFPHmSLGENVgyglkMLGVPRAElKARVKEALAMVDLegfeDRFVDQ---------------ISGGQQQRVA 146
Cdd:cd03254  81 VVLQDTFLFSG-TIMENI-----RLGRPNAT-DEEVIEAAKEAGA----HDFIMKlpngydtvlgenggnLSQGERQLLA 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 147 LARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfdITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDEL 224

PRK09984

phosphonate ABC transporter ATP-binding protein;

4-222

6.40e-33

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.20 E-value: 6.40e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL---EKPSEGQIFIDGEDVTHRSIQQRDI 80
Cdd:PRK09984   2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 -------CMVFQSYALFPHMSLGENVGYGlkMLG-VP---------RAELKARVKEALAMVDLEGFEDRFVDQISGGQQQ 143
Cdd:PRK09984  82 rksrantGYIFQQFNLVNRLSVLENVLIG--ALGsTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  144 RVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQ 222
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

7-224

1.61e-32

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 123.79 E-value: 1.61e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS-IQQRDICMVFQ 85
Cdd:PRK13536  42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArLARARIGVVPQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGEN-VGYGlKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK13536 122 FDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  165 SNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259

PRK15112

peptide ABC transporter ATP-binding protein SapF;

7-240

1.97e-32

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 121.82 E-value: 1.97e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT---------VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE-----DVTH 72
Cdd:PRK15112   5 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   73 RSiqQRdICMVFQ--SYALFPHMSLGENVGYGLKM-LGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALA 148
Cdd:PRK15112  85 RS--QR-IRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  149 RALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241

                        250
                 ....*....|....*.
gi 90111106  229 ----ASRFMASFMGDA 240
Cdd:PRK15112 242 lhelTKRLIAGHFGEA 257

COG4586

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

22-216

2.05e-32

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 123.27 E-value: 2.05e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ-QRDICMVF-QSYALFPHMSLGENv 99
Cdd:COG4586  38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEfARRIGVVFgQRSQLWWDLPAIDS- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 100 gygLKML----GVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
Cdd:COG4586 117 ---FRLLkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 90111106 176 RDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIM 216
Cdd:COG4586 194 REFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

15-225

2.49e-32

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 121.65 E-value: 2.49e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   15 RFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE--DVTHRSIQ--QRDICMVFQ--SYA 88
Cdd:PRK13638  10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLalRQQVATVFQdpEQQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   89 LFpHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PRK13638  90 IF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  169 ANLRRSMRDKIRELQKQFDITSLyVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

7-228

3.26e-32

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 121.30 E-value: 3.26e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-----EKPSEGQIFIDGEDVTHRSIQ----Q 77
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNlnrlR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPhMSLGENVGYGLKMLG-VPRAELKARVKEALAMVDL-EGFEDRF---VDQISGGQQQRVALARALI 152
Cdd:PRK14258  88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwDEIKHKIhksALDLSGGQQQRLCIARALA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNK-----GHIMQIGSPQDLYRQ 227
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246


                 .
gi 90111106  228 P 228
Cdd:PRK14258 247 P 247

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

4-227

4.45e-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: 125.69 E-value: 4.45e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     4 KNFVELRNVTKRF-----GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFI----DGEDVTHRS 74
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    75 IQQRD-----ICMVFQSYALFPHMSLGENVgygLKMLGVPRAELKARVKeALAMVDLEGFE--------DRFVDQISGGQ 141
Cdd:TIGR03269 357 PDGRGrakryIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMK-AVITLKMVGFDeekaeeilDKYPDELSEGE 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSP 221
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512


                  ....*.
gi 90111106   222 QDLYRQ 227
Cdd:TIGR03269 513 EEIVEE 518

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

1-200

4.77e-32

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 119.88 E-value: 4.77e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ 76
Cdd:PRK10584   1 MPAENIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   77 QR------DICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARA 150
Cdd:PRK10584  81 ARaklrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90111106  151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEA 200
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210

PRK13549

xylose transporter ATP-binding subunit; Provisional

8-216

5.76e-32

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 125.04 E-value: 5.76e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLeKPS---EGQIFIDGEDVTHRSI---QQRDIC 81
Cdd:PRK13549   7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIrdtERAGIA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSYALFPHMSLGENVGYGLKMLGVPR---AELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:PRK13549  86 IIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  159 LFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG-HIM 216
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGrHIG 223

cbiO

PRK13649

energy-coupling factor transporter ATPase;

7-227

7.56e-32

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 7.56e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVID-----NINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS----IQQ 77
Cdd:PRK13649   3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 --RDICMVFQsyalFPHMSLGE-----NVGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALAR 149
Cdd:PRK13649  83 irKKVGLVFQ----FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  150 ALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQkQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

7-219

8.46e-32

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: 118.79 E-value: 8.46e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN----------------------TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIF 64
Cdd:cd03220   1 IELENVSKSYPTYkggssslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  65 IDGedvthrsiqqRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQR 144
Cdd:cd03220  81 VRG----------RVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 145 VALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224

PRK14243

phosphate transporter ATP-binding protein; Provisional

7-205

1.13e-31

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 119.89 E-value: 1.13e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILR-------LVAGLEkpSEGQIFIDGEDVTHRSIQ--- 76
Cdd:PRK14243  11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPDVDpve 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   77 -QRDICMVFQSYALFPHmSLGENVGYGLKMLG------------VPRAELKARVKEALAMVDLegfedrfvdQISGGQQQ 143
Cdd:PRK14243  89 vRRRIGMVFQKPNPFPK-SIYDNIAYGARINGykgdmdelversLRQAALWDEVKDKLKQSGL---------SLSGGQQQ 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  144 RVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDItsLYVTHDQSEAFAVSD 205
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSD 218

cbiO

PRK13646

energy-coupling factor transporter ATPase;

22-227

1.52e-31

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 119.88 E-value: 1.52e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH-------RSIQQRdICMVFQsyalFPHMS 94
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyiRPVRKR-IGMVFQ----FPESQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   95 LGEN-----VGYGLKMLGVPRAELKARVKEALamVDLeGFEDRFVD----QISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK13646  98 LFEDtvereIIFGPKNFKMNLDEVKNYAHRLL--MDL-GFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

5-224

4.17e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 4.17e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    5 NFVELRNVTKRFGSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDIC 81
Cdd:PRK13647   3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSY--ALFPhMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK13647  83 LVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

10-217

4.29e-31

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.61 E-value: 4.29e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   10 RNVTKRFG----SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS------IQQRD 79
Cdd:PRK11629   9 DNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaeLRNQK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK11629  89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTvLVMNKGHIMQ 217
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTA 225

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

7-229

6.62e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.18 E-value: 6.62e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT-----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFI---------DGEDVTH 72
Cdd:PRK13631  22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELIT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   73 RSIQQ---------RDICMVFQ--SYALFPHmSLGENVGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGG 140
Cdd:PRK13631 102 NPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGS 220
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259


                 ....*....
gi 90111106  221 PQDLYRQPA 229
Cdd:PRK13631 260 PYEIFTDQH 268

NHLM_micro_ABC2

TIGR03797

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

7-228

6.85e-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: 123.14 E-value: 6.85e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFG--SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICM 82
Cdd:TIGR03797 452 IEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGV 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    83 VFQSYALFPHmSLGENVGyGLKMLGVPRAElkarvkEALAMVDLEgfEDrfVDQ---------------ISGGQQQRVAL 147
Cdd:TIGR03797 532 VLQNGRLMSG-SIFENIA-GGAPLTLDEAW------EAARMAGLA--ED--IRAmpmgmhtvisegggtLSGGQRQRLLI 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   148 ARALILKPKVLLFDEPLSNLDaNLRRSMrdkIRELQKQFDITSLYVTHDQS---EAfavsDTVLVMNKGHIMQIGSPQDL 224
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALD-NRTQAI---VSESLERLKVTRIVIAHRLStirNA----DRIYVLDAGRVVQQGTYDEL 671


                  ....
gi 90111106   225 YRQP 228
Cdd:TIGR03797 672 MARE 675

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

11-239

8.80e-31

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.89 E-value: 8.80e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-EKPS----EGQIFIDGEDV-THRSIQQ--RDICM 82
Cdd:PRK14271  26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIfNYRDVLEfrRRVGM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQSYALFPhMSLGENVGYGLKMLG-VPRAELKARVKEALAMVDL-EGFEDRFVD---QISGGQQQRVALARALILKPKV 157
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQfdITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP----ASRFM 233
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYV 262


                 ....*.
gi 90111106  234 ASFMGD 239
Cdd:PRK14271 263 AGLSGD 268

PRK14239

phosphate transporter ATP-binding protein; Provisional

1-231

9.48e-31

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.18 E-value: 9.48e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKnFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-----EKPSEGQIFIDGEDVTHR-- 73
Cdd:PRK14239   1 MTEP-ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPrt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   74 -SIQQR-DICMVFQSYALFPhMSLGENVGYGLKMLGVP-RAELKARVKEALAMVDL-EGFEDRFVDQ---ISGGQQQRVA 146
Cdd:PRK14239  80 dTVDLRkEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  147 LARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFdiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYR 226
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236


                 ....*
gi 90111106  227 QPASR 231
Cdd:PRK14239 237 NPKHK 241

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

15-208

1.03e-30

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.02 E-value: 1.03e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   15 RFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGqifidgeDVTHRSiqQRDICMVFQSYAL---FP 91
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAG--GARVAYVPQRSEVpdsLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   92 hMSLGENVGYGL----KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:NF040873  72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 90111106  168 DANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVL 208
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190

type_I_sec_HlyB

TIGR01846

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

7-227

2.30e-30

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: 121.77 E-value: 2.30e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV--THRSIQQRDICM 82
Cdd:TIGR01846 456 ITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiADPAWLRRQMGV 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    83 VFQSYALFPHmSLGENVGYGLKMLGVPRAELKARVKEALAMVDL--EGFEDRFVDQ---ISGGQQQRVALARALILKPKV 157
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAKLAGAHDFISElpQGYNTEVGEKganLSGGQRQRIAIARALVGNPRI 614

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   158 LLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:TIGR01846 615 LIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLAL 681

3a01208

TIGR00958

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

7-228

2.90e-30

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.37 E-value: 2.90e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGS---NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQqRDI 80
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHHYLH-RQV 557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    81 CMVFQSYALFPHmSLGENVGYGLKMlgVPRAELKARVKEALAMVDLEGFE---DRFVD----QISGGQQQRVALARALIL 153
Cdd:TIGR00958 558 ALVGQEPVLFSG-SVRENIAYGLTD--TPDEEIMAAAKAANAHDFIMEFPngyDTEVGekgsQLSGGQKQRIAIARALVR 634

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106   154 KPKVLLFDEPLSNLDANLRRSmrdkIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704

ABC_Carb_Monos_II

cd03215

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

7-215

3.05e-30

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: 113.68 E-value: 3.05e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRfgsnTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD---ICMV 83
Cdd:cd03215   5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 ---FQSYALFPHMSLGENVgyglkmlgvpraelkarvkeALAmvdlegfedrfvDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03215  81 pedRKREGLVLDLSVAENI--------------------ALS------------SLLSGGNQQKVVLARWLARDPRVLIL 128

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 161 DEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182

ABCC_Hemolysin

cd03252

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

7-227

4.22e-30

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: 114.89 E-value: 4.22e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV--THRSIQQRDICM 82
Cdd:cd03252   1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalADPAWLRRQVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFpHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDL--EGFEDRFVDQ---ISGGQQQRVALARALILKPKV 157
Cdd:cd03252  81 VLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElpEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRI 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226

ATM1

COG5265

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

7-227

7.81e-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: 119.92 E-value: 7.81e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVtkRFG---SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVthRSIQQ----RD 79
Cdd:COG5265 358 VRFENV--SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDVTQaslrAA 433

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  80 ICMVFQSYALFpHMSLGENVGYGlkMLGVPRAElkarVKEALAMVDLEGFEDRFVDQI-----------SGGQQQRVALA 148
Cdd:COG5265 434 IGIVPQDTVLF-NDTIAYNIAYG--RPDASEEE----VEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIA 506

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 149 RALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQS---EAfavsDTVLVMNKGHIMQIGSPQDLY 225
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStivDA----DEILVLEAGRIVERGTHAELL 580


                ..
gi 90111106 226 RQ 227
Cdd:COG5265 581 AQ 582

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

5-236

1.13e-29

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 114.06 E-value: 1.13e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    5 NFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIfidgedvtHRSIQQRdICMVF 84
Cdd:PRK09544   3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   85 QSYALFPHMSLgeNVGYGLKMLGVPRaelKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK09544  74 QKLYLDTTLPL--TVNRFLRLRPGTK---KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  165 SNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNkGHIMQIGSPQDLYRQPasRFMASF 236
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217

PRK13651

cobalt transporter ATP-binding subunit; Provisional

7-223

1.84e-29

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.80 E-value: 1.84e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNT-----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQI---FIDGEDVT------- 71
Cdd:PRK13651   3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKktkekek 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   72 -----------HRSIQQ-----RDICMVFQ--SYALFpHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDR 132
Cdd:PRK13651  83 vleklviqktrFKKIKKikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  133 FVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNK 212
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240

                        250
                 ....*....|.
gi 90111106  213 GHIMQIGSPQD 223
Cdd:PRK13651 241 GKIIKDGDTYD 251

ArpD

COG4618

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

7-223

2.12e-29

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: 118.31 E-value: 2.12e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICM 82
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGY 410

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHmSLGENVGyglkMLGVPRAElkaRVKEALAMVDL--------EGFEDRfVDQ----ISGGQQQRVALARA 150
Cdd:COG4618 411 LPQDVELFDG-TIAENIA----RFGDADPE---KVVAAAKLAGVhemilrlpDGYDTR-IGEggarLSGGQRQRIGLARA 481

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELqKQFDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

7-215

2.50e-29

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: 117.62 E-value: 2.50e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS--EGQIFIDGEDVTHRSI---QQRDIC 81
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIrdtERAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    82 MVFQSYALFPHMSLGENVGYG----LKMLGVPRAELKARVKEALAMVDLEGFED-RFVDQISGGQQQRVALARALILKPK 156
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   157 VLLFDEPLSNLDANLRRSMRDKIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKG-HI 215
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGqHV 220

Uup

COG0488

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

9-196

3.86e-29

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 3.86e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   9 LRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGeDVThrsiqqrdICMVFQSYA 88
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR--------IGYLPQEPP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  89 LFPHMSLGENVGYGLKmlgvPRAELKARVKEALA------------------MVDLEGFE-------------------D 131
Cdd:COG0488  72 LDDDLTVLDTVLDGDA----ELRALEAELEELEAklaepdedlerlaelqeeFEALGGWEaearaeeilsglgfpeedlD 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106 132 RFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrDKIRELQ---KQFDITSLYVTHD 196
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLEeflKNYPGTVLVVSHD 208

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

8-216

5.68e-29

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 5.68e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH------RSIQQ 77
Cdd:PRK10535   6 ELKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLRR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK10535  86 EHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDiTSLYVTHDQSEAfAVSDTVLVMNKGHIM 216
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIV 222

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

7-236

7.06e-29

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 116.44 E-value: 7.06e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLE--KPSEGQI--------------------- 63
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    64 ---------------FIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEG 128
Cdd:TIGR03269  81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   129 FEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVL 208
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250       260
                  ....*....|....*....|....*...
gi 90111106   209 VMNKGHIMQIGSPQDLyrqpASRFMASF 236
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV----VAVFMEGV 264

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

8-170

8.66e-29

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: 110.14 E-value: 8.66e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV-THRSIQQRDICMVFQS 86
Cdd:TIGR01189   2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    87 YALFPHMSLGENVGYGLKMLGVPRAElkarVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:TIGR01189  82 PGLKPELSALENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157


                  ....
gi 90111106   167 LDAN 170
Cdd:TIGR01189 158 LDKA 161

CydC

TIGR02868

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

7-196

1.39e-28

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: 115.92 E-value: 1.39e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT--HRSIQQRDICMV 83
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSslDQDEVRRRVSVC 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    84 FQSYALFpHMSLGENVgyglkMLGVPRAElKARVKEALAMVDLEGFEDRFVD-----------QISGGQQQRVALARALI 152
Cdd:TIGR02868 415 AQDAHLF-DTTVRENL-----RLARPDAT-DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALL 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 90111106   153 LKPKVLLFDEPLSNLDANLRRSMrdkIRELQKQFD-ITSLYVTHD 196
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITHH 529

cbiO

PRK13641

energy-coupling factor transporter ATPase;

22-228

2.35e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.46 E-value: 2.35e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT----HRSIQ--QRDICMVFQsyalFPHMSL 95
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKklRKKVSLVFQ----FPEAQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   96 GEN-----VGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
Cdd:PRK13641  99 FENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  170 NLRRSMRDKIRELQKQFDiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

11-224

4.31e-28

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 4.31e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--RDICMVFQSYA 88
Cdd:PRK10253  12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNAT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   89 LFPHMSLGENVGYG----LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK10253  92 TPGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  165 SNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231

PRK11176

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

7-227

6.88e-28

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 114.35 E-value: 6.88e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF-GSNT-VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV---THRSIQQRdIC 81
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLASLRNQ-VA 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSYALFpHMSLGENVGYGLKMLgVPRAELKARVKEALAMVDLEGFEDRFVDQI-------SGGQQQRVALARALILK 154
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYARTEQ-YSREQIEEAARMAYAMDFINKMDNGLDTVIgengvllSGGQRQRIAIARALLRD 498

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106  155 PKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLAQ 568

cbiO

PRK13643

energy-coupling factor transporter ATPase;

16-227

8.23e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.21 E-value: 8.23e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   16 FGSNTVIDnINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ------RDICMVFQsyal 89
Cdd:PRK13643  17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQ---- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   90 FPHMSLGE-----NVGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:PRK13643  92 FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  164 LSNLDANLRRSMRdKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK13643 172 TAGLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

6-170

8.53e-28

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 107.58 E-value: 8.53e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVThrsiQQRDicmVFQ 85
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALF--------PHMSLGENVGYGLKMLGVPRAElkaRVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13538  74 QDLLYlghqpgikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150

                        170
                 ....*....|...
gi 90111106  158 LLFDEPLSNLDAN 170
Cdd:PRK13538 151 WILDEPFTAIDKQ 163

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

8-221

8.84e-28

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 108.62 E-value: 8.84e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEK--PSEGQIFIDGEDVTHRSIQQR---DICM 82
Cdd:COG0396   2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQ--------SYALFPHMSLGENVGYGLKMLgvpraELKARVKEALAMVDL-EGFEDRFVDQ-ISGGQQQRVALARALI 152
Cdd:COG0396  82 AFQypveipgvSVSNFLRTALNARRGEELSAR-----EFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLL 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQS-EAFAVSDTVLVMNKGHIMQIGSP 221
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRiLDYIKPDFVHVLVDGRIVKSGGK 225

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

7-214

9.46e-28

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: 105.61 E-value: 9.46e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGedvthrsiqqrdicmvfqs 86
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  87 yalfphmslGENVGYglkmlgvpraelkarvkealamvdlegfedrfVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03221  62 ---------TVKIGY--------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 90111106 167 LDANlrrsMRDKIRELQKQFDITSLYVTHDQseAF--AVSDTVLVMNKGH 214
Cdd:cd03221 101 LDLE----SIEALEEALKEYPGTVILVSHDR--YFldQVATKIIELEDGK 144

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

6-263

2.13e-27

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 112.31 E-value: 2.13e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIqqRD-----I 80
Cdd:PRK11288   4 YLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST--TAalaagV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQSYALFPHMSLGENVgyglkMLG--------VPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALI 152
Cdd:PRK11288  82 AIIYQELHLVPEMTVAENL-----YLGqlphkggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITsLYVTHDQSEAFAVSDTVLVMNKGhimqigspqdlyrqpasRF 232
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDG-----------------RY 218

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 90111106  233 MASFMGDANLFPATFSDGYV-----DIYGYHlPRPL 263
Cdd:PRK11288 219 VATFDDMAQVDRDQLVQAMVgreigDIYGYR-PRPL 253

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

7-237

2.40e-27

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.75 E-value: 2.40e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF-GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICMV 83
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVV 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 FQSYALFpHMSLGENVgyglkMLGVPRA---ELKARVKEALAMVDLEGFEDRFV-------DQISGGQQQRVALARALIL 153
Cdd:PRK13657 415 FQDAGLF-NRSIEDNI-----RVGRPDAtdeEMRAAAERAQAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARALLK 488

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQS---EAfavsDTVLVMNKGHIMQIGSPQDLYrQPAS 230
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLStvrNA----DRILVFDNGRVVESGSFDELV-ARGG 561

                        250
                 ....*....|.
gi 90111106  231 RFM----ASFM 237
Cdd:PRK13657 562 RFAallrAQGM 572

YddA

COG4178

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

7-213

2.43e-27

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.59 E-value: 2.43e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTV-IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFI-DGEDvthrsiqqrdicMVF 84
Cdd:COG4178 363 LALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR------------VLF 430

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 ---QSYalFPHMSLGENVGYGLKMLGVPRAELKarvkEALAMVDLEGFEDRFvDQI-------SGGQQQRVALARALILK 154
Cdd:COG4178 431 lpqRPY--LPLGTLREALLYPATAEAFSDAELR----EALEAVGLGHLAERL-DEEadwdqvlSLGEQQRLAFARLLLHK 503

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 155 PKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHdQSEAFAVSDTVLVMNKG 213
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGH-RSTLAAFHDRVLELTGD 559

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

8-213

3.65e-27

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: 106.75 E-value: 3.65e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRF-----GSNT--VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGE----DVTHRS-- 74
Cdd:COG4778   6 EVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASpr 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  75 ----IQQRDICMVFQsyalF----PHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEgfeDR--------FvdqiS 138
Cdd:COG4778  86 eilaLRRRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLP---ERlwdlppatF----S 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228

ABCG_EPDR

cd03213

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

20-213

4.58e-27

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: 105.33 E-value: 4.58e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  20 TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS--EGQIFIDGEDVTHRSIQQRdICMVFQSYALFPHMSLGE 97
Cdd:cd03213  23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  98 NVGYGlkmlgvprAELKarvkealamvdlegfedrfvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRD 177
Cdd:cd03213 102 TLMFA--------AKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 90111106 178 KIRELQKQfDITSLYVTHD-QSEAFAVSDTVLVMNKG 213
Cdd:cd03213 153 LLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQG 188

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

8-170

5.75e-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: 105.65 E-value: 5.75e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVThrsiQQRDIcmVFQSY 87
Cdd:cd03231   2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----FQRDS--IARGL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  88 ALFPHMSlgenvgyGLKMLGVPRAELK--------ARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:cd03231  76 LYLGHAP-------GIKTTLSVLENLRfwhadhsdEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148

                       170
                ....*....|.
gi 90111106 160 FDEPLSNLDAN 170
Cdd:cd03231 149 LDEPTTALDKA 159

ABCC_cytochrome_bd

cd03247

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

7-219

1.13e-26

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: 103.93 E-value: 1.13e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN--TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD-ICMV 83
Cdd:cd03247   1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 FQSYALFpHMSLGENVGyglkmlgvpraelkarvkealamvdlegfedrfvDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:cd03247  81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 164 LSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIG 219
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

11-224

1.15e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.75 E-value: 1.15e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR---DICMVFQSY 87
Cdd:PRK10895   8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQEA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   88 ALFPHMSLGENVGYGLKML-GVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PRK10895  88 SIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  167 LDAnlrRSMRD--KIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK10895 168 VDP---ISVIDikRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224

MglA

COG1129

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

8-215

1.15e-26

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 1.15e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRfgsnTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ---RDICMV- 83
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVp 333

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  84 --FQSYALFPHMSLGENVGYG-LKMLG----VPRAELKARVKEALAMVDLE-GFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:COG1129 334 edRKGEGLVLDLSIRENITLAsLDRLSrgglLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDP 413

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472

bacteriocin_ABC

TIGR01193

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

16-224

1.54e-26

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: 110.60 E-value: 1.54e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    16 FGSNtVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH--RSIQQRDICMVFQSYALFPHm 93
Cdd:TIGR01193 485 YGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidRHTLRQFINYLPQEPYIFSG- 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    94 SLGENVGYGLKMlGVPRAELKARVKEALAMVDLE----GFEDRFVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:TIGR01193 563 SILENLLLGAKE-NVSQDEIWAACEIAEIKDDIEnmplGYQTELSEEgssISGGQKQRIALARALLTDSKVLILDESTSN 641

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106   167 LDANLRRSMRDKIRELQkqfDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:TIGR01193 642 LDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

17-232

2.25e-26

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 2.25e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   17 GSNTVIDNINLTIPQGQMVTLLGPSGCGKTT----ILRLVAglekpSEGQIFIDGEDVTHRSIQQ-----RDICMVFQ-- 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdp 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENVGYGLKM--LGVPRAELKARVKEALAMVDLE-GFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRF 232
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521

Uup

COG0488

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

7-215

4.93e-26

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 4.93e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIdGEDVThrsI----QQRDicm 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---IgyfdQHQE--- 388

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 vfqsyALFPHMSLGENVGYGLKmlgvpraelKARVKEALAMvdLEGF----ED--RFVDQISGGQQQRVALARALILKPK 156
Cdd:COG0488 389 -----ELDPDKTVLDELRDGAP---------GGTEQEVRGY--LGRFlfsgDDafKPVGVLSGGEKARLALAKLLLSPPN 452

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 157 VLLFDEPLSNLDANlrrsMRDKIRELQKQFDITSLYVTHDqsEAF--AVSDTVLVMNKGHI 215
Cdd:COG0488 453 VLLLDEPTNHLDIE----TLEALEEALDDFPGTVLLVSHD--RYFldRVATRILEFEDGGV 507

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

8-227

7.33e-26

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: 102.61 E-value: 7.33e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLE--KPSEGQIFIDGEDVTHRSIQQR---DICM 82
Cdd:cd03217   2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPhmslgenvgyglkmlGVpraelkaRVKEALAMVDlEGFedrfvdqiSGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03217  82 AFQYPPEIP---------------GV-------KNADFLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILDE 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 163 PLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEA-FAVSDTVLVMNKGHIMQIGsPQDLYRQ 227
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSG-DKELALE 194

cbiO

PRK13645

energy-coupling factor transporter ATPase;

9-225

7.79e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.70 E-value: 7.79e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNT-----VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH--RSIQQ---- 77
Cdd:PRK13645   9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEvkrl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 -RDICMVFQ--SYALFPHmSLGENVGYGLKMLGVPRAELKARVKEALAMVDL-EGFEDRFVDQISGGQQQRVALARALIL 153
Cdd:PRK13645  89 rKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

21-215

8.30e-26

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: 103.12 E-value: 8.30e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL---EKPSEGQIFIDGEDVtHRSIQQRDICMVFQSYALFPHMSLGE 97
Cdd:cd03234  22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLTVRE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  98 NVGYGLKMLGVPRAELKARVKEA----LAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRVedvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 90111106 174 SMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222

PRK10575

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

9-228

1.31e-25

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 103.33 E-value: 1.31e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICMVFQS 86
Cdd:PRK10575  14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   87 YALFPHMSLGENVGYGL----KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK10575  94 LPAAEGMTVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106  163 PLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239

ABCC_TAP

cd03248

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

4-215

1.56e-25

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: 102.16 E-value: 1.56e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   4 KNFVELRNVT---KRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQq 77
Cdd:cd03248   9 KGIVKFQNVTfayPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyeHKYLH- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 RDICMVFQSYALFPHmSLGENVGYGLKmlGVPRAELKARVKEALAMVDLEGFEDRFVD-------QISGGQQQRVALARA 150
Cdd:cd03248  88 SKVSLVGQEPVLFAR-SLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARA 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHDQSeAFAVSDTVLVMNKGHI 215
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLS-TVERADQILVLDGGRI 226

PRK10261

glutathione transporter ATP-binding protein; Provisional

22-237

1.71e-25

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 107.25 E-value: 1.71e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ-----RDICMVFQS-YA-LFPHMS 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQT 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   95 LGENVGYGLKMLGVPRAELKA-RVKEALAMVDLEGFED-RFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  173 RSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFM 237
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

6-233

3.21e-25

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 3.21e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    6 FVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGED---VTHRSIQQRDICM 82
Cdd:PRK09700   5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQSYALFPHMSLGENVGYGL----KMLGVP---RAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK09700  85 IYQELSVIDELTVLENLYIGRhltkKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  156 KVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFM 233
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

7-227

3.69e-25

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 106.75 E-value: 3.69e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRSIQQRDIcmv 83
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarHRRAVCPRI--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 fqSYA-------LFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:NF033858  79 --AYMpqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTH---DQSEAFavsDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATaymEEAERF---DWLVAMDAGRVLATGTPAELLAR 227

PRK11160

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

7-224

6.17e-25

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.68 E-value: 6.17e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ-RD-ICM 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISV 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQSYALFPHmSLGENVgyglkMLGVPRAElKARVKEALAMVDLEGF--EDRFVD--------QISGGQQQRVALARALI 152
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNL-----LLAAPNAS-DEALIEVLQQVGLEKLleDDKGLNawlgeggrQLSGGEQRRLGIARALL 491

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560

PRK11174

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

23-228

7.36e-25

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 105.31 E-value: 7.36e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   23 DNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLeKPSEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFpHMSLGENVg 100
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTLRDNV- 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  101 yglkMLGVPRAElKARVKEALAMVDLEGFEDRFV--------DQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
Cdd:PRK11174 444 ----LLGNPDAS-DEQLQQALENAWVSEFLPLLPqgldtpigDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  170 NL-RRSMRDKIRELQKQfdiTSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK11174 519 HSeQLVMQALNAASRRQ---TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574

livF

PRK11614

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

3-216

8.99e-25

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 100.72 E-value: 8.99e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    3 QKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH---RSIQQRD 79
Cdd:PRK11614   2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   80 ICMVFQSYALFPHMSLGENVGYGlkMLGVPRAELKARVKEALAMVDlEGFEDRF--VDQISGGQQQRVALARALILKPKV 157
Cdd:PRK11614  82 VAIVPEGRRVFSRMTVEENLAMG--GFFAERDQFQERIKWVYELFP-RLHERRIqrAGTMSGGEQQMLAIGRALMSQPRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIM 216
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

7-196

9.48e-25

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: 105.02 E-value: 9.48e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIdGEDVTHRSI-QQRDicmvfq 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVdQSRD------ 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    86 syALFPHMSLGENVGYGLKMLGVPRAELKARvkealAMVDLEGF----EDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:TIGR03719 396 --ALDPNKTVWEEISGGLDIIKLGKREIPSR-----AYVGRFNFkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 90111106   162 EPLSNLDANLRRSMRDKIRElqkqFDITSLYVTHD 196
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLN----FAGCAVVISHD 499

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

1-224

1.36e-24

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 1.36e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS---IQQ 77
Cdd:PRK15439   6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALFPHMSLGENVGYGLkmlgvPR-AELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:PRK15439  86 LGIYLVPQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  157 VLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227

GguA

NF040905

sugar ABC transporter ATP-binding protein;

8-213

8.56e-24

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 101.79 E-value: 8.56e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLeKPS---EGQIFIDGEDVTHRSI---QQRDIC 81
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDIrdsEALGIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   82 MVFQSYALFPHMSLGENVgyglkMLGVPRA--------ELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALIL 153
Cdd:NF040905  82 IIHQELALIPYLSIAENI-----FLGNERAkrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215

type_I_sec_PrtD

TIGR01842

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

17-219

3.64e-23

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: 100.11 E-value: 3.64e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    17 GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH--RSIQQRDICMVFQSYALFPHmS 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdRETFGKHIGYLPQDVELFPG-T 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    95 LGENVGyglKMLGVPRAElkaRVKEA--LAMVD--LEGFEDRFVDQI-------SGGQQQRVALARALILKPKVLLFDEP 163
Cdd:TIGR01842 408 VAENIA---RFGENADPE---KIIEAakLAGVHelILRLPDGYDTVIgpggatlSGGQRQRIALARALYGDPKLVVLDEP 481

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106   164 LSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSeAFAVSDTVLVMNKGHIMQIG 219
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFG 535

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

8-224

4.88e-23

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 4.88e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVT-KRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVF-- 84
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyi 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 ----QSYALFPHMSLGENVgyglkMLGVPRAE---------LKARVKEALAMVdlEGF------EDRFVDQISGGQQQRV 145
Cdd:COG3845 339 pedrLGRGLVPDMSVAENL-----ILGRYRRPpfsrggfldRKAIRAFAEELI--EEFdvrtpgPDTPARSLSGGNQQKV 411

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 146 ALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

7-227

1.24e-22

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 1.24e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRD-ICMVFQ 85
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRrVGYMSQ 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAfAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAA 487

ABCC_MRP_domain2

cd03244

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

7-221

1.48e-22

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: 94.10 E-value: 1.48e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTI----LRLVagleKPSEGQIFIDGEDVTHRSIQQ--R 78
Cdd:cd03244   3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  79 DICMVFQSYALFPHmSLGENVG----YGLKML--GVPRAELKARVKEALAMVDLEGFEDRfvDQISGGQQQRVALARALI 152
Cdd:cd03244  79 RISIIPQDPVLFSG-TIRSNLDpfgeYSDEELwqALERVGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALL 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 153 LKPKVLLFDEPLSNLDANLRRSMRDKIRElqkQF-DITSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSP 221
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

10-227

1.66e-22

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.99 E-value: 1.66e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   10 RNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSI------QQR----- 78
Cdd:PRK11701  10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaERRrllrt 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 DICMVFQSYA--LFPHMSLGENVGYGLKMLGVpR--AELKARVKEALAMVDLEgfEDRFVDQ---ISGGQQQRVALARAL 151
Cdd:PRK11701  90 EWGFVHQHPRdgLRMQVSAGGNIGERLMAVGA-RhyGDIRATAGDWLERVEID--AARIDDLpttFSGGMQQRLQIARNL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG-------SPQDL 224
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGltdqvldDPQHP 246


                 ...
gi 90111106  225 YRQ 227
Cdd:PRK11701 247 YTQ 249

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

8-170

2.04e-22

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 2.04e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVT---HRS----IQQRDi 80
Cdd:PRK13539   4 EGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpdVAEachyLGHRN- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 cmvfqsyALFPHMSLGENVGYGLKMLGVPRaelkARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK13539  83 -------AMKPALTVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151

                        170
                 ....*....|
gi 90111106  161 DEPLSNLDAN 170
Cdd:PRK13539 152 DEPTAALDAA 161

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

22-228

2.23e-22

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 2.23e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKT----TILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR------DICMVFQS--YAL 89
Cdd:PRK11022  23 VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   90 FPHMSLGENVGYGLKM-LGVPRAELKARVKEALAMV---DLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106  166 NLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245

ABCC_MRP_domain1

cd03250

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

7-213

3.16e-22

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: 92.53 E-value: 3.16e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVT-----KRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEdvthrsiqqrdIC 81
Cdd:cd03250   1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  82 MVFQSYALFPhMSLGENVGYGLKMlgvpRAELKARVKEALAMV-DLEGFEDRfvDQ---------ISGGQQQRVALARAL 151
Cdd:cd03250  70 YVSQEPWIQN-GTIRENILFGKPF----DEERYEKVIKACALEpDLEILPDG--DLteigekginLSGGQKQRISLARAV 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106 152 ILKPKVLLFDEPLSNLDANLRRS-MRDKIRELQKQfDITSLYVTHdQSEAFAVSDTVLVMNKG 213
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLN-NKTRILVTH-QLQLLPHADQIVVLDNG 203

PRK10790

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

7-224

5.34e-22

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 97.10 E-value: 5.34e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGS-NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDG---EDVTHRSIQQrDICM 82
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRQ-GVAM 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQ-----SYALFPHMSLGENVGyglkmlgvpraelKARVKEALAMVDL--------EGFEDRFVDQ---ISGGQQQRVA 146
Cdd:PRK10790 420 VQQdpvvlADTFLANVTLGRDIS-------------EEQVWQALETVQLaelarslpDGLYTPLGEQgnnLSVGQKQLLA 486

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  147 LARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfdiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

7-221

5.36e-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: 97.39 E-value: 5.36e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106      7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDV-THRSIQQRDICMV 83
Cdd:TIGR01257  929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMC 1008

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     84 FQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106    164 LSNLDANLRRSMRDKIreLQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSP 221
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144

PRK10261

glutathione transporter ATP-binding protein; Provisional

22-229

8.99e-22

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.46 E-value: 8.99e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKT----TILRLV--AGLEKPSEG--------QIFIDGE--DVTHRSIQQRDICMVFQ 85
Cdd:PRK10261  32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKmllrrrsrQVIELSEqsAAQMRHVRGADMAMIFQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 S--YALFPHMSLGENVGYGLKM-LGVPRAELKARVKEALAMV---DLEGFEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

21-185

1.64e-21

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 90.78 E-value: 1.64e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH-RSIQQRDICMVFQSYALFPHMSLGENV 99
Cdd:PRK13540  16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  100 GYGLKMlgvprAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKI 179
Cdd:PRK13540  96 LYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170


                 ....*.
gi 90111106  180 RELQKQ 185
Cdd:PRK13540 171 QEHRAK 176

CP_lyasePhnK

TIGR02323

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...

11-227

3.13e-21

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: 91.43 E-value: 3.13e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQI-FIDGEDVTH----------RSIQQRD 79
Cdd:TIGR02323   8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELelyqlseaerRRLMRTE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    80 ICMVFQSYA--LFPHMSLGENVGYGLKMLGVPR-AELKARVKEALAMVDLEgfEDRFVDQ---ISGGQQQRVALARALIL 153
Cdd:TIGR02323  88 WGFVHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEID--PTRIDDLpraFSGGMQQRLQIARNLVT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIG-------SPQDLYR 226
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGltdqvldDPQHPYT 245


                  .
gi 90111106   227 Q 227
Cdd:TIGR02323 246 Q 246

PRK15056

manganese/iron ABC transporter ATP-binding protein;

12-219

3.61e-21

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 3.61e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   12 VTKRFGsNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDvTHRSIQQRDICMVFQSYAL-- 89
Cdd:PRK15056  14 VTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYVPQSEEVdw 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   90 -FPhmSLGENV----GYG-LKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:PRK15056  92 sFP--VLVEDVvmmgRYGhMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106  164 LSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVlVMNKGHIMQIG 219
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

7-215

4.01e-21

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 94.27 E-value: 4.01e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTV-IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICMV 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAV 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 FQSYALFPHMSLGENvgyglkmlGVPRAELKARVKEALAMVDLEGFED-RFVD-QISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK10522 403 FTDFHLFDQLLGPEG--------KPANPALVEKWLERLKMAHKLELEDgRISNlKLSKGQKKRLALLLALAEERDILLLD 474

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90111106  162 EPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSeAFAVSDTVLVMNKGHI 215
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQL 527

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

7-177

5.02e-21

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.03 E-value: 5.02e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIdGEDVTHRSI-QQRDicmvfq 85
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAYVdQSRD------ 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 syALFPHMSLGENVGYGLKMLGVPRAELKARvkealAMVDLEGF----EDRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK11819 398 --ALDPNKTVWEEISGGLDIIKVGNREIPSR-----AYVGRFNFkggdQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLD 470

                        170
                 ....*....|....*.
gi 90111106  162 EPLSNLDANLRRSMRD 177
Cdd:PRK11819 471 EPTNDLDVETLRALEE 486

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

17-229

1.16e-20

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.94 E-value: 1.16e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   17 GSNTVIDNINLTIPQGQMVTLLGPSGCGKT-TILRLVAGLEKPS--EGQIFIDGEDVTH------RSIQQRDICMVFQS- 86
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNlpekelNKLRAEQISMIFQDp 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   87 -YALFPHMSLGENVGYGLkML--GVPRAElkaRVKEALAMVD-LEGFEDR-----FVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVL-MLhkGMSKAE---AFEESVRMLDaVKMPEARkrmkmYPHEFSGGMRQRVMIAMALLCRPKL 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

19-229

1.65e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.46 E-value: 1.65e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   19 NTVIDNINLTIPQGQMVTLLGPSGCGKT----TILRLVaglekPS------EGQIFIDGEDVTH------RSIQQRDICM 82
Cdd:PRK15134  22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHaseqtlRGVRGNKIAM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   83 VFQSyalfPHMSLG-----ENVGYGLKML--GVPRAELKARVKEALAMVDLEGFEDRFVD---QISGGQQQRVALARALI 152
Cdd:PRK15134  97 IFQE----PMVSLNplhtlEKQLYEVLSLhrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALL 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPA 229
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249

PRK13543

heme ABC exporter ATP-binding protein CcmA;

10-168

6.67e-20

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 86.83 E-value: 6.67e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   10 RNVTKRFGSntvidnINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVThRSIQQRDICMVFQSYAL 89
Cdd:PRK13543  21 RNEEPVFGP------LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLPGL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   90 FPHMSLGENVGYglkMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARaLILKPKVL-LFDEPLSNLD 168
Cdd:PRK13543  94 KADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169

ABCD_peroxisomal_ALDP

cd03223

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

7-195

6.87e-20

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: 85.28 E-value: 6.87e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVT-KRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL--------EKPSEGQIFIdgedvthrsIQQ 77
Cdd:cd03223   1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLLF---------LPQ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  78 RdicmvfqsyalfPHMSLGenvgyglkmlgvpraelkaRVKEALA---MvdlegfedrfvDQISGGQQQRVALARALILK 154
Cdd:cd03223  72 R------------PYLPLG-------------------TLREQLIypwD-----------DVLSGGEQQRLAFARLLLHK 109

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 90111106 155 PKVLLFDEPLSNLDANLRRSMRDKIRELQkqfdITSLYVTH 195
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

22-231

1.16e-19

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.06 E-value: 1.16e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKT-----TILRLVAGLEKpSEGQIFIDGEDVTHRSIQQRDICMVFQS--YALFPHMS 94
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   95 LGENVGYGLKMLGVPRAElkARVKEALAMVDLEGFE---DRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK10418  98 MHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  172 RRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

24-215

1.34e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 1.34e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   24 NINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR-DICMVF-----QSYALFPHMSLGE 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   98 NV---GYGLKMLGVPRAELKARVKEALAMVDLE-GFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
Cdd:PRK15439 361 NVcalTHNRRGFWIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 90111106  174 SMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481

ABCC_NFT1

cd03369

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

7-221

2.02e-19

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: 85.16 E-value: 2.02e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN--TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICM 82
Cdd:cd03369   7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFphmslgenvgyglkmLGVPRAEL-------KARVKEALAMVdlEGFEDrfvdqISGGQQQRVALARALILKP 155
Cdd:cd03369  87 IPQDPTLF---------------SGTIRSNLdpfdeysDEEIYGALRVS--EGGLN-----LSQGQRQLLCLARALLKRP 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106 156 KVLLFDEPLSNLDANLRRSMRDKIRELQKqfDITSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSP 221
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

5-215

2.73e-19

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: 84.62 E-value: 2.73e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   5 NFVELRNVTKRFGSN----TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS---EGQIFIDGEDVTH-RSIQ 76
Cdd:cd03233   2 STLSWRNISFTTGKGrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGvpraelkarvkealamvdlegfeDRFVDQISGGQQQRVALARALILKPK 156
Cdd:cd03233  82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRAS 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106 157 VLLFDEPLSNLDANLRRSMRDKIRELQKQFDIT---SLYVTHDqsEAFAVSDTVLVMNKGHI 215
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtfvSLYQASD--EIYDLFDKVLVLYEGRQ 198

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

4-197

5.76e-19

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 5.76e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   4 KNF-VELRNVTKRfgsntVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVThrsiqqrdicm 82
Cdd:COG2401  32 EAFgVELRVVERY-----VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ----------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 vfqsyaLFPHMSLGENvgyglkmlgVPRAELKARVKEALAMVdleGFED-----RFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG2401  96 ------FGREASLIDA---------IGRKGDFKDAVELLNAV---GLSDavlwlRRFKELSTGQKFRFRLALLLAERPKL 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 90111106 158 LLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQ 197
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197

BtuD

COG4138

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

25-223

6.72e-19

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

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 6.72e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  25 INLTIPQGQMVTLLGPSGCGKTTILRLVAGLEkPSEGQIFIDGEDVTHRSIQQ--RDICM------------VFQSYALf 90
Cdd:COG4138  15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYlsqqqsppfampVFQYLAL- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  91 pHMSLGENVGYGLKMLgvpraelkARVKEALAMVDLEGfedRFVDQISGGQQQRVALARALI-------LKPKVLLFDEP 163
Cdd:COG4138  93 -HQPAGASSEAVEQLL--------AQLAEALGLEDKLS---RPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 164 LSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219

PvdE

COG4615

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

8-215

9.08e-19

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: 87.16 E-value: 9.08e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   8 ELRNVTKRF-----GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ-RD-I 80
Cdd:COG4615 329 ELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQlF 408

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  81 CMVFQSYALFPHmslgenvgyglkMLGVPRAELKARVKEALAMVDLEG---FED-RFVD-QISGGQQQRVALARALILKP 155
Cdd:COG4615 409 SAVFSDFHLFDR------------LLGLDGEADPARARELLERLELDHkvsVEDgRFSTtDLSQGQRKRLALLVALLEDR 476

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106 156 KVLLFDEPLSNLDANLRRSM-RDKIRELQKQfDITSLYVTHDQSeAFAVSDTVLVMNKGHI 215
Cdd:COG4615 477 PILVFDEWAADQDPEFRRVFyTELLPELKAR-GKTVIAISHDDR-YFDLADRVLKMDYGKL 535

3a01204

TIGR00955

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

32-224

2.51e-18

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 2.51e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    32 GQMVTLLGPSGCGKTTIL-----RLVAGLEKpsEGQIFIDGEDVTHRSIQQRDiCMVFQSYALFPHMSLGENVGYG--LK 104
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQahLR 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   105 M-LGVPRAELKARVKEALAMVDLE-------GFEDRfVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
Cdd:TIGR00955 128 MpRRVTKKEKRERVDEVLQALGLRkcantriGVPGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 90111106   177 DKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:TIGR00955 207 QVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254

cyc_pep_trnsptr

TIGR01194

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...

25-217

2.95e-18

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]

Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 85.78 E-value: 2.95e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    25 INLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ-RDI-CMVFQSYALF---------PHM 93
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyRDLfSAIFADFHLFddligpdegEHA 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    94 SLGENVGYglkmlgVPRAELKARVKealamvdLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
Cdd:TIGR01194 441 SLDNAQQY------LQRLEIADKVK-------IEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKR 507

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 90111106   174 SMRDKIRELQKQFDITSLYVTHDqSEAFAVSDTVLVMNKGHIMQ 217
Cdd:TIGR01194 508 FFYEELLPDLKRQGKTIIIISHD-DQYFELADQIIKLAAGCIVK 550

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

18-229

5.00e-18

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.57 E-value: 5.00e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   18 SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAG-LEKPSE-------GQIFIDGEDVTH---RSIQQRDICMVFQS 86
Cdd:PRK13547  13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAidaPRLARLRAVLPQAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   87 YALFPhMSLGENVGYGLKMLGVPRAELKARVKE----ALAMVDLEGFEDRFVDQISGGQQQRVALARAL---------IL 153
Cdd:PRK13547  93 QPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106  154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRqPA 229
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PA 246

PRK10789

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

18-228

6.00e-18

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.76 E-value: 6.00e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   18 SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSL 95
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TV 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   96 GENVGyglkmLGVPRAElKARVKEA--LAMV--DL----EGFE----DRFVdQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:PRK10789 406 ANNIA-----LGRPDAT-QQEIEHVarLASVhdDIlrlpQGYDtevgERGV-MLSGGQKQRISIARALLLNAEILILDDA 478

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  164 LSNLDANLRRSMRDKIRELQKQFdiTSLYVTHDQSeAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540

MRP_assoc_pro

TIGR00957

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

22-237

1.21e-17

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: 84.23 E-value: 1.21e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     22 IDNINLTIPQGQMVTLLGPSGCGKTTILR-LVAGLEKpSEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVG 100
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENIL 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    101 YGlKMLGVPRAElkaRVKEALAMV-DLE----GFEDRFVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:TIGR00957  721 FG-KALNEKYYQ---QVLEACALLpDLEilpsGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106    173 RSMRDKIRELQKQF-DITSLYVTHDQSEAFAVsDTVLVMNKGHIMQIGSPQDLYRQPASrfMASFM 237
Cdd:TIGR00957  797 KHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGA--FAEFL 859

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

28-235

6.57e-17

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: 78.99 E-value: 6.57e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  28 TIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiQQRDICMVFQSYALFphMSLGENVGyglkmlg 107
Cdd:cd03237  21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-QYIKADYEGTVRDLL--SSITKDFY------- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 108 vPRAELKARVKEALAmvdLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANlRRSMRDK-IRELQKQF 186
Cdd:cd03237  91 -THPYFKTEIAKPLQ---IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKvIRRFAENN 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111106 187 DITSLYVTHDQSEAFAVSDTVLVMN--KGHIMQIGSPQDLyRQPASRFMAS 235
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVFEgePSVNGVANPPQSL-RSGMNRFLKN 215

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

8-215

8.85e-17

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.02 E-value: 8.85e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     8 ELRNVTKRFGSNTVI---DNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-EKPSEGQIFIDGEDVTHRSIQQ---RDI 80
Cdd:TIGR02633 259 EARNLTCWDVINPHRkrvDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGI 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    81 CMVFQS---YALFPHMSLGENV------GYGLKMLGVPRAELKArVKEALAMVDLEGFE-DRFVDQISGGQQQRVALARA 150
Cdd:TIGR02633 339 AMVPEDrkrHGIVPILGVGKNItlsvlkSFCFKMRIDAAAELQI-IGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKM 417

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106   151 LILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

3-223

1.56e-16

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 1.56e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    3 QKNFVELRNVTKRfgSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS---IQQRD 79
Cdd:PRK09700 262 HETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldAVKKG 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   80 ICMVFQSY---ALFPHMSLGENV---------GYGLKM-LGVPRAELK-ARVKEALAMVDLEGFEDRfVDQISGGQQQRV 145
Cdd:PRK09700 340 MAYITESRrdnGFFPNFSIAQNMaisrslkdgGYKGAMgLFHEVDEQRtAENQRELLALKCHSVNQN-ITELSGGNQQKV 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106  146 ALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495

PRK13549

xylose transporter ATP-binding subunit; Provisional

8-215

1.71e-16

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 1.71e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNT---VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL-EKPSEGQIFIDGEDVTHRSIQQ---RDI 80
Cdd:PRK13549 261 EVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGI 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   81 CMVFQS---YALFPHMSLGENVG-------YGLKMLGVPrAELKA--------RVKEALAMVDlegfedrfVDQISGGQQ 142
Cdd:PRK13549 341 AMVPEDrkrDGIVPVMGVGKNITlaaldrfTGGSRIDDA-AELKTilesiqrlKVKTASPELA--------IARLSGGNQ 411

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111106  143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483

MRP_assoc_pro

TIGR00957

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

7-227

1.82e-16

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 80.76 E-value: 1.82e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106      7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICM 82
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdlRFKITI 1364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     83 VFQSYALFP---HMSLG-------ENVGYGLKMlgvprAELKARVKEALAMVDLEGFEDRfvDQISGGQQQRVALARALI 152
Cdd:TIGR00957 1365 IPQDPVLFSgslRMNLDpfsqysdEEVWWALEL-----AHLKTFVSALPDKLDHECAEGG--ENLSVGQRQLVCLARALL 1437

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106    153 LKPKVLLFDEPLSNLDANLRRSMRDKIRelqKQF-DITSLYVTHDQSEAFAVSdTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIR---TQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509

PLN03211

ABC transporter G-25; Provisional

11-223

1.91e-16

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 1.91e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS--EGQIFIDGEDVTHRSIqqRDICMVFQSYA 88
Cdd:PLN03211  73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL--KRTGFVTQDDI 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   89 LFPHMSLGENVGYgLKMLGVPRA---ELKARVKEA----LAMVDLEG--FEDRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PLN03211 151 LYPHLTVRETLVF-CSLLRLPKSltkQEKILVAESviseLGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  160 FDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQD 223
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

12-210

2.28e-16

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: 77.79 E-value: 2.28e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  12 VTKRFGSNTVIDNiNLTIPQ-GQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIfiDGEDvthrsiQQRDICMVFQSYAL- 89
Cdd:cd03236   6 PVHRYGPNSFKLH-RLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPP------DWDEILDEFRGSELq 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  90 --FPHMsLGENVGYGLKMLGV---PRAeLKARVKEALAMVD-------------LEGFEDRFVDQISGGQQQRVALARAL 151
Cdd:cd03236  77 nyFTKL-LEGDVKVIVKPQYVdliPKA-VKGKVGELLKKKDergkldelvdqleLRHVLDRNIDQLSGGELQRVAIAAAL 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 152 ILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVM 210
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212

PRK10762

D-ribose transporter ATP binding protein; Provisional

8-213

8.10e-16

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 8.10e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTH---RSIQQRDICMVF 84
Cdd:PRK10762   6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFngpKSSQEAGIGIIH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   85 QSYALFPHMSLGENVGYGL----KMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK10762  86 QELNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

21-198

8.96e-16

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: 78.25 E-value: 8.96e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGL--------EKPSEGQIFIdgedvthrsIQQRdicmvfqsyalfPH 92
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY---------VPQR------------PY 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    93 MSLG---ENVGY-----GLKMLGVPRAELkarvKEALAMVDLEGFEDR---------FVDQISGGQQQRVALARALILKP 155
Cdd:TIGR00954 526 MTLGtlrDQIIYpdsseDMKRRGLSDKDL----EQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKP 601

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 90111106   156 KVLLFDEPLSNLDANlrrsMRDKIRELQKQFDITSLYVTHDQS 198
Cdd:TIGR00954 602 QFAILDECTSAVSVD----VEGYMYRLCREFGITLFSVSHRKS 640

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

26-210

2.62e-15

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.75 E-value: 2.62e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  26 NLTIPQ-GQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIfidGEDVTHRSIQQRdicmvFQSYALFPHmslgenvgygLK 104
Cdd:COG1245  92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLKR-----FRGTELQDY----------FK 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 105 ML---------------GVPRAeLKARVKEALAMVD-------------LEGFEDRFVDQISGGQQQRVALARALILKPK 156
Cdd:COG1245 154 KLangeikvahkpqyvdLIPKV-FKGTVRELLEKVDergkldelaeklgLENILDRDISELSGGELQRVAIAAALLRDAD 232

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 157 VLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVM 210
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

9-196

2.75e-15

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.90 E-value: 2.75e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     9 LRNVTKRFGSN-TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDgEDVThrsiqqrdICMVFQSY 87
Cdd:TIGR03719   7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK--------VGYLPQEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    88 ALFPHMSLGENVGYGLK--------------MLGVPRAEL------KARVKEALAMVDLEGFE---------------DR 132
Cdd:TIGR03719  78 QLDPTKTVRENVEEGVAeikdaldrfneisaKYAEPDADFdklaaeQAELQEIIDAADAWDLDsqleiamdalrcppwDA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106   133 FVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN----LRRSMRDkirelqkqFDITSLYVTHD 196
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE--------YPGTVVAVTHD 217

PRK10762

D-ribose transporter ATP binding protein; Provisional

22-215

3.17e-15

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 3.17e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQR-DICMVFQSY-----ALFPHMSL 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   96 GENVGY-GLKMLGVPRAELKARvKEALAMVDlegFEDRF------VDQI----SGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK10762 348 KENMSLtALRYFSRAGGSLKHA-DEQQAVSD---FIRLFniktpsMEQAigllSGGNQQKVAIARGLMTRPKVLILDEPT 423

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90111106  165 SNLDANLRRSMRDKIRELqKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473

ycf16

CHL00131

sulfate ABC transporter protein; Validated

1-220

6.50e-15

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.52 E-value: 6.50e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    1 MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGleKPS----EGQIFIDGEDVTHRSIQ 76
Cdd:CHL00131   2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   77 QRD---ICMVFQ--------SYALFPHMSLGENvgygLKMLGVPRA---ELKARVKEALAMVDL-EGFEDRFVDQ-ISGG 140
Cdd:CHL00131  80 ERAhlgIFLAFQypieipgvSNADFLRLAYNSK----RKFQGLPELdplEFLEIINEKLKLVGMdPSFLSRNVNEgFSGG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQS-EAFAVSDTVLVMNKGHIMQIG 219
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRlLDYIKPDYVHVMQNGKIIKTG 234


                 .
gi 90111106  220 S 220
Cdd:CHL00131 235 D 235

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

9-213

1.02e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 1.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ---RDICMVFQ 85
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   86 SYALFPHMSLGENV---GYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK10982  81 ELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90111106  163 PLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKG 213
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210

40850658_otr

NF000106

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

4-231

2.61e-14

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.85 E-value: 2.61e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTiLRLVAGLEKPSEGQ------IFIDGEDVTHRSIQQ 77
Cdd:NF000106  11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRrpwrf*TWCANRRALRRTIG* 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   78 RDICMVFQSYALfphmSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKV 157
Cdd:NF000106  90 HRPVR*GRRESF----SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASR 231
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR 238

PLN03130

ABC transporter C family member; Provisional

24-224

2.89e-14

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.00 E-value: 2.89e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    24 NINLTIPQGQMVTLLGPSGCGKTTILRLVAGlEKP--SEGQIFIDGEdvthrsiqqrdICMVFQSYALFpHMSLGENVGY 101
Cdd:PLN03130  635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPprSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   102 GLKmLGVPRAELKARVK------EALAMVDLEGFEDRFVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
Cdd:PLN03130  702 GSP-FDPERYERAIDVTalqhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 90111106   176 RDKI--RELQKQfdiTSLYVThDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:PLN03130  780 FDKCikDELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

22-227

4.26e-14

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.00 E-value: 4.26e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHMSLGENVGY 101
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIEL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  102 GLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRE 181
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 90111106  182 LQKQFDiTSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL---YRQ 227
Cdd:PRK13545 189 FKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVvdhYDE 236

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

26-210

6.89e-14

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 6.89e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   26 NLTIPQ-GQMVTLLGPSGCGKTTILRLVAGLEKPSEGQifiDGEDVTHRSIQQRDICMVFQSYalFPHMSLGE-NVGYGL 103
Cdd:PRK13409  92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSWDEVLKRFRGTELQNY--FKKLYNGEiKVVHKP 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  104 KMLG-VPRAeLKARVKEALAMVD-------------LEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
Cdd:PRK13409 167 QYVDlIPKV-FKGKVRELLKKVDergkldevverlgLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 90111106  170 NLRRSMRDKIRELQKqfDITSLYVTHDQSEAFAVSDTVLVM 210
Cdd:PRK13409 246 RQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284

ABCC_SUR1_N

cd03290

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

16-213

8.09e-14

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: 69.67 E-value: 8.09e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  16 FGSN-TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQ-SYA----L 89
Cdd:cd03290  10 WGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAaqkpW 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  90 FPHMSLGENVGYGLKMlgvPRAELKArVKEALAM---VDLEGFED------RFVDqISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03290  90 LLNATVEENITFGSPF---NKQRYKA-VTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFL 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 161 DEPLSNLDANLRRS-MRDKIRELQKQFDITSLYVTHdQSEAFAVSDTVLVMNKG 213
Cdd:cd03290 165 DDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217

PLN03232

ABC transporter C family member; Provisional

15-241

1.05e-13

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 1.05e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    15 RFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPH 92
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlRRVLSIIPQSPVLFSG 1324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    93 M------SLGENVGYGLkMLGVPRAELKARVKEALAMVDLEGFEDRfvDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PLN03232 1325 TvrfnidPFSEHNDADL-WEALERAHIKDVIDRNPFGLDAEVSEGG--ENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106   167 LDANLRRSMRDKIRElqkQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRF--MASFMGDAN 241
Cdd:PLN03232 1402 VDVRTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFfrMVHSTGPAN 1475

PLN03232

ABC transporter C family member; Provisional

18-226

1.07e-13

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 1.07e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    18 SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEgqifidgedvthrsiqqrDICMVFQ-SYALFPHMS-- 94
Cdd:PLN03232  629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE------------------TSSVVIRgSVAYVPQVSwi 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    95 ----LGENVGYGLKMlgvpRAELKARVKEALAMV-DLEGFEDRFVDQI-------SGGQQQRVALARALILKPKVLLFDE 162
Cdd:PLN03232  691 fnatVRENILFGSDF----ESERYWRAIDVTALQhDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDD 766

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106   163 PLSNLDANLRRSMRDKI--RELQKQfdiTSLYVThDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYR 226
Cdd:PLN03232  767 PLSALDAHVAHQVFDSCmkDELKGK---TRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

9-196

1.18e-13

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 1.18e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    9 LRNVTKRFGSNTVI-DNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDgEDVThrsiqqrdICMVFQSY 87
Cdd:PRK11819   9 MNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK--------VGYLPQEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   88 ALFPHMSLGENVgyglkMLGVprAELKARVKE----------------ALA--MVDLE-------GFE-DRFVDQ----- 136
Cdd:PRK11819  80 QLDPEKTVRENV-----EEGV--AEVKAALDRfneiyaayaepdadfdALAaeQGELQeiidaadAWDlDSQLEIamdal 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  137 -----------ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN----LRRSMRDkirelqkqFDITSLYVTHD 196
Cdd:PRK11819 153 rcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQFLHD--------YPGTVVAVTHD 219

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

3-224

1.47e-13

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.97 E-value: 1.47e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106      3 QKNFVELRNVTKRFG--SNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVThrsiqqRDI 80
Cdd:TIGR01257 1934 KTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------TNI 2007

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     81 CMVFQSYALFPHMSLGENVGYGLKML-------GVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALIL 153
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106    154 KPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLyVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157

PRK03695

vitamin B12-transporter ATPase; Provisional

25-228

1.62e-13

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 1.62e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   25 INLTIPQGQMVTLLGPSGCGKTTILRLVAGLeKPSEGQIFIDGEDVT---------HR---SIQQRD-ICM-VFQSYALf 90
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEawsaaelarHRaylSQQQTPpFAMpVFQYLTL- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   91 pHMSLGENVGYGLKMLGvpraelkaRVKEALAMVDLEGfedRFVDQISGGQQQRVALARALI-----LKP--KVLLFDEP 163
Cdd:PRK03695  93 -HQPDKTRTEAVASALN--------EVAEALGLDDKLG---RSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  164 LSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224

PTZ00265

multidrug resistance protein (mdr1); Provisional

59-211

2.39e-13

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 2.39e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    59 SEGQIFIDGEDVTHRSIQQ-RDI-CMVFQSYALFpHMSLGENVGYGLKmlGVPRAELKARVKeaLAMVD--LEGFEDRFV 134
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFGKE--DATREDVKRACK--FAAIDefIESLPNKYD 1349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   135 DQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHdQSEAFAVSDTV 207
Cdd:PTZ00265 1350 TNVgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKI 1428


                  ....
gi 90111106   208 LVMN 211
Cdd:PTZ00265 1429 VVFN 1432

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

25-215

4.77e-13

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 4.77e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   25 INLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRS----IQQRdicMVF-----QSYALFPHMSL 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdaIRAG---IMLcpedrKAEGIIPVHSV 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   96 GENVGYGLKMLGVPRAELKARVKEA-LAmvdlegfeDRFVDQ--------------ISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK11288 349 ADNINISARRHHLRAGCLINNRWEAeNA--------DRFIRSlniktpsreqlimnLSGGNQQKAILGRWLSEDMKVILL 420

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  161 DEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHI 215
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474

ABCC_CFTR2

cd03289

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

7-224

4.79e-13

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: 68.34 E-value: 4.79e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTI----LRLVAglekpSEGQIFIDGEDVTHRSIQQ--R 78
Cdd:cd03289   3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKwrK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  79 DICMVFQSYALFPHmSLGENvgygLKMLGVPRAELKARVKEAlamVDLEGFEDRFVDQ-----------ISGGQQQRVAL 147
Cdd:cd03289  78 AFGVIPQKVFIFSG-TFRKN----LDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106 148 ARALILKPKVLLFDEPLSNLDANLRRSMRdkiRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223

PRK11147

ABC transporter ATPase component; Reviewed

16-198

8.02e-13

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 8.02e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   16 FGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRsIQQ---RDIC-MVF------- 84
Cdd:PRK11147  13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVAR-LQQdppRNVEgTVYdfvaegi 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   85 --QSYAL--FPHMSLGENVGYGLKMLgvprAELkARVKEALAMVDLEGFEDRFVD--------------QISGGQQQRVA 146
Cdd:PRK11147  92 eeQAEYLkrYHDISHLVETDPSEKNL----NEL-AKLQEQLDHHNLWQLENRINEvlaqlgldpdaalsSLSGGWLRKAA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  147 LARALILKPKVLLFDEPLSNLDAnlrrsmrDKIRELQ---KQFDITSLYVTHDQS 198
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEgflKTFQGSIIFISHDRS 214

PTZ00265

multidrug resistance protein (mdr1); Provisional

7-211

9.84e-13

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 9.84e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVtkRFGSNTVID-----NINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFI-DGEDVTHRSIQ--QR 78
Cdd:PTZ00265  383 IQFKNV--RFHYDTRKDveiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRS 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    79 DICMVFQSYALFPHmSLGENVGYGLKML------------------------GVPRAELKARVKEALAMVDLEG------ 128
Cdd:PTZ00265  461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLkdlealsnyynedgndsqenknkrNSCRAKCAGDLNDMSNTTDSNEliemrk 539

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   129 -------------------------FEDRF-------VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
Cdd:PTZ00265  540 nyqtikdsevvdvskkvlihdfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 90111106   177 DKIRELQKQFDITSLYVTHDQSeAFAVSDTVLVMN 211
Cdd:PTZ00265  620 KTINNLKGNENRITIIIAHRLS-TIRYANTIFVLS 653

TOBE_2

pfam08402

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...

273-344

2.28e-12

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: 61.87 E-value: 2.28e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106   273 VGVRPEAITLSDrGEESQRCVIRHVAYMGPQYEVTVEWHGQEILL--QVNATRLQPDVGEQYYLEIHPYGMFVL 344
Cdd:pfam08402   1 LAIRPEKIRLAA-AANGLSGTVTDVEYLGDHTRYHVELAGGEELVvrVPNAHARPPAPGDRVGLGWDPEDAHVL 73

SapD

COG4170

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

21-228

3.84e-12

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.47 E-value: 3.84e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS----EGQIFIDGEDVTHRSIQQR------DICMVFQ--SYA 88
Cdd:COG4170  22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSC 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  89 LFPHMSLGENVgyglkMLGVPRAELK--------ARVKEALAMVDLEGFEDR------FVDQISGGQQQRVALARALILK 154
Cdd:COG4170 102 LDPSAKIGDQL-----IEAIPSWTFKgkwwqrfkWRKKRAIELLHRVGIKDHkdimnsYPHELTEGECQKVMIAMAIANQ 176

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 155 PKVLLFDEPLSNLDAN-----LRrsMRDKIRELQKqfdITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQP 228
Cdd:COG4170 177 PRLLIADEPTNAMESTtqaqiFR--LLARLNQLQG---TSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250

PRK15093

peptide ABC transporter ATP-binding protein SapD;

7-236

1.52e-11

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 1.52e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRF----GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKP----SEGQIFIDGEDVTHRSIQQR 78
Cdd:PRK15093   4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 ------DICMVFQSyalfPHMSL--GENVGYGLkMLGVPRAELKA--------RVKEALAMVDLEGFEDR------FVDQ 136
Cdd:PRK15093  84 rklvghNVSMIFQE----PQSCLdpSERVGRQL-MQNIPGWTYKGrwwqrfgwRKRRAIELLHRVGIKDHkdamrsFPYE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIM 216
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238

                        250       260
                 ....*....|....*....|....*..
gi 90111106  217 QIGSPQDL-------YRQPASRFMASF 236
Cdd:PRK15093 239 ETAPSKELvttphhpYTQALIRAIPDF 265

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

29-241

1.63e-11

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: 62.20 E-value: 1.63e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  29 IPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSiqqrdicmvfqsyalfphmslgenvgyglkmlgv 108
Cdd:cd03222  22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP---------------------------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 109 praelkarvkealamvdlegfedRFVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDI 188
Cdd:cd03222  68 -----------------------QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111106 189 TSLYVTHDQSEAFAVSDTVLVM-NKGHIMQIGSPQDLYRQPASRFMASFMGDAN 241
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFeGEPGVYGIASQPKGTREGINRFLRGYLITFR 177

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

22-196

2.26e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.30 E-value: 2.26e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   22 IDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHMSLGENVGY 101
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  102 GLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRE 181
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188

                        170
                 ....*....|....*
gi 90111106  182 LQKQfDITSLYVTHD 196
Cdd:PRK13546 189 FKEQ-NKTIFFVSHN 202

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

20-222

2.97e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 2.97e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     20 TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGleKPSEGQIFIDGEdVTHRSIQQRDICMVFQSYAL--------FP 91
Cdd:TIGR00956   75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGV-ITYDGITPEEIKKHYRGDVVynaetdvhFP 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     92 HMSLGENVGYGLKM-------LGVPRAELKARVKE-ALAMVDLEGFEDR-----FVDQISGGQQQRVALARALILKPKVL 158
Cdd:TIGR00956  152 HLTVGETLDFAARCktpqnrpDGVSREEYAKHIADvYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQ 231

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111106    159 LFDEPLSNLDANlrrSMRDKIRELQKQFDI--TSLYVTHDQS--EAFAVSDTVLVMNKGHIMQIGSPQ 222
Cdd:TIGR00956  232 CWDNATRGLDSA---TALEFIRALKTSANIldTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGPAD 296

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

28-196

3.82e-11

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 3.82e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   28 TIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDgEDVthrsiqqrdicmvfqSYAlfphmslgenvgyglkmlg 107
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI---------------SYK------------------- 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  108 vP---RAELKARVKEALAMV-----------------DLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:PRK13409 406 -PqyiKPDYDGTVEDLLRSItddlgssyykseiikplQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484

                        170       180
                 ....*....|....*....|....*....
gi 90111106  168 DANLRRSMRDKIRELQKQFDITSLYVTHD 196
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEREATALVVDHD 513

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

19-172

5.35e-11

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.04 E-value: 5.35e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   19 NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIdgedvthRSIQQRDICMVFQSYalfphmsLGEN 98
Cdd:PRK13541  13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNIAKPYCTY-------IGHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   99 VGYGLKMLGVPRAELKARVKEALAMVD-------LEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK13541  79 LGLKLEMTVFENLKFWSEIYNSAETLYaaihyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158


                 .
gi 90111106  172 R 172
Cdd:PRK13541 159 R 159

CFTR_protein

TIGR01271

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

9-245

5.80e-11

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: 63.78 E-value: 5.80e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106      9 LRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKpSEGQIFIDGEDVTHRSIQQ--RDICMVF 84
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTwrKAFGVIP 1298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     85 QSYALFP---HMSLGENVGYGLKMLGvpraelkaRVKEALAMVD-LEGFEDR----FVDQ---ISGGQQQRVALARALIL 153
Cdd:TIGR01271 1299 QKVFIFSgtfRKNLDPYEQWSDEEIW--------KVAEEVGLKSvIEQFPDKldfvLVDGgyvLSNGHKQLMCLARSILS 1370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    154 KPKVLLFDEPLSNLDANLRRSMRdkiRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQpASRFM 233
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE-TSLFK 1446

                          250
                   ....*....|....
gi 90111106    234 ASF--MGDANLFPA 245
Cdd:TIGR01271 1447 QAMsaADRLKLFPL 1460

AAA

smart00382

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

31-214

6.01e-11

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 6.01e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     31 QGQMVTLLGPSGCGKTTILRLVAG-LEKPSEGQIFIDGEDVTHRSIQQRdicmvfqsyalfphmslgenvgyglkmlgvp 109
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL------------------------------- 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    110 raelkarvkealamvdLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQ---- 185
Cdd:smart00382  50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllks 113

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 90111106    186 ------FDITSLYVTHDQSEAFAVSDTVLVMNKGH 214
Cdd:smart00382 114 eknltvILTTNDEKDLGPALLRRRFDRRIVLLLIL 148

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

28-209

6.27e-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: 63.26 E-value: 6.27e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  28 TIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDgEDVTHRSiQ--QRDICMVFQSYaLFphMSLGENVGYGLkm 105
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKP-QyiSPDYDGTVEEF-LR--SANTDDFGSSY-- 434

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 106 lgvpraeLKARVKEALamvDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQ 185
Cdd:COG1245 435 -------YKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504

                       170       180
                ....*....|....*....|....
gi 90111106 186 FDITSLYVTHDQSEAFAVSDTVLV 209
Cdd:COG1245 505 RGKTAMVVDHDIYLIDYISDRLMV 528

PRK11147

ABC transporter ATPase component; Reviewed

8-207

7.65e-11

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 7.65e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    8 ELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDgedvTHRSI----QQRDicmv 83
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVayfdQHRA---- 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   84 fqsyALFPHMSLGENVGYGLKML---GVPRAEL-----------KAR--VKeALamvdlegfedrfvdqiSGGQQQRVAL 147
Cdd:PRK11147 393 ----ELDPEKTVMDNLAEGKQEVmvnGRPRHVLgylqdflfhpkRAMtpVK-AL----------------SGGERNRLLL 451

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111106  148 ARaLILKPKVLL-FDEPLSNLDAnlrrSMRDKIRELQKQFDITSLYVTHDQseAFaVSDTV 207
Cdd:PRK11147 452 AR-LFLKPSNLLiLDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDR--QF-VDNTV 504

PRK15064

ABC transporter ATP-binding protein; Provisional

11-196

8.53e-11

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 8.53e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   11 NVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDG--------------EDVT----- 71
Cdd:PRK15064   6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPnerlgklrqdqfafEEFTvldtv 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   72 ---HRSI----QQRDicmvfQSYALfPHMSlgENVGYGLKMLGVPRAEL-----KARVKEALAMVDLEgFEDRF--VDQI 137
Cdd:PRK15064  86 imgHTELwevkQERD-----RIYAL-PEMS--EEDGMKVADLEVKFAEMdgytaEARAGELLLGVGIP-EEQHYglMSEV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111106  138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsmrdKIRELQ---KQFDITSLYVTHD 196
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIN-------TIRWLEdvlNERNSTMIIISHD 211

PTZ00243

ABC transporter; Provisional

24-235

1.28e-10

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 1.28e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    24 NINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFidgedvthrsiQQRDICMVFQSyALFPHMSLGENVGYGl 103
Cdd:PTZ00243  678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFF- 744

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   104 kmlgvpRAELKARVKEALAMVDLE--------GFEDRFVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDANL- 171
Cdd:PTZ00243  745 ------DEEDAARLADAVRVSQLEadlaqlggGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111106   172 RRSMRDKIreLQKQFDITSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMAS 235
Cdd:PTZ00243  819 ERVVEECF--LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAA 879

ABCC_CFTR1

cd03291

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

19-168

2.92e-10

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: 60.26 E-value: 2.92e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  19 NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGEN 98
Cdd:cd03291  50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKEN 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  99 VgyglkMLGVPRAELkaRVKEALAMVDLEGFEDRFVDQ-----------ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd03291 118 I-----IFGVSYDEY--RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190


                .
gi 90111106 168 D 168
Cdd:cd03291 191 D 191

PLN03073

ABC transporter F family; Provisional

17-168

4.47e-10

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 4.47e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   17 GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFidgedvthRSIQQRdiCMVFQSYalfpHMS-L 95
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR--MAVFSQH----HVDgL 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   96 GENVGYGLKML----GVPRAELKAR-----VKEALAMVDLEgfedrfvdQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PLN03073 586 DLSSNPLLYMMrcfpGVPEQKLRAHlgsfgVTGNLALQPMY--------TLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657


                 ..
gi 90111106  167 LD 168
Cdd:PLN03073 658 LD 659

PLN03130

ABC transporter C family member; Provisional

7-241

6.55e-10

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 6.55e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     7 VELRNVTKRFGSN--TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICM 82
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlRKVLGI 1317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    83 VFQSYALFphmslGENVGYGLKMLG----------VPRAELKARVKEALAMVDLEGFEDRfvDQISGGQQQRVALARALI 152
Cdd:PLN03130 1318 IPQAPVLF-----SGTVRFNLDPFNehndadlwesLERAHLKDVIRRNSLGLDAEVSEAG--ENFSVGQRQLLSLARALL 1390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   153 LKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfdITSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRF 232
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467

                         250
                  ....*....|.
gi 90111106   233 --MASFMGDAN 241
Cdd:PLN03130 1468 skMVQSTGAAN 1478

PRK15064

ABC transporter ATP-binding protein; Provisional

4-196

8.19e-10

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 8.19e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    4 KNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQI------------------Fi 65
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydF- 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   66 dGEDVThrsiqqrdicmvfqsyaLFPHMSLGENVGYGLKMLgvpRAELkARVkealamvdLEGFED--RFVDQISGGQQQ 143
Cdd:PRK15064 396 -ENDLT-----------------LFDWMSQWRQEGDDEQAV---RGTL-GRL--------LFSQDDikKSVKVLSGGEKG 445

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111106  144 RVALARALILKPKVLLFDEPLSNLDanlrrsMrDKIRELQ---KQFDITSLYVTHD 196
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD------M-ESIESLNmalEKYEGTLIFVSHD 494

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

7-200

1.02e-09

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 1.02e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGlEKPSE--------GQIFIDGEdvTHRSIQQR 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGE--TIWDIKKH 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   79 dICMVfqSYALfpHM-----SLGENV---GYgLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQ----ISGGQQQRVA 146
Cdd:PRK10938 338 -IGYV--SSSL--HLdyrvsTSVRNVilsGF-FDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADApfhsLSWGQQRLAL 411

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90111106  147 LARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEA 200
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465

CFTR_protein

TIGR01271

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

21-224

2.04e-09

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 2.04e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVg 100
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNI- 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    101 yglkMLGVPRAELKAR--VKEALAMVDLEGFEDRfvDQI---------SGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
Cdd:TIGR01271  508 ----IFGLSYDEYRYTsvIKACQLEEDIALFPEK--DKTvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106    170 NLRRSMRDkiRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDL 224
Cdd:TIGR01271  582 VTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

17-213

2.15e-09

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.48 E-value: 2.15e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  17 GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPS--EGQIFIDGedvthrsiQQRDICmvFQSYalfphms 94
Cdd:cd03232  18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING--------RPLDKN--FQRS------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  95 lgenVGYglkmlgVPRAEL---KARVKEALAM-VDLEGfedrfvdqISGGQQQRVALARALILKPKVLLFDEPLSNLDAn 170
Cdd:cd03232  81 ----TGY------VEQQDVhspNLTVREALRFsALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS- 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 90111106 171 lrRSMRDKIRELQKQFD--ITSLYVTHDQSEA-FAVSDTVLVMNKG 213
Cdd:cd03232 142 --QAAYNIVRFLKKLADsgQAILCTIHQPSASiFEKFDRLLLLKRG 185

PRK10636

putative ABC transporter ATP-binding protein; Provisional

12-227

4.06e-09

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 4.06e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   12 VTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIfidgedvthrsiqqrdicmvfqsyALFP 91
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------------------------GLAK 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   92 HMSLGENVGYGLKMLGVPRAELKARVKeaLAMVDLE----------GFE-DRFVD---QISGGQQQRVALARALILKPKV 157
Cdd:PRK10636 374 GIKLGYFAQHQLEFLRADESPLQHLAR--LAPQELEqklrdylggfGFQgDKVTEetrRFSGGEKARLVLALIVWQRPNL 451

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  158 LLFDEPLSNLDANLRRSMRDKIRElqkqFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQ 227
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517

ABCC_SUR2

cd03288

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

7-239

1.04e-08

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: 55.30 E-value: 1.04e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNVTKRFGSN--TVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQ--QRDICM 82
Cdd:cd03288  20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  83 VFQSYALFPHmSLGENVGYGLKML------GVPRAELKARVKE---ALAMVDLEGFEDrfvdqISGGQQQRVALARALIL 153
Cdd:cd03288 100 ILQDPILFSG-SIRFNLDPECKCTddrlweALEIAQLKNMVKSlpgGLDAVVTEGGEN-----FSVGQRQLFCLARAFVR 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 154 KPKVLLFDEPLSNLDANLRRSMRDKIreLQKQFDITSLYVTHDQSEAFAvSDTVLVMNKGHIMQIGSPQDLYRQPASRFM 233
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250


                ....*.
gi 90111106 234 ASFMGD 239
Cdd:cd03288 251 SLVRTD 256

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

22-213

3.12e-08

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 3.12e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  22 IDNINLTIPQGQMVTLLGPSGCGKTTIL----------RLVAGLEKPSEGQ-IFIDgedvthrsiqqrdicmvfqsyalf 90
Cdd:cd03238  11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVneglyasgkaRLISFLPKFSRNKlIFID------------------------ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  91 pHMSLGENVGYGLKMLGVPRAELkarvkealamvdlegfedrfvdqiSGGQQQRVALARALI--LKPKVLLFDEPLSNLD 168
Cdd:cd03238  67 -QLQFLIDVGLGYLTLGQKLSTL------------------------SGGELQRVKLASELFsePPGTLFILDEPSTGLH 121

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 90111106 169 ANLRRSMRDKIRELQKQfDITSLYVTHDQsEAFAVSDTVLVMNKG 213
Cdd:cd03238 122 QQDINQLLEVIKGLIDL-GNTVILIEHNL-DVLSSADWIIDFGPG 164

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

21-169

9.29e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 9.29e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAglEKPSEGQIFIDGEDVTHRSIQ---QRDICMVFQSYALFPHMSLGE 97
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDssfQRSIGYVQQQDLHLPTSTVRE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     98 NVGYGLKML---GVPRAELKARVKEALAMVDLEGFEDRFVDQISGG----QQQRVALARALILKPKVLLF-DEPLSNLDA 169
Cdd:TIGR00956  856 SLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLFlDEPTSGLDS 935

PTZ00243

ABC transporter; Provisional

3-232

1.28e-07

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 1.28e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106     3 QKNFVELRNVTKRF--GSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQ--R 78
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrR 1384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    79 DICMVFQSYALFPHmSLGENVGyglkmlgvPRAELK-ARVKEALAMVDL--------EGFEDRFVD---QISGGQQQRVA 146
Cdd:PTZ00243 1385 QFSMIPQDPVLFDG-TVRQNVD--------PFLEASsAEVWAALELVGLrervasesEGIDSRVLEggsNYSVGQRQLMC 1455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   147 LARALILK-PKVLLFDEPLSNLDANLRRSMRDKIRELQKQFdiTSLYVTHdQSEAFAVSDTVLVMNKGHIMQIGSPQDLY 225
Cdd:PTZ00243 1456 MARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532


                  ....*..
gi 90111106   226 RQPASRF 232
Cdd:PTZ00243 1533 MNRQSIF 1539

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

35-196

2.11e-07

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: 50.68 E-value: 2.11e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  35 VTLL-GPSGCGKTTILRLVaglekpsegqifidgedvthrsiqqrdicmvfqSYALFPHMSLGENVGYGL-KMlgvprae 112
Cdd:cd03240  24 LTLIvGQNGAGKTTIIEAL---------------------------------KYALTGELPPNSKGGAHDpKL------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106 113 lkARVKEALAMVDLEgFEDR------------------FVDQ-------------ISGGQQQ------RVALARALILKP 155
Cdd:cd03240  64 --IREGEVRAQVKLA-FENAngkkytitrslailenviFCHQgesnwplldmrgrCSGGEKVlasliiRLALAETFGSNC 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 90111106 156 KVLLFDEPLSNLDA-NLRRSMRDKIRELQKQFDITSLYVTHD 196
Cdd:cd03240 141 GILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182

PLN03140

ABC transporter G family member; Provisional

32-213

9.09e-07

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 9.09e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    32 GQMVTLLGPSGCGKTTILRLVAGLEKPS--EGQIFIDG---EDVTHRSI----QQRDI----CMVFQSYALFPHMSLGEN 98
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkKQETFARIsgycEQNDIhspqVTVRESLIYSAFLRLPKE 985

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    99 VGYGLKMLgvpraelkaRVKEALAMVDLEGFEDRFV-----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrR 173
Cdd:PLN03140  986 VSKEEKMM---------FVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---R 1053

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 90111106   174 SMRDKIRELQKQFDI--TSLYVTHDQS----EAFavsDTVLVMNKG 213
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTgrTVVCTIHQPSidifEAF---DELLLMKRG 1096

PLN03073

ABC transporter F family; Provisional

7-168

1.19e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 1.19e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106    7 VELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVA-----GLekPSEGQIF-----IDGEDVT----- 71
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqeVVGDDTTalqcv 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   72 ---------------HRSIQQRDIcmvfQSYALFPHMSLGENVGYGLKMLGVPRAELKARVK-------EALAMVDLEGF 129
Cdd:PLN03073 256 lntdiertqlleeeaQLVAQQREL----EFETETGKGKGANKDGVDKDAVSQRLEEIYKRLElidaytaEARAASILAGL 331

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 90111106  130 ------EDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PLN03073 332 sftpemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

137-218

2.58e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.58e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQfDITSLYVTHDQSEAFAVSDTVLVMNKGHIM 216
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470


                 ..
gi 90111106  217 QI 218
Cdd:PRK10982 471 GI 472

PRK10636

putative ABC transporter ATP-binding protein; Provisional

15-168

2.86e-06

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 2.86e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   15 RFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAG--------------------------LEKPSEGQIfIDGe 68
Cdd:PRK10636  10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsytfpgnwqlawvnqetpaLPQPALEYV-IDG- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   69 DVTHRSIQQRdicmvfqsyalfPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFE------DRFVDQISGGQQ 142
Cdd:PRK10636  88 DREYRQLEAQ------------LHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGfsneqlERPVSDFSGGWR 155

                        170       180
                 ....*....|....*....|....*.
gi 90111106  143 QRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLD 181

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

19-219

3.65e-06

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 3.65e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   19 NTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLE--KPSEGQIFIDGEDVTHRSIQQR---DICMVFQSYALFPHM 93
Cdd:PRK09580  14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   94 SlgeNVGYGLKMLGVPRaelKARVKEALAMVDLEGFEDRFVDQI---------------SGGQQQRVALARALILKPKVL 158
Cdd:PRK09580  94 S---NQFFLQTALNAVR---SYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELC 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106  159 LFDEPLSNLD-------ANLRRSMRDKIRELqkqfditsLYVTHDQS-EAFAVSDTVLVMNKGHIMQIG 219
Cdd:PRK09580 168 ILDESDSGLDidalkivADGVNSLRDGKRSF--------IIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

14-197

1.23e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 1.23e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  14 KRFGSNtvIDNINLTIPQGQMVTLLGPSGCGKTTILRlvaglekpsegqifidgedvthrsiqqrDICmvfqsYALFPHM 93
Cdd:cd03227   5 GRFPSY--FVPNDVTFGEGSLTIITGPNGSGKSTILD----------------------------AIG-----LALGGAQ 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  94 SLGENVGYGLKMLGVPRAELKARVkealamvdlegfedrFVDQISGGQQQRVALARALIL---KPKVL-LFDEPLSNLDA 169
Cdd:cd03227  50 SATRRRSGVKAGCIVAAVSAELIF---------------TRLQLSGGEKELSALALILALaslKPRPLyILDEIDRGLDP 114

                       170       180
                ....*....|....*....|....*...
gi 90111106 170 NLRRSMRDKIRELQKQFDITsLYVTHDQ 197
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQV-IVITHLP 141

CysA_C_terminal

pfam17850

CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ...

241-282

1.02e-04

CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.

Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 39.35 E-value: 1.02e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 90111106   241 NLFPATFSDGYVDIYGYHLPRPLHFGTQG-EGMVGVRPEAITL 282
Cdd:pfam17850   1 NLFHGRVEDGRVRIGGLALPLPELAGAEGsEVVAYVRPHDLEI 43

AAA_14

pfam13173

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...

31-80

1.06e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.

Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 38.72 E-value: 1.06e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111106    31 QGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDI 80
Cdd:pfam13173   1 SRKILVITGPRQVGKTTLLLQLIKELLPPENILYINLDDPRLLKLADFEL 50

COG1373

Predicted ATPase, AAA+ superfamily [General function prediction only];

21-87

1.41e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];

Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 40.31 E-value: 1.41e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111106  21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSegqIFIDGEDVTHRSIQQRDICMVFQSY 87
Cdd:COG1373   9 ILDKLLKLLDNRKAVVITGPRQVGKTTLLKQLAKELENI---LYINLDDPRLRALAEEDPDDLLEAL 72

ABC_SMC3_euk

cd03272

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...

130-189

2.25e-03

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: 39.17 E-value: 2.25e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111106 130 EDRFVDQISGGQQQRVALAraLIL-------KPKVLlFDEPLSNLDANLRRSMRDKIRELQK--QFDIT 189
Cdd:cd03272 152 EQQEMQQLSGGQKSLVALA--LIFaiqkcdpAPFYL-FDEIDAALDAQYRTAVANMIKELSDgaQFITT 217

GguA

NF040905

sugar ABC transporter ATP-binding protein;

21-163

2.91e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 2.91e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   21 VIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLE--KPSEGQIFIDGEDVTHRSIQQ---RDICMVFQ---SYALFPH 92
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDaidAGLAYVTEdrkGYGLNLI 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   93 MSLGENV-GYGLKmlGVPRAELKARVKEALAMvdlEGFEDRF------VDQI----SGGQQQRVALARALILKPKVLLFD 161
Cdd:NF040905 355 DDIKRNItLANLG--KVSRRGVIDENEEIKVA---EEYRKKMniktpsVFQKvgnlSGGNQQKVVLSKWLFTDPDVLILD 429


                 ..
gi 90111106  162 EP 163
Cdd:NF040905 430 EP 431

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

131-185

3.03e-03

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 3.03e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106  131 DRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQ 185
Cdd:PRK10938 130 DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

24-76

3.38e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 3.38e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106    24 NINLTIPQGQMVTLLGPSGCGKTTILR--LVAGLEKPSEGQIFIDGedvTHRSIQ 76
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPG---RYTSIE 677

PRK01156

chromosome segregation protein; Provisional

134-212

4.37e-03

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 4.37e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  134 VDQISGGQQQ------RVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIR-ELQKQFDITSLYVTHDQSEAFAVSDT 206
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIPQVIMISHHRELLSVADV 878


                 ....*.
gi 90111106  207 VLVMNK 212
Cdd:PRK01156 879 AYEVKK 884

SbcC

COG0419

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];

7-183

5.57e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];

Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 5.57e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106   7 VELRNvtkrFGSNTVIDNINLTIPqgqmVTLL-GPSGCGKTTILR-LVAGLEKPSEGQIFIDGEDVTHRSIQQRdICMVF 84
Cdd:COG0419   5 LRLEN----FRSYRDTETIDFDDG----LNLIvGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEAS-VELEF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111106  85 QS-------------YALFPHMS---LGENVGyglKMLGVPR--------AELKARVKEALAMVD------------LEG 128
Cdd:COG0419  76 EHggkryrierrqgeFAEFLEAKpseRKEALK---RLLGLEIyeelkerlKELEEALESALEELAelqklkqeilaqLSG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 90111106 129 FEDrfVDQISGGQQQRVALARALilkpkVLLFDepLSNLDANLRRSMRDKIRELQ 183
Cdd:COG0419 153 LDP--IETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA 198

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