NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16129400|ref|NP_415958|]
View 

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

Protein Classification

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

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including Fe(3+) ions and polyamines such as spermidine and putrescine

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-333 2.06e-175

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 489.99  E-value: 2.06e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNT 80
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 241 FDGLMAE------KLCGMT--------------GSFALRPEHIRLNTPGELQA-NGTIQAVQYQGAATRFELKLNGGEKL 299
Cdd:COG3842 242 LPGTVLGdegggvRTGGRTlevpadaglaaggpVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                       330       340       350
                ....*....|....*....|....*....|....
gi 16129400 300 LVSQANMTGEELPatltPGQQVMVSWSRDVMVPL 333
Cdd:COG3842 322 VVRVPNRAALPLE----PGDRVGLSWDPEDVVVL 351
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-333 2.06e-175

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 489.99  E-value: 2.06e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNT 80
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 241 FDGLMAE------KLCGMT--------------GSFALRPEHIRLNTPGELQA-NGTIQAVQYQGAATRFELKLNGGEKL 299
Cdd:COG3842 242 LPGTVLGdegggvRTGGRTlevpadaglaaggpVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                       330       340       350
                ....*....|....*....|....*....|....
gi 16129400 300 LVSQANMTGEELPatltPGQQVMVSWSRDVMVPL 333
Cdd:COG3842 322 VVRVPNRAALPLE----PGDRVGLSWDPEDVVVL 351
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 2.99e-132

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: 376.19  E-value: 2.99e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03300  81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-325 1.84e-129

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 374.67  E-value: 1.84e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK09452  95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  245 MAEKL-------------CGMTGSFA----------LRPEHIRLNTPGELQAN----GTIQAVQYQGAATRFELKLNGGE 297
Cdd:PRK09452 255 VIERLdeqrvranvegreCNIYVNFAvepgqklhvlLRPEDLRVEEINDDEHAegliGYVRERNYKGMTLDSVVELENGK 334

                        330       340
                 ....*....|....*....|....*....
gi 16129400  298 KLLVSQanMTGEELPA-TLTPGQQVMVSW 325
Cdd:PRK09452 335 MVMVSE--FFNEDDPDfDHSLGQKVAVTW 361
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 8-328 3.74e-114

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: 334.70  E-value: 3.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYAL 87
Cdd:TIGR03265   8 DNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    88 FPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:TIGR03265  88 FPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAE 247
Cdd:TIGR03265 168 RVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   248 -----------------KLCGMTGSFALRPEHIRLNtPGELQAN---GTIQAVQYQGAATRFELKLNG--GEKLLVSQAN 305
Cdd:TIGR03265 248 gsrarvggltlacapglAQPGASVRLAVRPEDIRVS-PAGNAANlllARVEDMEFLGAFYRLRLRLEGlpGQALVADVSA 326

                         330       340
                  ....*....|....*....|...
gi 16129400   306 MTGEELPatLTPGQQVMVSWSRD 328
Cdd:TIGR03265 327 SEVERLG--IRAGQPIWIELPAE 347
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
5-272 5.29e-83

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 255.00  E-value: 5.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDgVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:NF040840   2 IRIENLSKDWKEFKLRD-ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEkvALGFVH--QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:NF040840  81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIME--LLGISHllHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFD 242
Cdd:NF040840 159 SALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIE 238

                        250       260       270
                 ....*....|....*....|....*....|
gi 16129400  243 GlMAEKLCGMTgsfALRPEHIRLNTPGELQ 272
Cdd:NF040840 239 G-VAEKGGEGT---ILDTGNIKIELPEEKK 264
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-161 1.80e-41

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: 141.63  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400    98 AYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRK----PSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-205 1.33e-21

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 90.37  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKpasnlppweRDVNTVFQDYAL---FPh 90
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   91 MSILDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:NF040873  72 LTVRDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16129400  167 LKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRV 205
Cdd:NF040873 152 AESRERI-IALLAEEHARGATVVVVTHDLELVRRADPCV 189
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
3-222 7.80e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 78.63  E-value: 7.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    3 YAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERdVNT 80
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdAGDIATRRR-VGY 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFPHMSILDNVAygLMVK--GVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:NF033858 344 MSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  159 DEPLGALDLKLREQMQLELKKLQQSLGITfIFV-THDQGEALSmSDRVAVFNNGRIEQVDSPRDL 222
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
GguA NF040905
sugar ABC transporter ATP-binding protein;
6-217 3.50e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 75.98  E-value: 3.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GAISIFGKPA--SNLPPWE 75
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKV------LSGvyphgsyeGEILFDGEVCrfKDIRDSE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 RD-VNTVFQDYALFPHMSILDNVAYG--LMVKGV-NKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:NF040905  77 ALgIVIIHQELALIPYLSIAENIFLGneRAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400  152 EPRVLLLDEPLGALD----LKLREQMqLELKKlQqslGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVD 217
Cdd:NF040905 157 DVKLLILDEPTAALNeedsAALLDLL-LELKA-Q---GITSIIISHKLNEIRRVADSITVLRDGRtIETLD 222
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-226 4.37e-15

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 75.16  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTtclrliagfeqlSGGAISIFGKPASNLPPWeRDVNTVFQ 83
Cdd:NF000106  13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------------RGALPAHV*GPDAGRRPW-RF*TWCAN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYALFPHMSILDNVAYG----------LMVKG----VNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARAL 149
Cdd:NF000106  80 RRALRRTIG*HRPVR*GrresfsgrenLYMIGr*ldLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEA------LSMSDRVAVFNNGRIEQVDSP---R 220
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggR 238


                 ....*.
gi 16129400  221 DLYMRP 226
Cdd:NF000106 239 TLQIRP 244
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-161 7.31e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 69.38  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlppwERDVNTVFQ 83
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYA---------LFPHMSILDNVA-----YGLmvkgvNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARAL 149
Cdd:NF033858  77 RIAympqglgknLYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151

                        170
                 ....*....|..
gi 16129400  150 VNEPRVLLLDEP 161
Cdd:NF033858 152 IHDPDLLILDEP 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 30-204 2.35e-10

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: 58.15  E-value: 2.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFqdyalfphmsildnvayglmvkgvnkk 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    110 qrhamaqealekvalgfvhQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE-----LKKLQQSL 184
Cdd:smart00382  55 -------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115

                          170       180
                   ....*....|....*....|
gi 16129400    185 GITFIFVTHDQGEALSMSDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
GguA NF040905
sugar ABC transporter ATP-binding protein;
135-213 2.02e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.85  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  135 LSGGQRQRVAIARALVNEPRVLLLDEP-----LGAldlklreqmQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVA 206
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIY 475


                 ....*..
gi 16129400  207 VFNNGRI 213
Cdd:NF040905 476 VMNEGRI 482
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-333 2.06e-175

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 489.99  E-value: 2.06e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNT 80
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 241 FDGLMAE------KLCGMT--------------GSFALRPEHIRLNTPGELQA-NGTIQAVQYQGAATRFELKLNGGEKL 299
Cdd:COG3842 242 LPGTVLGdegggvRTGGRTlevpadaglaaggpVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                       330       340       350
                ....*....|....*....|....*....|....
gi 16129400 300 LVSQANMTGEELPatltPGQQVMVSWSRDVMVPL 333
Cdd:COG3842 322 VVRVPNRAALPLE----PGDRVGLSWDPEDVVVL 351
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 4-328 1.35e-136

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 391.74  E-value: 1.35e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQ 83
Cdd:COG3839   3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG3839  83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTS--NVF 241
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLL 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 242 DG-----------------LMAEKLCGMTGSFALRPEHIRLNTPGELQANGTIQAVQYQGAATRFELKLnGGEKLLVSQA 304
Cdd:COG3839 243 PGtvegggvrlggvrlplpAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRL-GGQELVARVP 321

                       330       340
                ....*....|....*....|....
gi 16129400 305 NMTGeelpatLTPGQQVMVSWSRD 328
Cdd:COG3839 322 GDTR------LRPGDTVRLAFDPE 339
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 2.99e-132

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: 376.19  E-value: 2.99e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03300  81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-325 1.84e-129

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 374.67  E-value: 1.84e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK09452  95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  245 MAEKL-------------CGMTGSFA----------LRPEHIRLNTPGELQAN----GTIQAVQYQGAATRFELKLNGGE 297
Cdd:PRK09452 255 VIERLdeqrvranvegreCNIYVNFAvepgqklhvlLRPEDLRVEEINDDEHAegliGYVRERNYKGMTLDSVVELENGK 334

                        330       340
                 ....*....|....*....|....*....
gi 16129400  298 KLLVSQanMTGEELPA-TLTPGQQVMVSW 325
Cdd:PRK09452 335 MVMVSE--FFNEDDPDfDHSLGQKVAVTW 361
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 5-332 1.40e-117

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 343.28  E-value: 1.40e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPA-SNLPPWERDVNTVFQ 83
Cdd:COG1118   3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG1118  83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVF-- 241
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLrg 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 242 ---------DGLMAEKLCGMTGSFA---LRPEHIRLNTPGELQAN--GTIQAVQYQGAATRFELKLNGGEKLLVsQANMT 307
Cdd:COG1118 243 rviggqleaDGLTLPVAEPLPDGPAvagVRPHDIEVSREPEGENTfpATVARVSELGPEVRVELKLEDGEGQPL-EAEVT 321

                       330       340
                ....*....|....*....|....*..
gi 16129400 308 GEELPA-TLTPGQQVMVSWSR-DVMVP 332
Cdd:COG1118 322 KEAWAElGLAPGDPVYLRPRPaRVFLP 348
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 8-328 3.74e-114

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: 334.70  E-value: 3.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYAL 87
Cdd:TIGR03265   8 DNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    88 FPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:TIGR03265  88 FPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAE 247
Cdd:TIGR03265 168 RVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   248 -----------------KLCGMTGSFALRPEHIRLNtPGELQAN---GTIQAVQYQGAATRFELKLNG--GEKLLVSQAN 305
Cdd:TIGR03265 248 gsrarvggltlacapglAQPGASVRLAVRPEDIRVS-PAGNAANlllARVEDMEFLGAFYRLRLRLEGlpGQALVADVSA 326

                         330       340
                  ....*....|....*....|...
gi 16129400   306 MTGEELPatLTPGQQVMVSWSRD 328
Cdd:TIGR03265 327 SEVERLG--IRAGQPIWIELPAE 347
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 5-217 1.80e-111

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: 322.55  E-value: 1.80e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03259  81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129400 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 35-333 8.14e-111

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: 325.22  E-value: 8.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    35 MLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAM 114
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   115 AQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHD 194
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   195 QGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAEKL-------------CGMTGSF----- 256
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKseqvvlagvegrrCDIYTDVpvekd 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   257 -----ALRPEHIRLNTPGELQ----ANGTIQAVQYQGAATRFELKLNGGEKLLVSqANMTGEELPATLTPGQQVMVSWSR 327
Cdd:TIGR01187 241 qplhvVLRPEKIVIEEEDEANssnaIIGHVIDITYLGMTLEVHVRLETGQKVLVS-EFFNEDDPHMSPSIGDRVGLTWHP 319


                  ....*.
gi 16129400   328 DVMVPL 333
Cdd:TIGR01187 320 GSEVVL 325
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
4-319 8.99e-103

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 306.00  E-value: 8.99e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVF 82
Cdd:PRK11650   3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   83 QDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK11650  83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGT----- 237
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpamnl 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  238 ---SNVFDGLMAEKLCGMTGSFA--------------LRPEHIRLnTPGELQANGTIQAVQYQGAATRFELKLNGGE--- 297
Cdd:PRK11650 243 ldgRVSADGAAFELAGGIALPLGggyrqyagrkltlgIRPEHIAL-SSAEGGVPLTVDTVELLGADNLAHGRWGGQPlvv 321

                        330       340
                 ....*....|....*....|..
gi 16129400  298 KLLVSQANMTGEELPATLTPGQ 319
Cdd:PRK11650 322 RLPHQERPAAGSTLWLHLPANQ 343
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 3-236 7.25e-98

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: 289.24  E-value: 7.25e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   3 YAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVF 82
Cdd:cd03296   1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNVAYGLMVKGV----NKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03296  81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 159 DEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 5-217 7.66e-98

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: 288.00  E-value: 7.66e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03301  81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129400 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 4-231 2.14e-96

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 286.22  E-value: 2.14e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLY----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwerDVN 79
Cdd:COG1116   7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1116  84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNN--GRI---EQVDSPrdlymRPRTPFV 231
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIveeIDVDLP-----RPRDREL 235
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
5-307 5.09e-95

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 285.85  E-value: 5.09e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11432  87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  245 MAEKLCGMTG------------------SFALRPEHIRLNTPGELQANGTIQAVQYQGAatRFELKLNGGEKLLVSQANM 306
Cdd:PRK11432 247 LSGDYVDIYGyrlprpaafafnlpdgecTVGVRPEAITLSEQGEESQRCTIKHVAYMGP--QYEVTVDWHGQELLLQVNA 324


                 .
gi 16129400  307 T 307
Cdd:PRK11432 325 T 325
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 5-213 1.33e-91

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: 272.42  E-value: 1.33e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD----VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwerDVNT 80
Cdd:cd03293   1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVAL-GFVHQRkPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03293  78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLsGFENAY-PHQLSGGMRQRVALARALAVDPDVLLLD 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNN--GRI 213
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 5-240 3.11e-90

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 269.75  E-value: 3.11e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400   165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 5-240 2.27e-88

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: 264.97  E-value: 2.27e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRaVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03299   1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03299  80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
5-301 8.23e-88

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 268.05  E-value: 8.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:PRK11000   4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11000  84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG-------- 236
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspkmnflp 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  237 ---TSNVFDGLMAEKLCGM--------TG-------SFALRPEHIRLNTPGELQANGTIQAVQYQGAATRFELKLNGGEK 298
Cdd:PRK11000 244 vkvTATAIEQVQVELPNRQqvwlpvegRGvqvganmSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIPAIRQ 323


                 ...
gi 16129400  299 LLV 301
Cdd:PRK11000 324 NLV 326
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 6-238 9.03e-88

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 265.80  E-value: 9.03e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTVF 82
Cdd:COG1125   3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVAL---GFVHqRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1125  83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeEYRD-RYPHELSGGQQQRVGVARALAADPPILLMD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTS 238
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-333 2.33e-87

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 267.47  E-value: 2.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNT 80
Cdd:PRK11607  16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINM 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK11607  96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  241 FDGLMAEK------------------------LCGMTGSFALRPEHIRLNTpgELQANGTIQAV------QYQGAATRFE 290
Cdd:PRK11607 256 FEGVLKERqedglvidspglvhplkvdadasvVDNVPVHVALRPEKIMLCE--EPPADGCNFAVgevihiAYLGDLSIYH 333

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 16129400  291 LKLNGGeKLLVSQANMTGEELPATLTPGQQVMVSWSRDVMVPL 333
Cdd:PRK11607 334 VRLKSG-QMISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVL 375
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
4-243 8.70e-84

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 257.32  E-value: 8.70e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQ 83
Cdd:PRK10851   2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYALFPHMSILDNVAYGLMVkgVNKKQR---HAMAQEA---LEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK10851  82 HYALFRHMTVFDNIAFGLTV--LPRRERpnaAAIKAKVtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGT 237
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239


                 ....*.
gi 16129400  238 SNVFDG 243
Cdd:PRK10851 240 VNRLQG 245
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
5-272 5.29e-83

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 255.00  E-value: 5.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDgVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:NF040840   2 IRIENLSKDWKEFKLRD-ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEkvALGFVH--QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:NF040840  81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIME--LLGISHllHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFD 242
Cdd:NF040840 159 SALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIE 238

                        250       260       270
                 ....*....|....*....|....*....|
gi 16129400  243 GlMAEKLCGMTgsfALRPEHIRLNTPGELQ 272
Cdd:NF040840 239 G-VAEKGGEGT---ILDTGNIKIELPEEKK 264
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 5-236 2.84e-80

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: 244.52  E-value: 2.84e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTV 81
Cdd:cd03295   1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVH--QRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03295  81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-214 3.42e-79

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 241.10  E-value: 3.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGD----VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER 76
Cdd:COG1136   1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  77 DV--NT----VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALV 150
Cdd:COG1136  81 ARlrRRhigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 151 NEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQgEALSMSDRVAVFNNGRIE 214
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 5-213 1.57e-77

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: 236.62  E-value: 1.57e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD----VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERD--- 77
Cdd:cd03255   1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 ---VNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03255  81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 155 VLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 15-235 2.95e-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: 237.93  E-value: 2.95e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE------RDVNTVFQDYALF 88
Cdd:cd03294  35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  89 PHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFV 235
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 5-212 9.01e-77

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: 233.23  E-value: 9.01e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP----ASNLPPWERDVNT 80
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdlEDELPPLRRRIGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLmvkgvnkkqrhamaqealekvalgfvhqrkpsqlSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03229  81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129400 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 2-235 4.40e-73

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 231.15  E-value: 4.40e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   2 TYAVEFDNVSRLYGD------------------------VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLS 57
Cdd:COG4175   1 MPKIEVRNLYKIFGKrperalklldqgkskdeilektgqTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  58 GGAISIFGKPASNLPPWE------RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRK 131
Cdd:COG4175  81 AGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 132 PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240

                       250       260
                ....*....|....*....|....
gi 16129400 212 RIEQVDSPRDLYMRPRTPFVAGFV 235
Cdd:COG4175 241 RIVQIGTPEEILTNPANDYVADFV 264
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 5-229 4.22e-71

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: 229.40  E-value: 4.22e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY-----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE---- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 -RDVNTVFQD--YALFPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVALG--FVHqRKPSQLSGGQRQRVAIARAL 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpdLAD-RYPHELSGGQRQRVAIARAL 419

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 150 VNEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQiLNL-LRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498


                .
gi 16129400 229 P 229
Cdd:COG1123 499 P 499
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
6-213 1.09e-69

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 218.19  E-value: 1.09e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYG----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlPPWERDVntV 81
Cdd:COG4525   5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--V 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG4525  82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16129400 162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVF--NNGRI 213
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 5-229 6.05e-69

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 215.24  E-value: 6.05e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK----PASNLPPWERDVNT 80
Cdd:COG1126   2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltdSKKDINKLRRKVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1126  82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 160 EPLGALD-------LKLreqmqleLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG1126 162 EPTSALDpelvgevLDV-------MRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
5-217 6.37e-68

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 212.22  E-value: 6.37e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE-----RDV 78
Cdd:COG2884   2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG2884  82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 159 DEPLGALDLKLREQ-MQLeLKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 5-213 6.72e-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: 207.36  E-value: 6.72e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-----PWE 75
Cdd:cd03257   2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 RDVNTVFQDY--ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQ---RKPSQLSGGQRQRVAIARALV 150
Cdd:cd03257  82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPHELSGGQRQRVAIARALA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
5-222 7.89e-66

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 207.22  E-value: 7.89e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK-PASNLPPWERDVNTVFQ 83
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRRRIGYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG1131  81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-230 6.40e-65

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: 205.42  E-value: 6.40e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYG----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RD 77
Cdd:COG1124   1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 VNTVFQDY--ALFPHMSILDNVAYGLMVKGVnkKQRHAMAQEALEKVALG--FVHqRKPSQLSGGQRQRVAIARALVNEP 153
Cdd:COG1124  81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPpsFLD-RYPHQLSGGQRQRVAIARALILEP 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 154 RVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
6-237 9.25e-65

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 204.60  E-value: 9.25e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGD--VRAvdgvSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQ 83
Cdd:COG3840   3 RLDDLTYRYGDfpLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVAYGLMVKG-VNKKQRHAMAQeALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG3840  79 ENNLFPHLTVAQNIGLGLRPGLkLTAEQRAQVEQ-ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGT 237
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 5-228 2.90e-64

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: 202.95  E-value: 2.90e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTV 81
Cdd:COG1122   1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1122  81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 29-217 3.06e-64

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: 202.53  E-value: 3.06e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  29 DGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP------ASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLm 102
Cdd:cd03297  22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGL- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 103 vKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQ 182
Cdd:cd03297 101 -KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179

                       170       180       190
                ....*....|....*....|....*....|....*
gi 16129400 183 SLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
5-238 3.47e-62

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 201.46  E-value: 3.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE----- 75
Cdd:COG1135   2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:COG1135  82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 156 LLLDEPLGALD-------LKLreqmqleLKKLQQSLGITFIFVTHDqgealsMS------DRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1135 162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDV 228

                       250
                ....*....|....*.
gi 16129400 223 YMRPRTPFVAGFVGTS 238
Cdd:COG1135 229 FANPQSELTRRFLPTV 244
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 37-243 4.54e-62

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: 201.48  E-value: 4.54e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  37 GPSGSGKTTCLRLIAGFEQLSGGAISIFGKP------ASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLmvkgvnKKQ 110
Cdd:COG4148  32 GPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPHRRRIGYVFQEARLFPHLSVRGNLLYGR------KRA 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 111 RHAMAQEALEKVA--LGFVH--QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGI 186
Cdd:COG4148 106 PRAERRISFDEVVelLGIGHllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDI 185

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 187 TFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDG 243
Cdd:COG4148 186 PILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA 242
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-222 1.10e-61

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: 196.74  E-value: 1.10e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERD--- 77
Cdd:COG1127   2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 --VNTVFQDYALFPHMSILDNVAYGL-MVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1127  82 rrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 155 VLLLDEPLGALD-LKLREQMQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1127 162 ILLYDEPTAGLDpITSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 5-227 6.97e-61

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: 194.72  E-value: 6.97e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD----VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK-----PASNLPPWE 75
Cdd:cd03258   2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllSGKELRKAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03258  82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 5-213 1.94e-60

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: 192.74  E-value: 1.94e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG----KPASNLPPWERDVNT 80
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltDDKKNINELRQKVGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHMSILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03262  81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 4-213 4.90e-59

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 190.27  E-value: 4.90e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-----WERD 77
Cdd:COG3638   2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 VNTVFQDYALFPHMSILDNVAYGL---------MVKGVNKKQRhAMAQEALEKVALG-FVHQRkPSQLSGGQRQRVAIAR 147
Cdd:COG3638  82 IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsLLGLFPPEDR-ERALEALERVGLAdKAYQR-ADQLSGGQQQRVAIAR 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 148 ALVNEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 5-222 1.47e-58

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: 188.54  E-value: 1.47e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQL-----SGGAISIFGKP--ASNLPPWE-- 75
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDiyDLDVDVLElr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 RDVNTVFQDYALFPhMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVAL-GFVHQR-KPSQLSGGQRQRVAIARALVNE 152
Cdd:cd03260  81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
4-202 4.81e-58

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 187.98  E-value: 4.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlPPWERDVntVFQ 83
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK11248  78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16129400  164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMS 202
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
5-234 3.91e-57

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 185.30  E-value: 3.91e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG----KPASNLPPWERDVNT 80
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKVDERLIRQEAGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK09493  82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  160 EPLGALDLKLREqmqlELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGF 234
Cdd:PRK09493 162 EPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-227 8.21e-57

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: 192.04  E-value: 8.21e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLY--GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG---FEQLSGGAISIFGKPASNLPPWE 75
Cdd:COG1123   1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 R--DVNTVFQD--YALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:COG1123  81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 15-229 1.23e-56

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 186.86  E-value: 1.23e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE-----RDVNTVFQD-YA-L 87
Cdd:COG4608  29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  88 FPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:COG4608 109 NPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHaDRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 166 DLKLREQ-MQLeLKKLQQSLGITFIFVTHDqgeaLSM----SDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG4608 189 DVSIQAQvLNL-LEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPLHP 252
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 5-222 1.49e-56

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: 183.47  E-value: 1.49e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE-----RDVN 79
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQR-HAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03261  81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400 159 DEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 15-229 2.80e-55

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: 182.95  E-value: 2.80e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGAISIFGKPASNLPPWE------RDVNTVFQD- 84
Cdd:COG0444  16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQDp 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 Y-ALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVHQRK---PSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG0444  96 MtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARALALEPKLLIAD 175

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 160 EPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSpRDLYMRPRTP 229
Cdd:COG0444 176 EPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEEGPV-EELFENPRHP 245
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 20-220 6.77e-55

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: 179.20  E-value: 6.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwERDVntVFQDYALFPHMSILDNVAy 99
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   100 gLMVKGVN----KKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:TIGR01184  77 -LAVDRVLpdlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16129400   176 ELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNN------GRIEQVDSPR 220
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPR 206
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 6-212 7.98e-54

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: 175.73  E-value: 7.98e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTV 81
Cdd:cd03225   1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03225  81 FQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 6-222 1.20e-53

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: 176.20  E-value: 1.20e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-WERDVNTVFQD 84
Cdd:COG4555   3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG4555  83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 165 LDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 12-229 3.47e-53

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: 182.96  E-value: 3.47e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  12 RLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTC----LRLIAgfeqlSGGAISIFGKPASNLP-----PWERDVNTVF 82
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSrralrPLRRRMQVVF 368

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QD-YA-LFPHMSILDNVAYGLMV--KGVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLV 448

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400 158 LDEPLGALDLKLREQMqLEL-KKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSpRDLYMRPRTP 229
Cdd:COG4172 449 LDEPTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQGPT-EQVFDAPQHP 520
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 5-226 3.70e-53

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: 176.10  E-value: 3.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYG-----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG-----KPASNLPPW 74
Cdd:TIGR04521   1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditaKKKKKLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    75 ERDVNTVFQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:TIGR04521  81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400   152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 4-222 5.11e-53

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: 174.85  E-value: 5.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTV 81
Cdd:COG1120   1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFPHMSILDNVAYGLM----VKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG1120  81 PQEPPAPFGLTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 158 LDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1120 161 LDEPTSHLDLAHQLEvLEL-LRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 5-206 8.68e-53

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: 173.20  E-value: 8.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK-----PASNLPPWERDV 78
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlRGRQLPLLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 16129400   159 DEPLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDqgeaLSMSDRVA 206
Cdd:TIGR02673 162 DEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHD----LSLVDRVA 204
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-213 9.26e-53

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: 174.46  E-value: 9.26e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERD--- 77
Cdd:COG0411   1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 -VNTvFQDYALFPHMSILDNVAYGLMVK------------GVNKKQRHAM---AQEALEKVALGFVHQRKPSQLSGGQRQ 141
Cdd:COG0411  81 iART-FQNPRLFPELTVLENVLVAAHARlgrgllaallrlPRARREEREArerAEELLERVGLADRADEPAGNLSYGQQR 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 8-227 9.62e-53

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 174.48  E-value: 9.62e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLppwERDVNTVFQDYAL 87
Cdd:PRK11247  16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLMFQDARL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   88 FPHMSILDNVAYGLmvKGVNKKQrhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK11247  93 LPWKKVIDNVGLGL--KGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIeQVDSPRDLyMRPR 227
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-GLDLTVDL-PRPR 224
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 6-213 2.57e-52

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: 172.75  E-value: 2.57e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-----WERDVN 79
Cdd:cd03256   2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFPHMSILDNVAYGLM--------VKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:cd03256  82 MIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400 152 EPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 5-213 1.23e-51

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: 169.98  E-value: 1.23e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAvdGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03298   1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVK-GVNKKQRHAMAQeALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03298  79 NNLFAHLTVEQNVGLGLSPGlKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16129400 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-222 1.42e-51

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 171.04  E-value: 1.42e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlpPWER---- 76
Cdd:COG1121   3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--ARRRigyv 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  77 ----DVNtvfqdyALFPhMSILDNVAYGL-----MVKGVNKKQRhAMAQEALEKV-ALGFVHqRKPSQLSGGQRQRVAIA 146
Cdd:COG1121  81 pqraEVD------WDFP-ITVRDVVLMGRygrrgLFRRPSRADR-EAVDEALERVgLEDLAD-RPIGELSGGQQQRVLLA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 147 RALVNEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI-----EQVDSPR 220
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVLTPE 229


                ..
gi 16129400 221 DL 222
Cdd:COG1121 230 NL 231
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 5-213 5.71e-51

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: 166.80  E-value: 5.71e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-WERDVNTVFQ 83
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVayglmvkgvnkkqrhamaqealekvalgfvhqrkpsQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03230  81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16129400 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 6-202 7.22e-51

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 168.04  E-value: 7.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF--EQLSG-GAISIFGKPASNLPPWERDVNTVF 82
Cdd:COG4136   3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSAsGEVLLNGRRLTALPAEQRRIGILF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNVAYGLmVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG4136  83 QDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16129400 163 GALDLKLREQM-QLELKKLQQsLGITFIFVTHDQGEALSMS 202
Cdd:COG4136 162 SKLDAALRAQFrEFVFEQIRQ-RGIPALLVTHDEEDAPAAG 201
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 6-211 9.27e-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: 167.71  E-value: 9.27e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP------PWERDVN 79
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSID 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TvfqdyaLFPhMSILDNVAYGL-----MVKGVNKKQRHAmAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03235  81 R------DFP-ISVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 155 VLLLDEPLGALDLKLREQMQLELKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRT 208
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 35-232 6.70e-50

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: 169.91  E-value: 6.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    35 MLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN------LPPWERDVNTVFQDYALFPHMSILDNVAYGLmvKGVNK 108
Cdd:TIGR02142  28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGM--KRARP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   109 KQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITF 188
Cdd:TIGR02142 106 SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPI 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 16129400   189 IFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVA 232
Cdd:TIGR02142 186 LYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
6-213 2.17e-49

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 164.22  E-value: 2.17e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTVFQ 83
Cdd:COG4619   2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPhMSILDNVAYGLMVKgvNKKQRHAMAQEALEKVALG-FVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG4619  82 EPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16129400 163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 4-215 6.88e-49

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: 163.76  E-value: 6.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGD----VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER--- 76
Cdd:COG4181   8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  77 ---DVNTVFQDYALFPHMSILDNVAYGLMVKGVnkKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEP 153
Cdd:COG4181  88 rarHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 154 RVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEAlSMSDRVAVFNNGRIEQ 215
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 24-216 7.07e-49

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: 163.11  E-value: 7.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYG--- 100
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlhp 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   101 -LMVKGVNKKQRHAMAQEalekVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKK 179
Cdd:TIGR01277  98 gLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 16129400   180 LQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQV 216
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 8-213 2.71e-48

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: 162.22  E-value: 2.71e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP---WERDVNTVFQD 84
Cdd:cd03219   4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGL-------MVKGVNKKQRHAM---AQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03219  84 PRLFPELTVLENVMVAAqartgsgLLLARARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
2-238 2.18e-47

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 160.74  E-value: 2.18e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   2 TYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-------ASNLPPW 74
Cdd:COG4598   6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrDGELVPA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  75 ERD--------VNTVFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAI 145
Cdd:COG4598  86 DRRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 146 ARALVNEPRVLLLDEPLGALDLKLreqmQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPEL----VGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241

                       250
                ....*....|....*.
gi 16129400 223 YMRPRTPFVAGFVGTS 238
Cdd:COG4598 242 FGNPKSERLRQFLSSS 257
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 5-213 2.36e-47

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 159.11  E-value: 2.36e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNL-----PPWERDV 78
Cdd:cd03292   1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03292  81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 159 DEPLGALDLKL-REQMQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03292 161 DEPTGNLDPDTtWEIMNL-LKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 5-222 4.57e-47

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: 158.69  E-value: 4.57e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-PWERDVNTVFQ 83
Cdd:cd03265   1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVA-----YGlmVKGVNKKQRhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03265  81 DLSVDDELTGWENLYiharlYG--VPGAERRER---IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400 159 DEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-227 1.52e-46

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 158.28  E-value: 1.52e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlSGGAISIFGKP--ASNL 71
Cdd:COG1117   8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDiyDPDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  72 PPWE--RDVNTVFQDYALFPhMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVAL-GFVHQR--KP-SQLSGGQRQRVA 144
Cdd:COG1117  86 DVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKDRlkKSaLGLSGGQQQRLC 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 145 IARALVNEPRVLLLDEPLGALD----LKLREQMQlELKKlqqslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPR 220
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpistAKIEELIL-ELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238


                ....*..
gi 16129400 221 DLYMRPR 227
Cdd:COG1117 239 QIFTNPK 245
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 6-213 2.27e-46

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: 155.29  E-value: 2.27e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERdvntvfqdy 85
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  86 alfphmsiLDNVAYglmvkgvnkkqrhaMAQeALEKV-ALGFVHqRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03214  72 --------ARKIAY--------------VPQ-ALELLgLAHLAD-RPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129400 165 LDLKlreqMQLE----LKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03214 128 LDIA----HQIEllelLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-212 3.67e-46

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: 153.94  E-value: 3.67e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERdvntvfqdy 85
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  86 alfphmsildnvayglmvkgvnkkQRHamaqealekvaLGFVHQrkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd00267  72 ------------------------RRR-----------IGYVPQ-----LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16129400 166 DLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 5-223 6.09e-46

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: 156.30  E-value: 6.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYG-DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-----ASNLPPWERDV 78
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrGKKLRKLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    79 NTVFQDYALFPHMSILDNVAYGL--------MVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALV 150
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400   151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 5-213 7.15e-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: 155.04  E-value: 7.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGeFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERD-VNTVFQ 83
Cdd:cd03264   1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03264  80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16129400 164 ALDLKLREQMQLELKKLqqSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03264 160 GLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 4-234 9.94e-46

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 155.94  E-value: 9.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI------FGKP--ASNLPPWE 75
Cdd:PRK11124   2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTpsDKAIRELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 RDVNTVFQDYALFPHMSILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK11124  82 RNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSprDLYMRPRTPFVAG 233
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIvEQGDA--SCFTQPQTEAFKN 238


                 .
gi 16129400  234 F 234
Cdd:PRK11124 239 Y 239
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 5-225 1.46e-45

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: 156.05  E-value: 1.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLY--GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG---KPASNLppWE--RD 77
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtLDEENL--WEirKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    78 VNTVFQDyalfPhmsilDN----------VAYGLMVKGVNKKQRHAMAQEALEKVAL-GFVHqRKPSQLSGGQRQRVAIA 146
Cdd:TIGR04520  79 VGMVFQN----P-----DNqfvgatveddVAFGLENLGVPREEMRKRVDEALKLVGMeDFRD-REPHLLSGGQKQRVAIA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400   147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALsMSDRVAVFNNGRIEQVDSPRDLYMR 225
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-213 2.70e-45

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 154.35  E-value: 2.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLM- 102
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNp 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  103 -VKgVNKKQRHAMAQEAlEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQ 181
Cdd:PRK10771  99 gLK-LNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176

                        170       180       190
                 ....*....|....*....|....*....|..
gi 16129400  182 QSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 9-205 2.96e-45

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: 153.15  E-value: 2.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     9 NVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKpaSNLPPWERDVNT-------- 80
Cdd:TIGR03608   3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKKASKfrreklgy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 16129400   161 PLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDQgEALSMSDRV 205
Cdd:TIGR03608 161 PTGSLDPKNRDEvLDL-LLELNDE-GKTIIIVTHDP-EVAKQADRV 203
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 16-213 4.26e-45

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: 153.28  E-value: 4.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    16 DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER------DVNTVFQDYALFP 89
Cdd:TIGR02211  17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    90 HMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:TIGR02211  97 DFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 16129400   170 REQMQLELKKLQQSLGITFIFVTHDQGEALSMsDRVAVFNNGRI 213
Cdd:TIGR02211 177 AKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 5-229 6.55e-45

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 156.50  E-value: 6.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLY----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE----- 75
Cdd:PRK11153   2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  156 LLLDEPLGALD-------LKLreqmqleLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:PRK11153 162 LLCDEATSALDpattrsiLEL-------LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234


                 .
gi 16129400  229 P 229
Cdd:PRK11153 235 P 235
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
19-241 1.72e-44

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 157.12  E-value: 1.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE------RDVNTVFQDYALFPHMS 92
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   93 ILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400  173 MQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGF---VGTSNVF 241
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFfrgVDISQVF 274
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 5-212 1.17e-43

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: 147.91  E-value: 1.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNT 80
Cdd:cd03228   1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFpHMSILDNVayglmvkgvnkkqrhamaqealekvalgfvhqrkpsqLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03228  81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129400 161 PLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGR 212
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
4-234 1.25e-43

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 150.16  E-value: 1.25e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG-----------KPASNLp 72
Cdd:COG4161   2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLL- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  73 pwERDVNTVFQDYALFPHMSILDN-VAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:COG4161  81 --RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSprDLYMRPRTPF 230
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIiEQGDA--SHFTQPQTEA 235


                ....
gi 16129400 231 VAGF 234
Cdd:COG4161 236 FAHY 239
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 6-222 5.04e-43

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: 147.97  E-value: 5.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVF 82
Cdd:cd03224   2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNvaygLMVKGVNKKQRHamAQEALEKV-----ALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:cd03224  82 EGRRIFPELTVEEN----LLLGAYARRRAK--RKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 158 LDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 20-225 1.04e-42

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: 148.80  E-value: 1.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-----WERDVNTVFQDY--ALFPHMS 92
Cdd:TIGR02769  27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQDSpsAVNPRMT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    93 ILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:TIGR02769 107 VRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400   171 EQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSPRDLYMR 225
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDVAQLLSFK 242
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 4-222 1.31e-42

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: 156.53  E-value: 1.31e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVS-RLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVN 79
Cdd:COG2274 473 DIELENVSfRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIG 552

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFpHMSILDNVAYGLmvKGVNKKQrhamAQEALEKVAL-GFVHQRkP-----------SQLSGGQRQRVAIAR 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGD--PDATDEE----IIEAARLAGLhDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIAR 624

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEEL 696
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-225 4.28e-42

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 147.57  E-value: 4.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVR---AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE-- 75
Cdd:PRK13650   1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDir 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 RDVNTVFQDY-ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13650  81 HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400  155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEaLSMSDRVAVFNNGRIEQVDSPRDLYMR 225
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
20-213 4.28e-42

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 147.14  E-value: 4.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-----PWERDVNTVFQDY--ALFPHMS 92
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQDSisAVNPRKT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   93 ILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16129400  171 EQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 4-237 6.21e-42

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 146.05  E-value: 6.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI----------FGKPASNLPP 73
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLIRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   74 WERDVNTVFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNE 152
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP--- 229
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPrtr 241


                 ....*....
gi 16129400  230 -FVAGFVGT 237
Cdd:PRK11264 242 qFLEKFLLQ 250
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-213 9.41e-42

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 151.71  E-value: 9.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP---WERD 77
Cdd:COG1129   1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 VNTVFQDYALFPHMSILDNVAYGLMVKG---VNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1129  81 IAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 155 VLLLDEPLGALDLKLREQMqLEL-KKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1129 161 VLILDEPTASLTEREVERL-FRIiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-161 1.80e-41

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: 141.63  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400    98 AYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRK----PSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 5-222 3.57e-41

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: 143.03  E-value: 3.57e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVR--AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-ASNLPPWERDVNTV 81
Cdd:cd03263   1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:cd03263  81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400 162 LGALDLKLREQMQLELKKLQQslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 5-213 1.02e-40

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 141.59  E-value: 1.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQD 84
Cdd:cd03268   1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQrhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03268  81 PGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16129400 165 LDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 5-213 4.97e-40

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: 140.20  E-value: 4.97e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVR----AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-PWERDVN 79
Cdd:cd03266   2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03266  82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16129400 160 EPLGALDLkLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03266 162 EPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 4-213 2.39e-39

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: 139.45  E-value: 2.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE-QLSGGAISIFGKPASNLPPWE-RD---- 77
Cdd:COG1119   3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWElRKrigl 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 VNTVFQDYaLFPHMSILDNVAYGL-----MVKGVNKKQRHAmAQEALEkvALGFVH--QRKPSQLSGGQRQRVAIARALV 150
Cdd:COG1119  83 VSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRER-ARELLE--LLGLAHlaDRPFGTLSQGEQRRVLIARALV 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
4-222 3.07e-39

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 146.08  E-value: 3.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNT 80
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIGV 418

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFpHMSILDNVAYGlmvkgvNKKQRHAMAQEALEKV-ALGFVhQRKP-----------SQLSGGQRQRVAIARA 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAqAHEFI-EALPdgydtvvgergVNLSGGQRQRIAIARA 490

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDqgeaLS---MSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHR----LStirNADRILVLDDGRIVEQGTHEEL 561
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 5-213 3.57e-39

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: 137.80  E-value: 3.57e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-------PWERd 77
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 vntvfqdyALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:cd03269  80 --------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 158 LDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 5-194 9.46e-39

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: 136.45  E-value: 9.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-WERDVNTVFQ 83
Cdd:COG4133   3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYALFPHMSILDNVAYGLMVKGVnkKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG4133  83 ADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 16129400 164 ALDLK----LREQMQLELKKlqqslGITFIFVTHD 194
Cdd:COG4133 161 ALDAAgvalLAELIAAHLAR-----GGAVLLTTHQ 190
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 4-213 1.79e-38

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: 136.18  E-value: 1.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVN 79
Cdd:cd03245   2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFpHMSILDNVAYGLmvkgvnkkqRHAMAQEALEKVALGFVHQ---RKP-----------SQLSGGQRQRVAI 145
Cdd:cd03245  82 YVPQDVTLF-YGTLRDNITLGA---------PLADDERILRAAELAGVTDfvnKHPngldlqigergRGLSGGQRQAVAL 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 146 ARALVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSL-GITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 5-213 2.91e-38

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: 133.71  E-value: 2.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWErdvntvfqd 84
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 yalfphmsildnvayglmvkgvnkkqrhamAQEAlekvALGFVHQrkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03216  72 ------------------------------ARRA----GIAMVYQ-----LSVGERQMVEIARALARNARLLILDEPTAA 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16129400 165 LDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 15-229 4.76e-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: 142.13  E-value: 4.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKT----TCLRLIAGFEQLSGGAISIFGKPASNLPPWE------RDVNTVFQD 84
Cdd:COG4172  21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 --YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVHQR---KPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLLIA 180

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 159 DEPLGALDLKLREQMqLEL-KKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG4172 181 DEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHP 251
cbiO PRK13640
energy-coupling factor transporter ATPase;
4-226 6.89e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 136.47  E-value: 6.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVR--AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF---EQLSGGAISIFGKPASNLPPWE-RD 77
Cdd:PRK13640   5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiRE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 -VNTVFQDY-ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13640  85 kVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400  156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEAlSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
5-213 1.09e-37

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 134.23  E-value: 1.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNL-----PPWERDV 78
Cdd:PRK10908   2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK10908  82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  159 DEPLGALDLKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10908 162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-213 1.13e-37

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 136.39  E-value: 1.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-------PWER 76
Cdd:COG4152   1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  77 dvntvfqdyALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:COG4152  81 ---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400 157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 4-223 1.13e-37

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: 141.43  E-value: 1.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNT 80
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPasWRRQIAW 415

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFpHMSILDNVAYGlmvkgvnkkQRHA-MAQ--EALEKVAL-GFVhQRKP-----------SQLSGGQRQRVAI 145
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLG---------RPDAsDEEleAALEAAGLdEFV-AALPdgldtplgeggRGLSGGQAQRLAL 484

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
cbiO PRK13637
energy-coupling factor transporter ATPase;
18-223 1.20e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 135.95  E-value: 1.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG----KPASNLPPWERDVNTVFQ--DYALFPHm 91
Cdd:PRK13637  21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVKLSDIRKKVGLVFQypEYQLFEE- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF--VHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129400  170 REQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 5-223 2.00e-37

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: 133.82  E-value: 2.00e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY---GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNL-PPWERD-VN 79
Cdd:cd03249   1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnLRWLRSqIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 TVFQDYALFPhMSILDNVAYGL------MVKGVNKKqrhAMAQEALEKVALGF---VHQRKpSQLSGGQRQRVAIARALV 150
Cdd:cd03249  81 LVSQEPVLFD-GTIAENIRYGKpdatdeEVEEAAKK---ANIHDFIMSLPDGYdtlVGERG-SQLSGGQKQRIAIARALL 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400 151 NEPRVLLLDEPLGALDLKLREQMQlelKKLQQ-SLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQ---EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
14-238 4.32e-37

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 133.56  E-value: 4.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS---------------NLPPWERDV 78
Cdd:PRK10619  15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLLRTRL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   79 NTVFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVHQRK-PSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK10619  95 TMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253


                 ..
gi 16129400  237 TS 238
Cdd:PRK10619 254 GS 255
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 8-213 4.95e-37

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: 132.67  E-value: 4.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVFQD 84
Cdd:cd03218   4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03218  84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16129400 165 LDLKLREQMQLELKKLQQSlGITfIFVT-HDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKV 211
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 1-227 4.99e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 133.43  E-value: 4.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG-----GAISIFGKP--ASNLPP 73
Cdd:PRK14267   1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiySPDVDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   74 WE--RDVNTVFQDYALFPHMSILDNVAYGLMVKGV--NKKQRHAMAQEALEKVAL-GFVHQR---KPSQLSGGQRQRVAI 145
Cdd:PRK14267  81 IEvrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  146 ARALVNEPRVLLLDEPLGALD---LKLREQMQLELKKlqqslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235


                 ....*
gi 16129400  223 YMRPR 227
Cdd:PRK14267 236 FENPE 240
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 17-213 5.37e-37

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 133.67  E-value: 5.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER--DVNTVFQDYAL--FPHMS 92
Cdd:COG1101  19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  93 ILDNVA--------YGLmVKGVNKKQRhAMAQEALEKVALGFVHQ--RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG1101  99 IEENLAlayrrgkrRGL-RRGLTKKRR-ELFRELLATLGLGLENRldTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHT 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129400 163 GALDLKlREQMQLEL-KKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1101 177 AALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 4-221 6.00e-37

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: 140.39  E-value: 6.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     4 AVEFDNVSRLY-GDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVN 79
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    80 TVFQDYALFpHMSILDNVAYGlmvkgvnkkQRHAMAQEALEKVALGFVH---QRKPS-----------QLSGGQRQRVAI 145
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG---------APYADDEEILRAAELAGVTefvRRHPDgldmqigergrSLSGGQRQAVAL 612

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400   146 ARALVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSL-GITFIFVTHdQGEALSMSDRVAVFNNGRIeQVDSPRD 221
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERF---KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI-VADGPKD 684
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
8-221 1.33e-36

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 132.16  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE----RDVntVFQ 83
Cdd:COG4559   5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  84 DYAL-FPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKV-ALGFVHQRKPsQLSGGQRQRVAIARALV-------NEPR 154
Cdd:COG4559  83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVgLAHLAGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPR 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 155 VLLLDEPLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAvLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
23-205 1.33e-36

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 131.86  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPW------ERDVNTVFQDYALFPHMSILDN 96
Cdd:PRK11629  28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFTALEN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   97 VAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE 176
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187

                        170       180
                 ....*....|....*....|....*....
gi 16129400  177 LKKLQQSLGITFIFVTHDQGEALSMSDRV 205
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 6-222 1.85e-36

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: 131.26  E-value: 1.85e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVF 82
Cdd:COG0410   5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNvaygLMVKGVNKKQRHAmAQEALEKV-----ALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG0410  85 EGRRIFPSLTVEEN----LLLGAYARRDRAE-VRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400 158 LDEP-LGaLDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG0410 160 LDEPsLG-LAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
19-223 3.24e-36

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 132.06  E-value: 3.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTVFQDY-ALFPHMSILD 95
Cdd:PRK13635  22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQNPdNQFVGATVQD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   96 NVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16129400  176 ELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 9-222 3.83e-36

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: 136.86  E-value: 3.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     9 NVSRLY-----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI-FGKP---ASNLPPWERD-- 77
Cdd:TIGR03269 284 NVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwvdMTKPGPDGRGra 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    78 ---VNTVFQDYALFPHMSILDNVAYGLmvkGVNKKQRHAMAQEALEKVALGF-------VHQRKPSQLSGGQRQRVAIAR 147
Cdd:TIGR03269 364 kryIGILHQEYDLYPHRTVLDNLTEAI---GLELPDELARMKAVITLKMVGFdeekaeeILDKYPDELSEGERHRVALAQ 440

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400   148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 17-230 4.90e-36

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 132.78  E-value: 4.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE-----RDVNTVFQD-YA-LFP 89
Cdd:PRK11308  28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   90 HMSILDNVAYGLMVK-GVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK11308 108 RKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 8-221 8.56e-36

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 130.28  E-value: 8.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE----RDVntVFQ 83
Cdd:PRK13548   6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrRAV--LPQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYAL-FPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALV------NEPRVL 156
Cdd:PRK13548  84 HSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  157 LLDEPLGALDlkLREQ---MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:PRK13548 163 LLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 14-235 8.87e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 130.03  E-value: 8.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRL------------IAGFEQLSGGaiSIFGKPASNLppwERDVNTV 81
Cdd:PRK14247  13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQ--DIFKMDVIEL---RRRVQMV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   82 FQDYALFPHMSILDNVAYGLMVKGV--NKKQRHAMAQEALEKVAL-GFVHQR---KPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK14247  88 FQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  156 LLLDEPLGALD----LKLrEQMQLELKKlqqslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFV 231
Cdd:PRK14247 168 LLADEPTANLDpentAKI-ESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241


                 ....
gi 16129400  232 AGFV 235
Cdd:PRK14247 242 EKYV 245
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
37-230 9.64e-36

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 132.69  E-value: 9.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   37 GPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS------NLPPWERDVNTVFQDYALFPHMSILDNVAYGLmvkgvnkkq 110
Cdd:PRK11144  31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM--------- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  111 RHAMAQEALEKVA-LGFVH--QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL-KLREQMQLeLKKLQQSLGI 186
Cdd:PRK11144 102 AKSMVAQFDKIVAlLGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELLPY-LERLAREINI 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16129400  187 TFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY----MRPRTPF 230
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWassaMRPWLPK 228
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-213 1.15e-35

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 136.39  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLY----GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE- 75
Cdd:PRK10535   1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 -----RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALV 150
Cdd:PRK10535  81 aqlrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEAlSMSDRVAVFNNGRI 213
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 9-226 1.50e-35

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 129.51  E-value: 1.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    9 NVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLS-----GGAISIFGK----PASNLPPWERDVN 79
Cdd:PRK14239  10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHniysPRTDTVDLRKEIG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   80 TVFQDYALFPhMSILDNVAYGLMVKGVNKKQRhamAQEALEKVALGF-----VHQRKPSQ---LSGGQRQRVAIARALVN 151
Cdd:PRK14239  90 MVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSLKGAsiwdeVKDRLHDSalgLSGGQQQRVCIARVLAT 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgiTFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 22-194 3.39e-35

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 127.97  E-value: 3.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER------DVNTVFQDYALFPHMSILD 95
Cdd:PRK10584  28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   96 NVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187

                        170
                 ....*....|....*....
gi 16129400  176 ELKKLQQSLGITFIFVTHD 194
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHD 206
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 4-222 5.08e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 128.57  E-value: 5.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVR--AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS--NLPPWERDVN 79
Cdd:PRK13632   7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   80 TVFQ--DYAlFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK13632  87 IIFQnpDNQ-FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALsMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 9-235 7.78e-35

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 127.86  E-value: 7.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    9 NVSRLY---GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI------FGKPASNLPP--WERD 77
Cdd:PRK14246  12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyFGKDIFQIDAikLRKE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDYALFPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVAL-GFVHQR---KPSQLSGGQRQRVAIARALVNE 152
Cdd:PRK14246  92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALK 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVA 232
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249


                 ...
gi 16129400  233 GFV 235
Cdd:PRK14246 250 KYV 252
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 12-225 8.97e-35

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 132.91  E-value: 8.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   12 RLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTC----LRLIAgfeqlSGGAISIFGKPASNLP-----PWERDVNTVF 82
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVF 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   83 QD--YALFPHMSILDNVAYGLMV--KGVNKKQRHAMAQEALEKVALG-FVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK15134 369 QDpnSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLII 448

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVD------SPRDLYMR 225
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQGDcervfaAPQQEYTR 523
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 18-230 2.30e-34

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 128.29  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER-----DVNTVFQD--YALFPH 90
Cdd:PRK15079  35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   91 MSILDNVAYGL------MVKGVNKKQRHAMaqeaLEKVAL-GFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK15079 115 MTIGEIIAEPLrtyhpkLSRQEVKDRVKAM----MLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 18-226 2.44e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 127.44  E-value: 2.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI------FGKPASNLPPWERDVNTVFQ--DYALFP 89
Cdd:PRK13634  21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQLFE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   90 HmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-222 7.17e-34

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 126.46  E-value: 7.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERD-VN 79
Cdd:PRK13537   4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13537  84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 14-212 1.05e-33

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 124.72  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE---RDVNTVFQDYALFPH 90
Cdd:PRK11300  15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFRE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   91 MSILDN--VAYGLMVK-----------GVNKKQRHAMAQEA--LEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11300  95 MTVIENllVAQHQQLKtglfsgllktpAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 11-230 1.48e-33

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 130.36  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   11 SRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK-----PASNLPPWERDVNTVFQD- 84
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQDp 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YA-LFPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVALGFVHQ-RKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10261 411 YAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEA 490

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 8-213 1.95e-33

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 123.60  E-value: 1.95e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVFQD 84
Cdd:COG1137   7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIGYLPQE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG1137  87 ASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16129400 165 LDLKLREQMQLELKKLQQSlGITfIFVT-HDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1137 167 VDPIAVADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGKV 214
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 3-226 2.48e-33

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: 129.12  E-value: 2.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   3 YAVEFDNVSRLY--GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDV 78
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddLRRRI 411

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  79 NTVFQDYALFpHMSILDNVAYGlmvkgvNKKQRHAMAQEALEKVALGFVHQRKP-----------SQLSGGQRQRVAIAR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQN 560
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 5-213 1.01e-32

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: 121.42  E-value: 1.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLY---GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPasnLPPWE-----R 76
Cdd:cd03248  12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEhkylhS 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  77 DVNTVFQDYALFPHmSILDNVAYGLMVKG---VNKKQRHAMAQEALEKVALGFVHQ--RKPSQLSGGQRQRVAIARALVN 151
Cdd:cd03248  89 KVSLVGQEPVLFAR-SLQDNIAYGLQSCSfecVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIR 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 152 EPRVLLLDEPLGALDLKLREQMQlelKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
4-223 2.15e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 122.25  E-value: 2.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYG-----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS------NLP 72
Cdd:PRK13641   2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   73 PWERDVNTVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VHQRKPSQLSGGQRQRVAIARAL 149
Cdd:PRK13641  82 KLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-212 2.75e-32

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 125.52  E-value: 2.75e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPweRD--- 77
Cdd:COG3845   2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP--RDaia 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  78 --VNTVFQDYALFPHMSILDNVAYGLMVKG---VNKKQRHAMAQEALEKvaLGF-VH-QRKPSQLSGGQRQRVAIARALV 150
Cdd:COG3845  80 lgIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSER--YGLdVDpDAKVEDLSVGEQQRVEILKALY 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGK 218
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 5-223 3.11e-32

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 120.03  E-value: 3.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN--LPPWERDVNT 80
Cdd:cd03251   1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFpHMSILDNVAYGlmVKGVNKKQ-----RHAMAQEALEKVALGF---VHQRKpSQLSGGQRQRVAIARALVNE 152
Cdd:cd03251  81 VSQDVFLF-NDTVAENIAYG--RPGATREEveeaaRAANAHEFIMELPEGYdtvIGERG-VKLSGGQRQRIAIARALLKD 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDLY 223
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH----RLSTienADRIVVLEDGKIVERGTHEELL 224
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 18-213 5.27e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 121.35  E-value: 5.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTclrLIAGFEQL---SGGAISIF-----GKPASNLPPWE-------------- 75
Cdd:PRK13651  21 KALDNVSVEINQGEFIAIIGQTGSGKTT---FIEHLNALllpDTGTIEWIfkdekNKKKTKEKEKVleklviqktrfkki 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 -------RDVNTVFQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAI 145
Cdd:PRK13651  98 kkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQRSPFELSGGQKRRVAL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 5-222 5.80e-32

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: 119.25  E-value: 5.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP--PWERDVNTV 81
Cdd:cd03254   3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFPHmSILDNVAYG---LMVKGVNKKQRHAMAQEALEKVALGFVHQRKP--SQLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03254  83 LQDTFLFSG-TIMENIRLGrpnATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGEngGNLSQGERQLLAIARAMLRDPKIL 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 157 LLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTHDEL 224
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 8-213 5.95e-32

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: 119.69  E-value: 5.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVFQD 84
Cdd:TIGR04406   5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    85 YALFPHMSILDNVAYGL-MVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:TIGR04406  85 ASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 16129400   164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKV 213
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 6-213 9.68e-32

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: 116.93  E-value: 9.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRLYGDVRA--VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNTV 81
Cdd:cd03246   2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGYL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFPHmSILDNVayglmvkgvnkkqrhamaqealekvalgfvhqrkpsqLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:cd03246  82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129400 162 LGALDLKlREQMQLELKKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:cd03246 124 NSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1-213 1.01e-31

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 119.56  E-value: 1.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRLY---------GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--AS 69
Cdd:COG4167   1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKleYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  70 NLPPWERDVNTVFQD--YALFPHM---SILD-----NVAYglmvkgvNKKQRHAMAQEALEKVALGFVHQR-KPSQLSGG 138
Cdd:COG4167  81 DYKYRCKHIRMIFQDpnTSLNPRLnigQILEeplrlNTDL-------TAEEREERIFATLRLVGLLPEHANfYPHMLSSG 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 139 QRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 1-213 1.92e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.07  E-value: 1.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERD 77
Cdd:PRK13647   1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnAENEKWVRSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDY--ALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13647  81 VGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  156 LLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 5-223 3.20e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 118.32  E-value: 3.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLY-GDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERDVNT 80
Cdd:PRK13648   8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQD-YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13648  88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400  160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
cbiO PRK13649
energy-coupling factor transporter ATPase;
4-223 3.73e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 118.69  E-value: 3.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYG-----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN------LP 72
Cdd:PRK13649   2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   73 PWERDVNTVFQdyalFPHM-----SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALG-FVHQRKPSQLSGGQRQRVAIA 146
Cdd:PRK13649  82 QIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 5-213 4.28e-31

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: 117.33  E-value: 4.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN--LPPWERDVNTV 81
Cdd:cd03253   1 IEFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 FQDYALFpHMSILDNVAYGLMvkGVNKKQ-----RHAMAQEALEKVALGF---VHQRKpSQLSGGQRQRVAIARALVNEP 153
Cdd:cd03253  81 PQDTVLF-NDTIGYNIRYGRP--DATDEEvieaaKAAQIHDKIMRFPDGYdtiVGERG-LKLSGGEKQRVAIARAILKNP 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 154 RVLLLDEPLGALDLKLREQMQLELKKLqqSLGITFIFVTHDQGEALSmSDRVAVFNNGRI 213
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-220 1.04e-30

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 117.04  E-value: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF---EQLSGGAISIFGKPASNLPPWERD 77
Cdd:PRK09984   1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNT-------VFQDYALFPHMSILDNVAYGLM---------VKGVNKKQRHAmAQEALEKVALG-FVHQRKpSQLSGGQR 140
Cdd:PRK09984  81 IRKsrantgyIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQR-ALQALTRVGMVhFAHQRV-STLSGGQQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  141 QRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVA------VFNNGRIE 214
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIValrqghVFYDGSSQ 238


                 ....*.
gi 16129400  215 QVDSPR 220
Cdd:PRK09984 239 QFDNER 244
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 5-226 1.16e-30

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 116.34  E-value: 1.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwerdvntvfQD 84
Cdd:COG4604   2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---------RE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 YALfpHMSIL--DN-VAYGLMV------------KGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARAL 149
Cdd:COG4604  73 LAK--RLAILrqENhINSRLTVrelvafgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 150 VNEPRVLLLDEPLGALDLKL-REQMQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRP 226
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHsVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI-ITP 226
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 6-213 1.91e-30

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: 115.31  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVF 82
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    83 QDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQE---ALEKVAlgfvhQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:TIGR03410  82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16129400   160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-223 2.12e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 116.73  E-value: 2.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLY---GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK--PASNLPPWE 75
Cdd:PRK13642   1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 RDVNTVFQDY-ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13642  81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 30-222 2.42e-30

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


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 114.95  E-value: 2.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASnlpPWERDVNTVFQ------DYALFPHMSILDNVAYGLMV 103
Cdd:TIGR03771   6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQrhefawDFPISVAHTVMSGRTGHIGW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   104 KGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQS 183
Cdd:TIGR03771  83 LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA 162

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 16129400   184 lGITFIFVTHDQGEALSMSDRVAVFnNGRIEQVDSPRDL 222
Cdd:TIGR03771 163 -GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 19-226 2.50e-30

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: 115.16  E-value: 2.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    19 AVDGVSIAIKDGEFFSMLGPSGSGKT-TCLRLI----AGFEQLSGgAISIFGKPASNLPPWERDVNTVFQD--YALFPHM 91
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSlTCLAILgllpPGLTQTSG-EILLDGRPLLPLSIRGRHIATIMQNprTAFNPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF---VHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:TIGR02770  80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400   169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 4-222 3.61e-30

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: 120.83  E-value: 3.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     4 AVEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVN 79
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLG 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    80 TVFQDYALFPHmSILDNVAYGLMVKgvnkkqrHAMAQEALEKVALGFVHQRKP-----------SQLSGGQRQRVAIARA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400   149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQqslgITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAH----RLSTirnADRIYVLDAGRVVQQGTYDEL 671
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 2-209 4.12e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 115.26  E-value: 4.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    2 TYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlSGGAISIFGKP--ASNLP 72
Cdd:PRK14243   8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNlyAPDVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   73 PWE--RDVNTVFQDYALFPHmSILDNVAYGLMVKGVnKKQRHAMAQEALEKVALGFVHQRKPSQ----LSGGQRQRVAIA 146
Cdd:PRK14243  86 PVEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  147 RALVNEPRVLLLDEPLGALD----LKLREQMQlELKKlqqslGITFIFVTHDQGEALSMSDRVAVFN 209
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDpistLRIEELMH-ELKE-----QYTIIIVTHNMQQAARVSDMTAFFN 224
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 5-222 4.24e-30

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 120.21  E-value: 4.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYG--DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN--LPPWERDVNT 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    81 VFQDYALFPHmSILDNVAYGLMVKGVNKKQRHAM----AQEALEKVALGFVHQ--RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQADRAEIERALaaayAQDFVDKLPLGLDTPigENGVLLSGGQRQRLAIARALLKDAP 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400   155 VLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH----RLSTiekADRIVVMDDGRIVERGTHNEL 554
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 14-214 6.91e-30

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 113.78  E-value: 6.91e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLppwerDVNTVFQdyalfPHMSI 93
Cdd:cd03220  32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  94 LDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16129400 174 QLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIE 214
Cdd:cd03220 182 QRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 5-228 9.17e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 114.79  E-value: 9.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP----ASNLPPWERDVN 79
Cdd:PRK13639   2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydKKSLLEVRKTVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   80 TVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK13639  82 IVFQnpDDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400  158 LDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 4-194 1.48e-29

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: 118.16  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     4 AVEFDNVSRLYGDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNT 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAW 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    81 VFQDYALFPHmSILDNVAYGLmvkgvnKKQRHAMAQEALEKVALGFVHQRKP-----------SQLSGGQRQRVAIARAL 149
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR------PDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAF 473

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 16129400   150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHD 194
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 15-233 2.79e-29

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 114.82  E-value: 2.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKT----TCLRLIAGFEQLSGGAIsiF-GKPASNLPpwERDVN--------TV 81
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSAT--FnGREILNLP--EKELNklraeqisMI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   82 FQD--YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVHQRK---PSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK09473 103 FQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKL 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAG 233
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIG 260
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 4-216 5.87e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 112.44  E-value: 5.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG-----GAISIFGKPA----SNLPPW 74
Cdd:PRK14258   7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   75 ERDVNTVFQDYALFPhMSILDNVAYGLMVKGVNKK-QRHAMAQEALEKVAL--GFVHQRKPS--QLSGGQRQRVAIARAL 149
Cdd:PRK14258  87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdEIKHKIHKSalDLSGGQQQRLCIARAL 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVF--NNGRIEQV 216
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQL 234
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 3-223 9.53e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 112.25  E-value: 9.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    3 YAVEFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP----ASNLPPWERD 77
Cdd:PRK13636   4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysRKGLMKLRES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQ--DYALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13636  84 VGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  156 LLLDEPLGALDLK-LREQMQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13636 163 LVLDEPTAGLDPMgVSEIMKL-LVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-222 1.17e-28

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 113.39  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    2 TYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER-DVNT 80
Cdd:PRK13536  39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFPHMSILDN-VAYGLMVkGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENlLVFGRYF-GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  160 EPLGALDLKLREQMQLELKKLqQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 5-227 1.31e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 114.17  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTVF 82
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   83 QDYAL--------------FPHMSILDnvayglmvkGVNKKQRHAMaQEALEKVALGFVHQRKPSQLSGGQRQRVAIARA 148
Cdd:PRK09536  84 QDTSLsfefdvrqvvemgrTPHRSRFD---------TWTETDRAAV-ERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  149 LVNEPRVLLLDEPLGALDLKlREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR 227
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 8-213 2.64e-28

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 108.88  E-value: 2.64e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   8 DNVSRLYGDV-RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAsnlPPWER--DVNTVFQD 84
Cdd:cd03226   3 ENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERrkSIGYVMQD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 --YALFPHmSILDNVAYGLMVKGVNKKQrhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03226  80 vdYQLFTD-SVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16129400 163 GALDLKLREQMQLELKKLqQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03226 155 SGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 8-222 5.99e-28

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 108.83  E-value: 5.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVFQD 84
Cdd:PRK10895   7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK10895  87 ASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400  164 ALDlklrEQMQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK10895 167 GVD----PISVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
cbiO PRK13645
energy-coupling factor transporter ATPase;
7-223 6.65e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 110.10  E-value: 6.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    7 FDNVSRLYG-----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFeQLSGGAISIFG--------KPASNLPP 73
Cdd:PRK13645   9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL-IISETGQTIVGdyaipanlKKIKEVKR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   74 WERDVNTVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALV 150
Cdd:PRK13645  88 LRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGIIA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 9-236 6.97e-28

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 109.80  E-value: 6.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    9 NVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF-EQLSG---------GAISIFGkpASNLPPWERDV 78
Cdd:PRK14271  26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysgdvllGGRSIFN--YRDVLEFRRRV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   79 NTVFQDYALFPhMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVAL-GFVHQR---KPSQLSGGQRQRVAIARALVNEP 153
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  154 RVLLLDEPLGALDLKLREQMQLELKKLQQSLgiTFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR----TP 229
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKhaetAR 260


                 ....*..
gi 16129400  230 FVAGFVG 236
Cdd:PRK14271 261 YVAGLSG 267
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 10-213 7.83e-28

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 108.57  E-value: 7.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  10 VSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGkpasnLPPWERDV----------- 78
Cdd:cd03267  27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKkflrrigvvfg 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  79 --NTVFQD------YALFPHMSILDNVAYglmvkgvnkKQRHAMAQEALEkvaLGFVHQRKPSQLSGGQRQRVAIARALV 150
Cdd:cd03267 102 qkTQLWWDlpvidsFYLLAAIYDLPPARF---------KKRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALL 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 5-213 9.52e-28

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: 108.34  E-value: 9.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVS-RLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-ASNLPPW-ERDVNT 80
Cdd:cd03252   1 ITFEHVRfRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWlRRQVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFpHMSILDNVAY---GLMVKGVNKKQRHAMAQEALEKVALGF--VHQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03252  81 VLQENVLF-NRSIRDNIALadpGMSMERVIEAAKLAGAHDFISELPEGYdtIVGEQGAGLSGGQRQRIAIARALIHNPRI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 156 LLLDEPLGALDLKLREQMQLELKKLqqSLGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
cbiO PRK13646
energy-coupling factor transporter ATPase;
5-223 1.08e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 109.48  E-value: 1.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYG-----DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN------LPP 73
Cdd:PRK13646   3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   74 WERDVNTVFQdyalFPHMSIL-DNVA----YGLMVKGVNKKQRHAMAQEALekVALGF---VHQRKPSQLSGGQRQRVAI 145
Cdd:PRK13646  83 VRKRIGMVFQ----FPESQLFeDTVEreiiFGPKNFKMNLDEVKNYAHRLL--MDLGFsrdVMSQSPFQMSGGQMRKIAI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
cbiO PRK13643
energy-coupling factor transporter ATPase;
18-223 2.33e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 108.67  E-value: 2.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI------FGKPASNLPPWERDVNTVFQ--DYALFP 89
Cdd:PRK13643  20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKPVRKKVGVVFQfpESQLFE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   90 HmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PRK13643 100 E-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  169 LREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13643 179 ARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 5-226 3.45e-27

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 112.12  E-value: 3.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLY---GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPasnLPPWE-----R 76
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDhhylhR 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    77 DVNTVFQDYALFPHmSILDNVAYGLmvKGVNKKQRHAMAQEALekvALGFVHQ----------RKPSQLSGGQRQRVAIA 146
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAAN---AHDFIMEfpngydtevgEKGSQLSGGQKQRIAIA 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   147 RALVNEPRVLLLDEPLGALDLKLrEQMQLELKKLQqslGITFIFVTHDqgeaLSM---SDRVAVFNNGRIEQVDSPRDLY 223
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAEC-EQLLQESRSRA---SRTVLLIAHR----LSTverADQILVLKKGSVVEMGTHKQLM 701


                  ...
gi 16129400   224 MRP 226
Cdd:TIGR00958 702 EDQ 704
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 18-213 1.44e-26

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: 103.67  E-value: 1.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVF------QDYALFPHM 91
Cdd:cd03215  14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  92 SILDNVAYglmvkgvnkkqrhamaqealekvalgfvhqrkPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:cd03215  94 SVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 16129400 172 QMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
4-213 3.17e-26

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 109.28  E-value: 3.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS--NLPPWERDVNT 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAV 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFpHMSILDNVAYGlmvkgvNKKQRHAMAQEALEKV-ALGFVhQRKP-----------SQLSGGQRQRVAIARA 148
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVG------RPDATDEEMRAAAERAqAHDFI-ERKPdgydtvvgergRQLSGGERQRLAIARA 485

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgITFIfVTHdqgeALSM---SDRVAVFNNGRI 213
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGR-TTFI-IAH----RLSTvrnADRILVFDNGRV 547
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 5-226 3.75e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 104.88  E-value: 3.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLY-GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS--NLPPWERDVNTV 81
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   82 FQ--DYALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13652  84 FQnpDDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-221 4.28e-26

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 104.01  E-value: 4.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVS---RLY-------------------GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG 58
Cdd:COG1134   1 MSSMIEVENVSksyRLYhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  59 GAISIFGKPASNLppwerDVNTVFQdyalfPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALG-FVHQrkP-SQLS 136
Cdd:COG1134  81 GRVEVNGRVSALL-----ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGdFIDQ--PvKTYS 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 137 GGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQV 216
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227


                ....*
gi 16129400 217 DSPRD 221
Cdd:COG1134 228 GDPEE 232
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-223 5.85e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 104.40  E-value: 5.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVR------AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG---KPASNL 71
Cdd:PRK13633   1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   72 ppWE--RDVNTVFQDyalfPHMSIL-----DNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVA 144
Cdd:PRK13633  81 --WDirNKAGMVFQN----PDNQIVativeEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  145 IARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
5-226 7.37e-26

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 104.08  E-value: 7.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKpasNLPPWERD------- 77
Cdd:PRK11831   8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---NIPAMSRSrlytvrk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 -VNTVFQDYALFPHMSILDNVAYGLmvkgvnkkQRHAMAQEA---------LEKVALGFVHQRKPSQLSGGQRQRVAIAR 147
Cdd:PRK11831  85 rMSMLFQSGALFTDMNVFDNVAYPL--------REHTQLPAPllhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALAR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  148 ALVNEPRVLLLDEP--------LGALdLKLreqmqleLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSP 219
Cdd:PRK11831 157 AIALEPDLIMFDEPfvgqdpitMGVL-VKL-------ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228


                 ....*..
gi 16129400  220 RDLYMRP 226
Cdd:PRK11831 229 QALQANP 235
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 5-222 1.24e-25

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: 107.52  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYG-DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTV 81
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    82 FQDYALFPHmSILDNVAYG----LMVKGVNKKQRHAMAQEALEKVALGFvHQR---KPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGakenVSQDEIWAACEIAEIKDDIENMPLGY-QTElseEGSSISGGQKQRIALARALLTDSK 631

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400   155 VLLLDEPLGALDLKLREQMQLELKKLQQSlgiTFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 9-223 1.70e-25

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: 102.60  E-value: 1.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     9 NVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG----------FEQLSGGAISIFgkpasNLPPWER-- 76
Cdd:TIGR02323   8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlapdhgtatYIMRSGAELELY-----QLSEAERrr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    77 ----DVNTVFQDYA--LFPHMSILDNVAYGLMVKGvnkkQRH-----AMAQEALEKVALGFVH-QRKPSQLSGGQRQRVA 144
Cdd:TIGR02323  83 lmrtEWGFVHQNPRdgLRMRVSAGANIGERLMAIG----ARHygnirATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   145 IARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQV-D 217
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltDQVlD 238


                  ....*.
gi 16129400   218 SPRDLY 223
Cdd:TIGR02323 239 DPQHPY 244
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-236 1.73e-25

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 106.53  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP---ASNLPPWERD 77
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAALAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDYALFPHMSILDNVAYG-LMVKG--VNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK11288  81 VAIIYQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  155 VLLLDEPLGALDLKLREQmqleLKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRieQVDSPRDLYMRPRTPFV 231
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQ----LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQVDRDQLV 234


                 ....*
gi 16129400  232 AGFVG 236
Cdd:PRK11288 235 QAMVG 239
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 15-194 1.96e-25

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: 106.68  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTVFQDYALFpHMS 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    93 ILDNVAYGlmvkgvNKKQRHAMAQEALEKVALGFVHQRKP-----------SQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:TIGR02868 425 VRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498

                         170       180       190
                  ....*....|....*....|....*....|...
gi 16129400   162 LGALDLKLREQMQLELkkLQQSLGITFIFVTHD 194
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHH 529
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 8-223 3.07e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 101.93  E-value: 3.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS-----NLPPWER------ 76
Cdd:PRK11701  10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyALSEAERrrllrt 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   77 DVNTVFQDYA--LFPHMSILDNVAYGLMVKGvnkkQRH-----AMAQEALEKVALGfvHQR---KPSQLSGGQRQRVAIA 146
Cdd:PRK11701  90 EWGFVHQHPRdgLRMQVSAGGNIGERLMAVG----ARHygdirATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQV-DSP 219
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesgltDQVlDDP 243


                 ....
gi 16129400  220 RDLY 223
Cdd:PRK11701 244 QHPY 247
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-218 6.62e-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: 6.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP---WERD 77
Cdd:PRK11614   2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDYALFPHMSILDNVAYGLMVkgVNKKQRhamaQEALEKVALGF--VHQRKPSQ---LSGGQRQRVAIARALVNE 152
Cdd:PRK11614  82 VAIVPEGRRVFSRMTVEENLAMGGFF--AERDQF----QERIKWVYELFprLHERRIQRagtMSGGEQQMLAIGRALMSQ 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400  153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDS 218
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 1-212 1.01e-24

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 104.24  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GAISIFGKP--ASN 70
Cdd:PRK13549   2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV------LSGvyphgtyeGEIIFEGEElqASN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   71 LPPWERD-VNTVFQDYALFPHMSILDNVAYG--LMVKGV-NKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIA 146
Cdd:PRK13549  76 IRDTERAgIAIIHQELALVKELSVLENIFLGneITPGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400  147 RALVNEPRVLLLDEPLGALDLKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 16-226 1.22e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 101.85  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   16 DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI------------------FGKPASNLPPWERD 77
Cdd:PRK13631  38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpYSKKIKNFKELRRR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVH-QRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlERSPFGLSGGQKRRVAIAGILAIQPE 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  155 VLLLDEPLGALDLK-LREQMQLELKKLQQslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13631 197 ILIFDEPTAGLDPKgEHEMMQLILDAKAN--NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
8-227 1.75e-24

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 100.09  E-value: 1.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwerdvNTVFQDYAL 87
Cdd:PRK11231   6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARRLAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   88 FP--HM-----SILDNVAYG----LMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK11231  81 LPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400  157 LLDEPLGALDLklreQMQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRPR 227
Cdd:PRK11231 161 LLDEPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV-MTPG 229
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 7-194 1.81e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 103.61  E-value: 1.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   7 FDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgkpasnlPPWERdVNTVFQDYA 86
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  87 LFPHMSILDNV----------------AYGLMVKGVNKKQRHAMAQEALE---------KVA-----LGF---VHQRKPS 133
Cdd:COG0488  72 LDDDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEalggweaeaRAEeilsgLGFpeeDLDRPVS 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 134 QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK----LREQmqlelkkLQQSLGiTFIFVTHD 194
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEF-------LKNYPG-TVLVVSHD 208
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 10-213 3.58e-24

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 100.55  E-value: 3.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  10 VSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGkpasnLPPWE------RDVNTVF- 82
Cdd:COG4586  28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKrrkefaRRIGVVFg 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNvaYGLM--VKGVNK---KQRHAMAQEALEkvaLG-FVHQ--RkpsQLSGGQRQRVAIARALVNEPR 154
Cdd:COG4586 103 QRSQLWWDLPAIDS--FRLLkaIYRIPDaeyKKRLDELVELLD---LGeLLDTpvR---QLSLGQRMRCELAAALLHRPK 174

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 155 VLLLDEP-LGaLDLKLREQMQLELKKLQQSLGITFIFVTHDQG--EALsmSDRVAVFNNGRI 213
Cdd:COG4586 175 ILFLDEPtIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRI 233
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 16-213 3.66e-24

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: 98.50  E-value: 3.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  16 DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGAISIFGKPaSNLPPWERDVNTVFQDYALFPHMS 92
Cdd:cd03234  19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQP-RKPDQFQKCVAYVRQDDILLPGLT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  93 ILDNVAYGLMVKGVN---KKQRHAM-AQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:cd03234  98 VRETLTYTAILRLPRkssDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16129400 169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 12-229 7.67e-24

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 98.23  E-value: 7.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   12 RLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKT-TCLRLI----AGFEQLSGgAISIFGKPASNLPPWERDVNTVFQD-- 84
Cdd:PRK10418  11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAG-RVLLDGKPVAPCALRGRKIATIMQNpr 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 YALFPHMSILDNVAYGLMVKGvnKKQRHAMAQEALEKVALGFVH---QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10418  90 SAFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
6-213 7.88e-24

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 101.63  E-value: 7.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   6 EFDNVSRlygdVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE---------- 75
Cdd:COG1129 258 EVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvp 333

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  76 --RdvntvfQDYALFPHMSILDNVAYGLMVKG-----VNKKQRHAMAQEALEKVALGFVHQRKP-SQLSGGQRQRVAIAR 147
Cdd:COG1129 334 edR------KGEGLVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAK 407

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400 148 ALVNEPRVLLLDEP-----LGAldlKlREQMQLeLKKL-QQSLGItfIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1129 408 WLATDPKVLILDEPtrgidVGA---K-AEIYRL-IRELaAEGKAV--IVISSELPELLGLSDRILVMREGRI 472
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 5-221 8.39e-24

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: 101.75  E-value: 8.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVS-RLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlppWERDVNTVF 82
Cdd:COG4618 331 LSVENLTvVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---WDREELGRH 407

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 -----QDYALFPHmSILDNVAyglmvkgvnkkqRHAMAQ-----EALEKVAlgfVH---QRKP-----------SQLSGG 138
Cdd:COG4618 408 igylpQDVELFDG-TIAENIA------------RFGDADpekvvAAAKLAG---VHemiLRLPdgydtrigeggARLSGG 471

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 139 QRQRVAIARALVNEPRVLLLDEPLGALD----LKLREQMQlELKKlqqsLGITFIFVTHDQGeALSMSDRVAVFNNGRIE 214
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDdegeAALAAAIR-ALKA----RGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545


                ....*..
gi 16129400 215 QVDsPRD 221
Cdd:COG4618 546 AFG-PRD 551
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 17-230 1.64e-23

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 101.09  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   17 VRAVDGVSIAIKDGEFFSMLGPSGSGKT-TCLRLIAGFEQLSGGA--------------ISIFGKPASNLPPWE-RDVNT 80
Cdd:PRK10261  29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSEQSAAQMRHVRgADMAM 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQD--YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVHQ---RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIAMALSCRPA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400  155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 20-213 1.98e-23

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: 95.70  E-value: 1.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGAIS----IFGKPaSNLPPWERDVNTVFQDYALFPHMSIld 95
Cdd:cd03213  25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVSgevlINGRP-LDKRSFRKIIGYVPQDDILHPTLTV-- 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  96 nvayglmvkgvnkkqrhamaQEALEKVAlgfvhqrKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:cd03213 100 --------------------RETLMFAA-------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16129400 176 ELKKLQQSlGITFIFVTHD-QGEALSMSDRVAVFNNGRI 213
Cdd:cd03213 153 LLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 4-213 3.50e-23

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: 100.20  E-value: 3.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     4 AVEFDNVSRLYGDVRAV--DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNL-PPW-ERDVN 79
Cdd:TIGR01846 455 AITFENIRFRYAPDSPEvlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMG 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    80 TVFQDYALFPHmSILDNVAY---GLMVKGVNKKQRHAMAQEALEKVALGFVHQ--RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALcnpGAPFEHVIHAAKLAGAHDFISELPQGYNTEvgEKGANLSGGQRQRIAIARALVGNPR 613

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400   155 VLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
17-226 5.14e-23

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 96.40  E-value: 5.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS--NLPPWERDVNTVFQD--YALFPHMS 92
Cdd:PRK15112  26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   93 ILDNVAYGLMVK-GVNKKQRHAMAQEALEKVALGFVHQRK-PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK15112 106 ISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400  171 EQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 5-214 6.36e-23

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: 93.53  E-value: 6.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYG--DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVF 82
Cdd:cd03247   1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALFPHMSILDNVAyglmvkgvnkkqrhamaqealekvalgfvhqrkpSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03247  81 NQRPYLFDTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPT 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129400 163 GALDlKLREQMQLELkKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIE 214
Cdd:cd03247 127 VGLD-PITERQLLSL-IFEVLKDKTLIWITH-HLTGIEHMDKILFLENGKII 175
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 4-193 7.27e-23

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 99.11  E-value: 7.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVS-RLYGDVRAVDGVSIAIKDGEffSML--GPSGSGKTTCLRLIAGFEQLSGGAISifgkpasnLPPWERdvnt 80
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGAR---- 427

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 vfqdyALF----PHM---SILDNVAYGLMVKGVNkkqrHAMAQEALEKVALG------FVHQRKPSQLSGGQRQRVAIAR 147
Cdd:COG4178 428 -----VLFlpqrPYLplgTLREALLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFAR 498

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16129400 148 ALVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSL-GITFIFVTH 193
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
cbiO PRK13644
energy-coupling factor transporter ATPase;
5-226 1.02e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 95.82  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGD-VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPA---SNLPPWERDVNT 80
Cdd:PRK13644   2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQD-YALFPHMSILDNVAYG---LMVKGVNKKQRHAMAqeaLEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK13644  82 VFQNpETQFVGRTVEEDLAFGpenLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENVLSDV 226
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 20-213 1.04e-22

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: 98.57  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGkpaSNLPPWERD-----VNTVFQDYALFPHmSIL 94
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQWDREtfgkhIGYLPQDVELFPG-TVA 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    95 DNVAyglmvkgvnKKQRHAMAQEALEKVALGFVH---QRKP-----------SQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:TIGR01842 410 ENIA---------RFGENADPEKIIEAAKLAGVHeliLRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDE 480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400   161 PLGALD----LKLREQMQlELKKlqqsLGITFIFVTHDQGeALSMSDRVAVFNNGRI 213
Cdd:TIGR01842 481 PNSNLDeegeQALANAIK-ALKA----RGITVVVITHRPS-LLGCVDKILVLQDGRI 531
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 1-213 2.80e-22

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 97.43  E-value: 2.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP---WERD 77
Cdd:PRK15439   8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDYALFPHMSILDNVAYGLmvkgvnkkQRHAMAQEALEKVALGFVHQRKPSQLSG----GQRQRVAIARALVNEP 153
Cdd:PRK15439  88 IYLVPQEPLLFPNLSVKENILFGL--------PKRQASMQKMKQLLAALGCQLDLDSSAGslevADRQIVEILRGLMRDS 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  154 RVLLLDEPLGALDLKLREQMQLELKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTI 218
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 6-197 3.01e-22

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 93.24  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNTVFQ 83
Cdd:PRK10247   9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYALFPHmSILDNVAYGLMVKGVN---KKQRHAMAQEALEKVALgfvhQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK10247  89 TPTLFGD-TVYDNLIFPWQIRNQQpdpAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 16129400  161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGE 197
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 23-215 3.39e-22

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 97.22  E-value: 3.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFeqLS-GGAISIFGKPASNLPP--WERDVNTVFQDYALFpHMSILDNVAY 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPesWRKHLSWVGQNPQLP-HGTLRDNVLL 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  100 G---LMVKGVNKKQRHAMAQEALEKVALGFVHQRK--PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQ 174
Cdd:PRK11174 446 GnpdASDEQLQQALENAWVSEFLPLLPQGLDTPIGdqAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 16129400  175 LELKklQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK11174 526 QALN--AASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 8-230 3.83e-22

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 94.81  E-value: 3.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDV----RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF----EQLSGGAISIFGKPASNLPPWER--- 76
Cdd:PRK11022   7 DKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnl 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   77 ---DVNTVFQDyalfpHMSILD---NVAYGLMV-----KGVNKKQRHAMAQEALEKVALGFVHQR---KPSQLSGGQRQR 142
Cdd:PRK11022  87 vgaEVAMIFQD-----PMTSLNpcyTVGFQIMEaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  143 VAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241


                 ....*...
gi 16129400  223 YMRPRTPF 230
Cdd:PRK11022 242 FRAPRHPY 249
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 5-219 6.73e-22

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: 96.02  E-value: 6.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG---FEQLSGGAI---------------SIFGK 66
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIIyhvalcekcgyverpSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    67 P----ASNLPPWERDV----NTVFQD------------YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF 126
Cdd:TIGR03269  81 PcpvcGGTLEPEEVDFwnlsDKLRRRirkriaimlqrtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   127 VHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVA 206
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250
                  ....*....|...
gi 16129400   207 VFNNGRIEQVDSP 219
Cdd:TIGR03269 241 WLENGEIKEEGTP 253
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-211 7.51e-22

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 96.01  E-value: 7.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP---WERD 77
Cdd:PRK09700   2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDYALFPHMSILDNVAYG-LMVK---GVN----KKQRhAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARAL 149
Cdd:PRK09700  82 IGIIYQELSVIDELTVLENLYIGrHLTKkvcGVNiidwREMR-VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 18-230 8.06e-22

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 95.93  E-value: 8.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKT----TCLRLI--------------AG----------FEQLSGGAIS-IFGKPA 68
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfHGesllhaseqtLRGVRGNKIAmIFQEPM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   69 SNLPPW---ERDVNTVfqdyaLFPHmsildnvayglmvKGVNKKQRHAMAQEALEKVALGFVHQR---KPSQLSGGQRQR 142
Cdd:PRK15134 103 VSLNPLhtlEKQLYEV-----LSLH-------------RGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  143 VAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244


                 ....*...
gi 16129400  223 YMRPRTPF 230
Cdd:PRK15134 245 FSAPTHPY 252
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 5-212 1.02e-21

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: 95.66  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG--GAISIFGKP--ASNLPPWERD-VN 79
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkASNIRDTERAgIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    80 TVFQDYALFPHMSILDNVAYG--LMVKG--VNKKQRHAMAQEALEKVALGFVHQRKP-SQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400   155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-205 1.33e-21

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 90.37  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKpasnlppweRDVNTVFQDYAL---FPh 90
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   91 MSILDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:NF040873  72 LTVRDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16129400  167 LKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRV 205
Cdd:NF040873 152 AESRERI-IALLAEEHARGATVVVVTHDLELVRRADPCV 189
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 4-215 1.60e-21

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: 95.27  E-value: 1.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   4 AVEFDNVSRLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP--WERDVNT 80
Cdd:COG5265 357 EVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQasLRAAIGI 436

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFpHMSILDNVAYGlmvkgvnkkqRHAMAQEALEKVA-----LGFVhQRKPSQ-----------LSGGQRQRVA 144
Cdd:COG5265 437 VPQDTVLF-NDTIAYNIAYG----------RPDASEEEVEAAAraaqiHDFI-ESLPDGydtrvgerglkLSGGEKQRVA 504

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 145 IARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRI-EQ 215
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH----RLSTivdADEILVLEAGRIvER 573
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 5-214 2.91e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 94.36  E-value: 2.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgKPASNlppwerdVNTVF-- 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGET-------VKIGYfd 384

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  83 QDYALF-PHMSILDNVAYGlmvkGVNKKQRHAMAQeaLEkvALGFV--HQRKP-SQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG0488 385 QHQEELdPDKTVLDELRDG----APGGTEQEVRGY--LG--RFLFSgdDAFKPvGVLSGGEKARLALAKLLLSPPNVLLL 456

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400 159 DEPLGALDLKLREQmqlelkkLQQSL----GiTFIFVTHDQgEAL-SMSDRVAVFNNGRIE 214
Cdd:COG0488 457 DEPTNHLDIETLEA-------LEEALddfpG-TVLLVSHDR-YFLdRVATRILEFEDGGVR 508
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
6-221 6.27e-21

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 93.31  E-value: 6.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    6 EFDNVSRLygDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK---PASNLPPWERDVNTVF 82
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAVKKGMAYIT 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   83 Q---DYALFPHMSILDNVA---------YGLMVKGVNKKQRHAMAQEALEKVAL--GFVHQrKPSQLSGGQRQRVAIARA 148
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALkcHSVNQ-NITELSGGNQQKVLISKW 423

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 8-166 3.26e-20

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 87.24  E-value: 3.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDyAL 87
Cdd:PRK13539   6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN-AM 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400   88 FPHMSILDNVAYGLMVKGvnkkQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK13539  85 KPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
14-234 3.37e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.53  E-value: 3.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS----NLPPWERDVNTVFQD--YAL 87
Cdd:PRK13638  11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQDpeQQI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   88 FpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKV-ALGFVHQrkPSQ-LSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK13638  91 F-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVdAQHFRHQ--PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  166 DLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGF 234
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-212 4.54e-20

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: 87.10  E-value: 4.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSR-----LYGDVR--AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAI---SIFGK-PAS 69
Cdd:COG4778   1 MTTLLEVENLSKtftlhLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGWvDLA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  70 NLPPWE------RDVNTVFQdyalF----PHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKvaLGfVHQR----KPSQL 135
Cdd:COG4778  81 QASPREilalrrRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLAR--LN-LPERlwdlPPATF 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 136 SGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE---QMQLELKklqqSLGITFIFVTHDQG--EALsmSDRVAVFNN 210
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvvELIEEAK----ARGTAIIGIFHDEEvrEAV--ADRVVDVTP 227


                ..
gi 16129400 211 GR 212
Cdd:COG4778 228 FS 229
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 5-219 2.67e-19

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: 84.85  E-value: 2.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTC----LRLIagfeQLSGGAISIFGKPASNLPP--WER 76
Cdd:cd03244   3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLhdLRS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  77 DVNTVFQDYALFPhmsildnvayGLMVKGVNKKQRH--AMAQEALEKVALGFVHQRKP-----------SQLSGGQRQRV 143
Cdd:cd03244  79 RISIIPQDPVLFS----------GTIRSNLDPFGEYsdEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 144 AIARALVNEPRVLLLDEPLGALDLKLREQMQlelKKLQQSL-GITFIFVTH------DqgealsmSDRVAVFNNGRIEQV 216
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAHrldtiiD-------SDRILVLDKGRVVEF 218


                ...
gi 16129400 217 DSP 219
Cdd:cd03244 219 DSP 221
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 19-219 3.70e-19

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 88.92  E-value: 3.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-ASNLPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     98 AYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLEL 177
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 16129400    178 KKLQQslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSP 219
Cdd:TIGR01257 1105 LKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 17-213 4.48e-19

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 87.77  E-value: 4.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER---DVNTVFQD---YALFPH 90
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIPEDrlgRGLVPD 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  91 MSILDNVAYGL-----MVKG--VNKKQRHAMAQEALEK--VALGFVHQRkPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG3845 351 MSVAENLILGRyrrppFSRGgfLDRKAIRAFAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVILARELSRDPKLLIAAQP 429

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129400 162 LGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG3845 430 TRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 5-215 5.97e-19

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


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 87.69  E-value: 5.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYGDVRA--VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwERDVN--- 79
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR-EVLANsva 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    80 TVFQDYALFpHMSILDNVAygLMVKGVNKKQRHAMAQEAlekvALGFVHQRKP-----------SQLSGGQRQRVAIARA 148
Cdd:TIGR03796 557 MVDQDIFLF-EGTVRDNLT--LWDPTIPDADLVRACKDA----AIHDVITSRPggydaelaeggANLSGGQRQRLEIARA 629

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400   149 LVNEPRVLLLDEPLGALDlklreqMQLElKKLQQSL---GITFIFVTHdqgeALSM---SDRVAVFNNGRIEQ 215
Cdd:TIGR03796 630 LVRNPSILILDEATSALD------PETE-KIIDDNLrrrGCTCIIVAH----RLSTirdCDEIIVLERGKVVQ 691
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
5-213 7.60e-19

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 87.38  E-value: 7.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLY--GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK-----PASNLppwERD 77
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASL---RNQ 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 VNTVFQDYALFpHMSILDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGF--VHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYARTEQysreQIEEAARMAYAMDFINKMDNGLdtVIGENGVLLSGGQRQRIAIARALLR 497

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgiTFIFVTHdqgeALSM---SDRVAVFNNGRI 213
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH----RLSTiekADEILVVEDGEI 556
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 15-166 9.01e-19

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: 82.79  E-value: 9.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP-WERDVNTVFQDYALFPHMSI 93
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400    94 LDNVAYGLMVKGvnKKQRhaMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:TIGR01189  91 LENLHFWAAIHG--GAQR--TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
15-207 1.12e-18

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 85.34  E-value: 1.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE----QLSGGAISIFGKPASNLPPWER------DVNTVFQD 84
Cdd:COG4170  18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQE 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 yalfPhMSILD---NVAYGLM-------VKGV---NKKQRHAMAQEALEKVAL---GFVHQRKPSQLSGGQRQRVAIARA 148
Cdd:COG4170  98 ----P-SSCLDpsaKIGDQLIeaipswtFKGKwwqRFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMA 172

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAV 207
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 16-166 2.01e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 82.16  E-value: 2.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  16 DVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-ASNLPPWERDVNTVFQDYALFPHMSI 93
Cdd:cd03231  11 DGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPlDFQRDSIARGLLYLGHAPGIKTTLSV 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  94 LDNVAYglmvkgvnKKQRHAMAQ--EALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:cd03231  91 LENLRF--------WHADHSDEQveEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 3-213 2.61e-18

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 85.65  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    3 YAVEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPpwERD--- 77
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--EAAlrq 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 -VNTVFQDYALFPHmSILDNVAYGLmvkgvNKKQRHAMAqEALEKVALGFVHQRKPS----------QLSGGQRQRVAIA 146
Cdd:PRK11160 415 aISVVSQRVHLFSA-TLRDNLLLAA-----PNASDEALI-EVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIA 487

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  147 RALVNEPRVLLLDEPLGALDlKLREQMQLELkKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLD-AETERQILEL-LAEHAQNKTVLMITH-RLTGLEQFDRICVMDNGQI 551
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-209 4.15e-18

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 82.47  E-value: 4.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgkpasnlppwERD--- 77
Cdd:PRK09544   1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNgkl 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 -VNTVFQDYALFPHMSIldNVAYGLMVKGVNKKqrhAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK09544  68 rIGYVPQKLYLDTTLPL--TVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129400  157 LLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFN 209
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
21-193 1.02e-17

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 80.23  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   21 DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPwerdvntVFQDYALF--------PHMS 92
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-------EYHQDLLYlghqpgikTELT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   93 ILDNVAYGLMVKGVnkkQRHAMAQEALEKVAL-GFVHQrkP-SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK13538  91 ALENLRFYQRLHGP---GDDEALWEALAQVGLaGFEDV--PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165

                        170       180
                 ....*....|....*....|....
gi 16129400  171 EQM-QLELKKLQQslGITFIFVTH 193
Cdd:PRK13538 166 ARLeALLAQHAEQ--GGMVILTTH 187
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 22-212 1.12e-17

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: 80.21  E-value: 1.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSG-----GAIS-----------------IFGKPASnlppwERDV 78
Cdd:cd03250  23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGsvsvpGSIAyvsqepwiqngtireniLFGKPFD-----EERY 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  79 NTVFQDYALFPHMSILDNvayGLMV----KGVNkkqrhamaqealekvalgfvhqrkpsqLSGGQRQRVAIARALVNEPR 154
Cdd:cd03250  98 EKVIKACALEPDLEILPD---GDLTeigeKGIN---------------------------LSGGQKQRISLARAVYSDAD 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 155 VLLLDEPLGALDLKLREQM--QLELKKLQqsLGITFIFVTHdQGEALSMSDRVAVFNNGR 212
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIfeNCILGLLL--NNKTRILVTH-QLQLLPHADQIVVLDNGR 204
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 5-193 1.26e-17

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: 79.12  E-value: 1.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSrLY---GDVRaVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgkpasnlpPWERDVntv 81
Cdd:cd03223   1 IELENLS-LAtpdGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDL--- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  82 fqdyaLF----PHM---SILDNVAYglmvkgvnkkqrhamaqeALEKValgfvhqrkpsqLSGGQRQRVAIARALVNEPR 154
Cdd:cd03223  67 -----LFlpqrPYLplgTLREQLIY------------------PWDDV------------LSGGEQQRLAFARLLLHKPK 111

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16129400 155 VLLLDEPLGALDlklrEQMQLELKKLQQSLGITFIFVTH 193
Cdd:cd03223 112 FVFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 5-195 1.53e-17

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: 77.87  E-value: 1.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgkpasnlppwerdvntvfqd 84
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  85 yalfphmsildnvayglmvkgvnkkqrhamaqEALEKVALGFVhqrkpSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03221  58 --------------------------------TWGSTVKIGYF-----EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                       170       180       190
                ....*....|....*....|....*....|.
gi 16129400 165 LDLKLREQMQLELKKLQQslgiTFIFVTHDQ 195
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDR 127
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 22-213 3.65e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 82.40  E-value: 3.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAgFEQLSG----GAISIFGKPAsNLPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:TIGR00955  43 NVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    98 AYGLMVK---GVNKKQRHAMAQEALEKVAL--------GFVHQRKpsQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:TIGR00955 121 MFQAHLRmprRVTKKEKRERVDEVLQALGLrkcantriGVPGRVK--GLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 16129400   167 LKLREQMQLELKKLQQSlGITFIFVTHD-QGEALSMSDRVAVFNNGRI 213
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRV 245
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
15-230 7.02e-17

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 80.23  E-value: 7.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF---------------------------EQLSGGAIS-IFGK 66
Cdd:PRK15093  18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrlsprerRKLVGHNVSmIFQE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   67 PASNLPPWERDVNTVFQdyalfphmSILDNVAYGLMVKGVNKKQRHAMaqEALEKValGFVHQRK-----PSQLSGGQRQ 141
Cdd:PRK15093  98 PQSCLDPSERVGRQLMQ--------NIPGWTYKGRWWQRFGWRKRRAI--ELLHRV--GIKDHKDamrsfPYELTEGECQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245


                 ....*....
gi 16129400  222 LYMRPRTPF 230
Cdd:PRK15093 246 LVTTPHHPY 254
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 20-213 7.44e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 81.20  E-value: 7.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVF---QDY---ALFPHMSI 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVyisEDRkrdGLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   94 LDNVAYGLMVKGVNK--KQRHAMAQEALEKVALGFvHQRKPSQ------LSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK10762 348 KENMSLTALRYFSRAggSLKHADEQQAVSDFIRLF-NIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16129400  166 DLKLREQM-QLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10762 427 DVGAKKEIyQL-INQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 19-327 1.05e-16

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 81.60  E-value: 1.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlppwerDVNTVFQDYALFPHMSILDNVA 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDAIDDLL 2027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     99 YG-------LMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:TIGR01257 2028 TGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    172 QMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLymrpRTPFVAGFVGTSNVF---DGLMAEk 248
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDGYIVTMKIKspkDDLLPD- 2181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    249 lcgmtgsfaLRP--EHIRLNTPGELQANGTIQAVQYQGAATR----FELKLNGGEKLLVsqanmtgEELPATLTPGQQVM 322
Cdd:TIGR01257 2182 ---------LNPveQFFQGNFPGSVQRERHYNMLQFQVSSSSlariFQLLISHKDSLLI-------EEYSVTQTTLDQVF 2245


                   ....*
gi 16129400    323 VSWSR 327
Cdd:TIGR01257 2246 VNFAK 2250
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 15-213 1.92e-16

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: 76.41  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGKPASNLPPWERDVNTV---FQDYALFP 89
Cdd:cd03217  11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIflaFQYPPEIP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  90 HMSILDnvayglMVKGVNKkqrhamaqealekvalGFvhqrkpsqlSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:cd03217  91 GVKNAD------FLRYVNE----------------GF---------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16129400 170 REQMQLELKKLqQSLGITFIFVTHDQGEALSM-SDRVAVFNNGRI 213
Cdd:cd03217 140 LRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 18-195 2.18e-16

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 76.92  E-value: 2.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGAISIFGKPASNlpPWERDVntvfqdyalfphmSILDNV 97
Cdd:COG2401  44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCVDVPDN--QFGREA-------------SLIDAI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  98 AyglmvKGVNKKQrhamAQEALEKVALG--FVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:COG2401 107 G-----RKGDFKD----AVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177

                       170       180
                ....*....|....*....|
gi 16129400 176 ELKKLQQSLGITFIFVTHDQ 195
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 5-213 2.34e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 79.63  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERDVNTV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvtAEQPEDYRKLFSAV 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   82 FQDYALFPHmsildnvayglMVKGVNKKQRHAMAQEALEKvaLGFVHQRKPS-------QLSGGQRQRVAIARALVNEPR 154
Cdd:PRK10522 403 FTDFHLFDQ-----------LLGPEGKPANPALVEKWLER--LKMAHKLELEdgrisnlKLSKGQKKRLALLLALAEERD 469

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQL 527
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
19-215 2.72e-16

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 79.76  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN--LPPWERDVNTVFQDYALFPHmSILDN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVANN 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   97 VAYGlmvkgvnkkqRHAMAQEALEKVA-LGFVHQ---RKPS-----------QLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10789 409 IALG----------RPDATQQEIEHVArLASVHDdilRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  162 LGALDLKLREQMqleLKKLQQ-SLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK10789 479 LSAVDGRTEHQI---LHNLRQwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQ 529
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
8-222 3.75e-16

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 76.95  E-value: 3.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVNTVFQDY 85
Cdd:PRK10253  11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   86 ALFPHMSILDNVAYG------LMVKGvnKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK10253  91 TTPGDITVQELVARGryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
23-228 7.79e-16

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 76.36  E-value: 7.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS--NLPPWERDVNTVFQDYALFPHMSILDNVAYG 100
Cdd:PRK10575  30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRELVAIG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  101 -------LMVKGVNKKQRhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:PRK10575 110 rypwhgaLGRFGAADREK---VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  174 QLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRPRT 228
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-MRGET 240
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
3-222 7.80e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 78.63  E-value: 7.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    3 YAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERdVNT 80
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdAGDIATRRR-VGY 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFPHMSILDNVAygLMVK--GVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:NF033858 344 MSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  159 DEPLGALDLKLREQMQLELKKLQQSLGITfIFV-THDQGEALSmSDRVAVFNNGRIEQVDSPRDL 222
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 14-205 7.95e-16

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 78.45  E-value: 7.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgkpASNL--------PPweRDVN-TVFqD 84
Cdd:PRK11147  13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY----EQDLivarlqqdPP--RNVEgTVY-D 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 Y----------ALFPHMSILDNVAYGLMVKGVNKKQRhamAQEALEK--------------VALGFVHQRKPSQLSGGQR 140
Cdd:PRK11147  86 FvaegieeqaeYLKRYHDISHLVETDPSEKNLNELAK---LQEQLDHhnlwqlenrinevlAQLGLDPDAALSSLSGGWL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  141 QRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgitfIFVTHDQGEALSMSDRV 205
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRI 223
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-203 8.16e-16

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 76.07  E-value: 8.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS-----NL---PPWERDVNTVF----QDYA 86
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqkNLvayVPQSEEVDWSFpvlvEDVV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   87 L---FPHMSILDnvayglmvkgVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK15056 102 MmgrYGHMGWLR----------RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 16129400  164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSD 203
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 17-211 1.53e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 77.35  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPP---WERDVNTVFQDYALFPHMSI 93
Cdd:PRK10762  17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIPQLTI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   94 LDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL-Dlk 168
Cdd:PRK10762  97 AENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD-- 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16129400  169 lREQMQL-----ELKklQQSLGITFIfvTHDQGEALSMSDRVAVFNNG 211
Cdd:PRK10762 175 -TETESLfrvirELK--SQGRGIVYI--SHRLKEIFEICDDVTVFRDG 217
PLN03211 PLN03211
ABC transporter G-25; Provisional
 20-212 1.62e-15

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 77.23  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGAISIFGKPASnlpPWERDVNTVFQDYALFPHMSILDN 96
Cdd:PLN03211  84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRET 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   97 VAYGLMV---KGVNKKQRHAMAQEALEKVALG-----FVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PLN03211 161 LVFCSLLrlpKSLTKQEKILVAESVISELGLTkcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16129400  169 LREQMQLELKKLQQSlGITFIFVTHD-QGEALSMSDRVAVFNNGR 212
Cdd:PLN03211 241 AAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 27-208 1.72e-15

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: 74.75  E-value: 1.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  27 IKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPW-ERDVNTVFQDYAlfphMSILDNVAYGLMVKg 105
Cdd:cd03237  22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRDLL----SSITKDFYTHPYFK- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 106 vnkkqrhamaQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLG 185
Cdd:cd03237  97 ----------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166

                       170       180
                ....*....|....*....|...
gi 16129400 186 ITFIFVTHDQGEALSMSDRVAVF 208
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVF 189
hmuV PRK13547
heme ABC transporter ATP-binding protein;
18-226 2.53e-15

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 74.86  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   18 RAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGA----------ISIFGKPASNLPPWE----RDVNTVFQ 83
Cdd:PRK13547  15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGaprgarvtgdVTLNGEPLAAIDAPRlarlRAVLPQAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYAlFPhMSILDNVAYG----LMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVN-------- 151
Cdd:PRK13547  93 QPA-FA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400  152 -EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRP 226
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV-LTP 245
GguA NF040905
sugar ABC transporter ATP-binding protein;
6-217 3.50e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 75.98  E-value: 3.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GAISIFGKPA--SNLPPWE 75
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKV------LSGvyphgsyeGEILFDGEVCrfKDIRDSE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   76 RD-VNTVFQDYALFPHMSILDNVAYG--LMVKGV-NKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVN 151
Cdd:NF040905  77 ALgIVIIHQELALIPYLSIAENIFLGneRAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400  152 EPRVLLLDEPLGALD----LKLREQMqLELKKlQqslGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVD 217
Cdd:NF040905 157 DVKLLILDEPTAALNeedsAALLDLL-LELKA-Q---GITSIIISHKLNEIRRVADSITVLRDGRtIETLD 222
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-226 4.37e-15

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 75.16  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTtclrliagfeqlSGGAISIFGKPASNLPPWeRDVNTVFQ 83
Cdd:NF000106  13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------------RGALPAHV*GPDAGRRPW-RF*TWCAN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYALFPHMSILDNVAYG----------LMVKG----VNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARAL 149
Cdd:NF000106  80 RRALRRTIG*HRPVR*GrresfsgrenLYMIGr*ldLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEA------LSMSDRVAVFNNGRIEQVDSP---R 220
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggR 238


                 ....*.
gi 16129400  221 DLYMRP 226
Cdd:NF000106 239 TLQIRP 244
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 5-166 1.03e-14

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 74.97  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfGKpasnlppwerdvnTVFQD 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE-------------TVKLA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    85 Y------ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEAlekvALGFV---HQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:TIGR03719 389 YvdqsrdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVG----RFNFKgsdQQKKVGQLSGGERNRVHLAKTLKSGGNV 464

                         170
                  ....*....|.
gi 16129400   156 LLLDEPLGALD 166
Cdd:TIGR03719 465 LLLDEPTNDLD 475
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 24-210 1.40e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 75.07  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFgkpasNLPPWERDVNTVFQDYALFpHMSILDNVAYG--- 100
Cdd:PTZ00265 1249 NVGMKNVNEFSLTKEGGSGEDSTVFKNSGKILLDGVDICDY-----NLKDLRNLFSIVSQEPMLF-NMSIYENIKFGked 1322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   101 LMVKGVNKKQRHAMAQEALEKVALGFVHQRKP--SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELK 178
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402

                         170       180       190
                  ....*....|....*....|....*....|..
gi 16129400   179 KLQQSLGITFIFVTHdQGEALSMSDRVAVFNN 210
Cdd:PTZ00265 1403 DIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
27-167 3.04e-14

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 70.65  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   27 IKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLppwERDVNTVFQDY--ALFPHMSILDNVAYGLMVK 104
Cdd:PRK13543  34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHlpGLKADLSTLENLHFLCGLH 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400  105 GVNKKQrhaMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK13543 111 GRRAKQ---MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 257-333 1.22e-13

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: 65.33  E-value: 1.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400   257 ALRPEHIRLNTPGElQANGTIQAVQYQGAATRFELKLNGGEKLLVSQANMTgeelPATLTPGQQVMVSWSRDVMVPL 333
Cdd:pfam08402   2 AIRPEKIRLAAAAN-GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAH----ARPPAPGDRVGLGWDPEDAHVL 73
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 17-214 1.47e-13

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 71.39  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGKPASNLPPW---ERDVNTVFQD---YALFP 89
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVP 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    90 HMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPS------QLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16129400   164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIE 214
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 17-213 1.72e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 71.11  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   17 VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGKPASNLPPWE---RDVNTVFQD---YALFP 89
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVP 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   90 HMSILDNV---AYGLMVKG--VNKKQRHAMAQEALEKVALGFVHQRKP-SQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK13549 355 VMGVGKNItlaALDRFTGGsrIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129400  164 ALDLKLReqmqLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13549 435 GIDVGAK----YEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
4-193 3.44e-13

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 70.13  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP--PWERDVNT 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAM 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   81 VFQDYALFPHmSILDNVAYGlmvkgvnKKQRHAMAQEALEKVAL--------GFVHQRKPSQ---LSGGQRQRVAIARAL 149
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLaelarslpDGLYTPLGEQgnnLSVGQKQLLALARVL 491

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTH 193
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-161 7.31e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 69.38  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNlppwERDVNTVFQ 83
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   84 DYA---------LFPHMSILDNVA-----YGLmvkgvNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARAL 149
Cdd:NF033858  77 RIAympqglgknLYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151

                        170
                 ....*....|..
gi 16129400  150 VNEPRVLLLDEP 161
Cdd:NF033858 152 IHDPDLLILDEP 163
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 9-212 7.74e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 68.99  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    9 NVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP---ASNLPPWERDVNTVFQDY 85
Cdd:PRK10982   3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   86 ALFPHMSILDNVAYGLM-VKG--VNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK10982  83 NLVLQRSVMDNMWLGRYpTKGmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16129400  163 GALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
11-213 8.58e-13

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 68.78  E-value: 8.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   11 SRLYGDVR-AVDG---------VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPAS----------- 69
Cdd:PRK11288 250 PRPLGEVRlRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairag 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   70 -NLPPWERDvntvfQDyALFPHMSILDNVA---------YGLMVkgvNKKQRHAMAQEALEKVAlgfVHQRKPSQ----L 135
Cdd:PRK11288 330 iMLCPEDRK-----AE-GIIPVHSVADNINisarrhhlrAGCLI---NNRWEAENADRFIRSLN---IKTPSREQlimnL 397

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  136 SGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 5-166 1.21e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 68.61  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfGKpasnlppwerdvnTVFQD 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-------------TVKLA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   85 Y------ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEAlekvALGFV---HQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11819 391 YvdqsrdALDPNKTVWEEISGGLDIIKVGNREIPSRAYVG----RFNFKggdQQKKVGVLSGGERNRLHLAKTLKQGGNV 466

                        170
                 ....*....|.
gi 16129400  156 LLLDEPLGALD 166
Cdd:PRK11819 467 LLLDEPTNDLD 477
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 5-219 2.99e-12

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: 64.74  E-value: 2.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGD--VRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP--PWERDVNT 80
Cdd:cd03369   7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  81 VFQDYALFPHmSILDNVayglmvkGVNKKQRHAMAQEALeKVALGfvhqrkPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03369  87 IPQDPTLFSG-TIRSNL-------DPFDEYSDEEIYGAL-RVSEG------GLNLSQGQRQLLCLARALLKRPRVLVLDE 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400 161 PLGALDLKLREQMQLELKKLQQslGITFIFVTHDQGEALSMsDRVAVFNNGRIEQVDSP 219
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 5-193 3.18e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 67.75  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLYG---DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI---FGKPASNLPPWERDV 78
Cdd:PTZ00265  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKWWRSKI 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    79 NTVFQDYALFPHmSILDNVAYGLM-VKGV----------------NKKQRHAMAQEALEKVAL--------GFVHQRK-- 131
Cdd:PTZ00265  463 GVVSQDPLLFSN-SIKNNIKYSLYsLKDLealsnyynedgndsqeNKNKRNSCRAKCAGDLNDmsnttdsnELIEMRKny 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   132 -----------------------------------PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE 176
Cdd:PTZ00265  542 qtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621

                         250
                  ....*....|....*..
gi 16129400   177 LKKLQQSLGITFIFVTH 193
Cdd:PTZ00265  622 INNLKGNENRITIIIAH 638
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 28-194 8.16e-12

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 64.31  E-value: 8.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  28 KDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGAISIFGKPASNlPPWERDVN----TVFQDY-----------ALFP-HM 91
Cdd:cd03236  24 REGQVLGLVGPNGIGKSTALKI------LAGKLKPNLGKFDDP-PDWDEILDefrgSELQNYftkllegdvkvIVKPqYV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:cd03236  97 DLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176

                       170       180
                ....*....|....*....|...
gi 16129400 172 QMQLELKKLQQSlGITFIFVTHD 194
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHD 198
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 20-213 9.28e-12

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 64.09  E-value: 9.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQlSGGAISIFGKPASNLPPWE--------------RDVNTVFQDY 85
Cdd:COG4138  12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhraylsqqqspPFAMPVFQYL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  86 ALfpHMSildnvayglmVKGVNKKQRHAMAQEAlEKVALGFVHQRKPSQLSGGQRQRVAIARAL------VN-EPRVLLL 158
Cdd:COG4138  91 AL--HQP----------AGASSEAVEQLLAQLA-EALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400 159 DEPLGALDLklreQMQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4138 158 DEPMNSLDV----AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 16-193 9.53e-12

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: 63.50  E-value: 9.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  16 DVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGK-PASNLPPWERDVNTVFQDYA----LFPH 90
Cdd:cd03290  13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAaqkpWLLN 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  91 MSILDNVAYGlmvkGVNKKQRHAMAQEALEKVA----LGFVHQRKPSQ----LSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03290  93 ATVEENITFG----SPFNKQRYKAVTDACSLQPdidlLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168

                       170       180       190
                ....*....|....*....|....*....|..
gi 16129400 163 GALDLKLREQ-MQLELKKLQQSLGITFIFVTH 193
Cdd:cd03290 169 SALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 23-213 1.68e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 65.07  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWER-DVNTVF-----QDYALFPHMSILDN 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   97 VaYGLMVKGVNKKQRHAMAQEALEKV--ALG--FVHQRKPSQ-LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:PRK15439 362 V-CALTHNRRGFWIKPARENAVLERYrrALNikFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16129400  172 QMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
12-194 3.41e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 64.06  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   12 RLYGdvravdgvSIAIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGAISIFGKPASNlPPWERDVN----TVFQDYal 87
Cdd:PRK13409  89 KLYG--------LPIPKEGKVTGILGPNGIGKTTAVKI------LSGELIPNLGDYEEE-PSWDEVLKrfrgTELQNY-- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   88 fphmsiLDNVAYGLM---------------VKG-----VNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIAR 147
Cdd:PRK13409 152 ------FKKLYNGEIkvvhkpqyvdlipkvFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAA 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16129400  148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHD 194
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 26-194 3.87e-11

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 64.04  E-value: 3.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  26 AIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGAISIFGKPaSNLPPWErDVNTVFQDYALFPHMSILDN----VAY-- 99
Cdd:COG1245  95 VPKKGKVTGILGPNGIGKSTALKI------LSGELKPNLGDY-DEEPSWD-EVLKRFRGTELQDYFKKLANgeikVAHkp 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 100 ------GLMVKGV-----NKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:COG1245 167 qyvdliPKVFKGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246

                       170       180
                ....*....|....*....|....*....
gi 16129400 169 LReqmqLELKKLQQSL---GITFIFVTHD 194
Cdd:COG1245 247 QR----LNVARLIRELaeeGKYVLVVEHD 271
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 14-203 4.58e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 61.50  E-value: 4.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   14 YGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP-ASNLPPWERDVNTVFQDYALFPHMS 92
Cdd:PRK13540  11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSiKKDLCTYQKQLCFVGHRSGINPYLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   93 ILDNVAYGLMVKGVNKKqrhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK13540  91 LRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 16129400  173 MQLELKKLQQSLGItfIFVTHDQGEALSMSD 203
Cdd:PRK13540 166 IITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 5-208 6.08e-11

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 63.26  E-value: 6.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   5 VEFDNVSRLYGDVR-AVDGVSIaiKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIS----IFGKPASNLPPWERDVn 79
Cdd:COG1245 342 VEYPDLTKSYGGFSlEVEGGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISYKPQYISPDYDGTV- 418

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  80 tvfqdyalfphMSILDNVAYGLMvkGVNKKQrhamaQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1245 419 -----------EEFLRSANTDDF--GSSYYK-----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129400 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDqgeaLSM----SDRVAVF 208
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVF 529
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 6-194 7.48e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 63.05  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    6 EFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKpasnlppweRDVnTVFQDY 85
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK---------LEV-AYFDQH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   86 --ALFPHMSILDNVAYGLMVKGVNKKQRHAMA--QEAL--EKVAlgfvhqRKPSQ-LSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK11147 391 raELDPEKTVMDNLAEGKQEVMVNGRPRHVLGylQDFLfhPKRA------MTPVKaLSGGERNRLLLARLFLKPSNLLIL 464

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 16129400  159 DEPLGALDLklrEQMQLeLKKLQQSLGITFIFVTHD 194
Cdd:PRK11147 465 DEPTNDLDV---ETLEL-LEELLDSYQGTVLLVSHD 496
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 21-213 1.09e-10

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 60.85  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  21 DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGKPASNLPPWER---DVNTVFQDYALFPHMSILD 95
Cdd:COG0396  17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  96 --NVAYG----------LMVKGVNKKQRH-AMAQEALEK-VALGFvhqrkpsqlSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG0396  97 flRTALNarrgeelsarEFLKLLKEKMKElGLDEDFLDRyVNEGF---------SGGEKKRNEILQMLLLEPKLAILDET 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400 162 LGALDL-----------KLREQmqlelkklqqslGITFIFVTHdQGEALSM--SDRVAVFNNGRI 213
Cdd:COG0396 168 DSGLDIdalrivaegvnKLRSP------------DRGILIITH-YQRILDYikPDFVHVLVDGRI 219
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 15-250 1.74e-10

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: 62.27  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLR-LIAGFEQLSG-----GAIS-----------------IFGKPASnl 71
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGhvhmkGSVAyvpqqawiqndslreniLFGKALN-- 726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     72 PPWERdvnTVFQDYALFPHMSIL---DNVAYGlmVKGVNkkqrhamaqealekvalgfvhqrkpsqLSGGQRQRVAIARA 148
Cdd:TIGR00957  727 EKYYQ---QVLEACALLPDLEILpsgDRTEIG--EKGVN---------------------------LSGGQKQRVSLARA 774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    149 LVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSLGI----TFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLYM 224
Cdd:TIGR00957  775 VYSNADIYLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850

                          250       260
                   ....*....|....*....|....*.
gi 16129400    225 RprtpfvagfvgtsnvfDGLMAEKLC 250
Cdd:TIGR00957  851 R----------------DGAFAEFLR 860
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 23-228 1.95e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 60.33  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFeqLSG-GAISIFGKPASNLPPWE---------RDVNT-----VFQDYAL 87
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQPLEAWSAAElarhraylsQQQTPpfampVFQYLTL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   88 FphmsildnvayglmvkgvnkkqRHAMAQEALEKVALGFVHQ---------RKPSQLSGGQRQRVAIA-------RALVN 151
Cdd:PRK03695  93 H----------------------QPDKTRTEAVASALNEVAEalglddklgRSVNQLSGGEWQRVRLAavvlqvwPDINP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNGRIeQVDSPRDLYMRPRT 228
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKL-LASGRRDEVLTPEN 225
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 27-208 2.04e-10

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: 59.12  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  27 IKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifgkpasnlppWERDvntvfqdyalfphmsildNVAYglmvkgv 106
Cdd:cd03222  22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-----------WDGI------------------TPVY------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 107 nkkqrhamaqealekvalgfvhqrKPS--QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSL 184
Cdd:cd03222  66 ------------------------KPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121

                       170       180
                ....*....|....*....|....
gi 16129400 185 GITFIFVTHDQGEALSMSDRVAVF 208
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVF 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 30-204 2.35e-10

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: 58.15  E-value: 2.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFqdyalfphmsildnvayglmvkgvnkk 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    110 qrhamaqealekvalgfvhQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE-----LKKLQQSL 184
Cdd:smart00382  55 -------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115

                          170       180
                   ....*....|....*....|
gi 16129400    185 GITFIFVTHDQGEALSMSDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 5-198 4.47e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 60.41  E-value: 4.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGKP-ASNLPPWE--RDV-- 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLFGRRrGSGETIWDikKHIgy 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   79 --NTVFQDYALfpHMSILDNVAYGL-----MVKGVNKKQRHaMAQEALEKVALGFVHQRKPSQ-LSGGQRQRVAIARALV 150
Cdd:PRK10938 341 vsSSLHLDYRV--STSVRNVILSGFfdsigIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALV 417

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16129400  151 NEPRVLLLDEPLGALDLKLReqmQLELKKLQQSLG---ITFIFVTHDQGEA 198
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNR---QLVRRFVDVLISegeTQLLFVSHHAEDA 465
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 40-222 4.74e-10

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: 60.58  E-value: 4.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  40 GSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLpPWERD-VNTVFQDYALFPHmsildnvaygLMvkGVNKKQRHAMAQ 116
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPvtADNR-EAYRQlFSAVFSDFHLFDR----------LL--GLDGEADPARAR 434

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 117 EALEKVALgfvhQRKPS---------QLSGGQRQRVAIARALVnEPR-VLLLDE------PLgaldlkLR----EQMQLE 176
Cdd:COG4615 435 ELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALL-EDRpILVFDEwaadqdPE------FRrvfyTELLPE 503

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16129400 177 LKKlqqsLGITFIFVTHDQ---GEAlsmsDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG4615 504 LKA----RGKTVIAISHDDryfDLA----DRVLKMDYGKLVELTGPAAL 544
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
5-208 5.31e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 60.59  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    5 VEFDNVSRLYGDVR-AVDGVSIaiKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIS----IFGKPASNLPpwerDVN 79
Cdd:PRK13409 341 VEYPDLTKKLGDFSlEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkISYKPQYIKP----DYD 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   80 TVFQDYaLFPHMSILDNVAYglmvkgvnkkqrhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13409 415 GTVEDL-LRSITDDLGSSYY---------------KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129400  160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDqgeaLSM----SDRVAVF 208
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMVF 527
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 5-193 7.18e-10

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: 60.15  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     5 VEFDNVSRLY--GDVrAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifgKPASN----LPPWERDV 78
Cdd:TIGR00954 452 IKFENIPLVTpnGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT---KPAKGklfyVPQRPYMT 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    79 NTVFQDYALFPhMSILDnvaygLMVKGVNKKQRHAMaqeaLEKVALGFVHQRKPS---------QLSGGQRQRVAIARAL 149
Cdd:TIGR00954 528 LGTLRDQIIYP-DSSED-----MKRRGLSDKDLEQI----LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLF 597

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 16129400   150 VNEPRVLLLDEPLGALDLKLREQMQlelkKLQQSLGITFIFVTH 193
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMY----RLCREFGITLFSVSH 637
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 3-194 7.29e-10

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: 59.95  E-value: 7.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     3 YAVEFDNVSRLYGDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ-LSGGAISIFGKPASNLPpwerdvnt 80
Cdd:TIGR03719   3 YIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKdFNGEARPQPGIKVGYLP-------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    81 vfQDYALFPHMSILDNVAYGL--MVKGVNKKQRHAMA--------------QEAL-EKVALGFVHQ------------RK 131
Cdd:TIGR03719  75 --QEPQLDPTKTVRENVEEGVaeIKDALDRFNEISAKyaepdadfdklaaeQAELqEIIDAADAWDldsqleiamdalRC 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   132 P------SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDlklREQMQ-LElKKLQQSLGiTFIFVTHD 194
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAwLE-RHLQEYPG-TVVAVTHD 217
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 23-213 9.31e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 59.74  E-value: 9.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERdVNTVF-------QDYALFPHMSI-- 93
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFalvteerRSTGIYAYLDIgf 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   94 ---LDNV-----AYGLMVKGVNKKQRHAMAQEALEKVAlgfVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK10982 346 nslISNIrnyknKVGLLDNSRMKSDTQWVIDSMRVKTP---GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16129400  166 DLKLR-EQMQLELKKLQQSLGItfIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10982 423 DVGAKfEIYQLIAELAKKDKGI--IIISSEMPELLGITDRILVMSNGLV 469
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-205 1.69e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 58.75  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    4 AVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgKPA--SNLPPWERDVNTV 81
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSenANIGYYAQDHAYD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   82 F-QDYALFPHMSILDNVAYG-LMVKGVnkKQRHAMAQEALEKvalgfvhqrKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK15064 395 FeNDLTLFDWMSQWRQEGDDeQAVRGT--LGRLLFSQDDIKK---------SVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16129400  160 EPLGALDLKLREQMQLELKKLQQSLgitfIFVTHDQGEALSMSDRV 205
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKYEGTL----IFVSHDREFVSSLATRI 505
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-215 2.05e-09

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 57.52  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   19 AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGkpasnlppwerDVNTVFQDYALFPHMSILDNVA 98
Cdd:PRK13546  39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   99 YGLMVKGVNKKQRHAMAQEALEKVALG-FVHQrKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLreqMQLEL 177
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGeFIYQ-PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF---AQKCL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 16129400  178 KKLQQ--SLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK13546 184 DKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 23-211 3.13e-09

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: 57.17  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKpasnlppwerdVNTVFQDYALFPHmSILDNVAYGLM 102
Cdd:cd03291  56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGVS 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 103 VKGVNKKQRHAMAQeaLEKVALGFVHQRKPS------QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM-QL 175
Cdd:cd03291 124 YDEYRYKSVVKACQ--LEEDITKFPEKDNTVlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfES 201

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 16129400 176 ELKKLQQSLgiTFIFVThDQGEALSMSDRVAVFNNG 211
Cdd:cd03291 202 CVCKLMANK--TRILVT-SKMEHLKKADKILILHEG 234
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 15-213 3.57e-09

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 56.57  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   15 GDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGKPASNLPPWERdvntvfqdyalfPHMS 92
Cdd:CHL00131  18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER------------AHLG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   93 ILDNVAYGLMVKGV----------NKKQRHAMAQEA------------LEKVALG--FVHQRKPSQLSGGQRQRVAIARA 148
Cdd:CHL00131  86 IFLAFQYPIEIPGVsnadflrlayNSKRKFQGLPELdplefleiinekLKLVGMDpsFLSRNVNEGFSGGEKKRNEILQM 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129400  149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQgEALS--MSDRVAVFNNGRI 213
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQ-RLLDyiKPDYVHVMQNGKI 230
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 7-211 4.21e-09

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: 58.00  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400      7 FDNVSRLYGDVraVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPA-SNLPPWerdvntvfqdy 85
Cdd:TIGR01271  431 FSNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISfSPQTSW----------- 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     86 aLFPHmSILDNVAYGL---------MVKGVNKKQRHAMAQEAlEKVALGfvhqRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:TIGR01271  498 -IMPG-TIKDNIIFGLsydeyrytsVIKACQLEEDIALFPEK-DKTVLG----EGGITLSGGQRARISLARAVYKDADLY 570

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400    157 LLDEPLGALD-LKLREQMQLELKKLQQSLgiTFIFVThDQGEALSMSDRVAVFNNG 211
Cdd:TIGR01271  571 LLDSPFTHLDvVTEKEIFESCLCKLMSNK--TRILVT-SKLEHLKKADKILLLHEG 623
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 1-166 5.98e-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: 54.94  E-value: 5.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   1 MTYAVEFDNVSRlygdvRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLS--GGAISIFGKPasNLPPWERDV 78
Cdd:cd03232   9 LNYTVPVKGGKR-----QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRP--LDKNFQRST 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  79 NTVFQDYALFPHMSIldnvayglmvkgvnkkqrhamaQEALEKVAL--GfvhqrkpsqLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03232  82 GYVEQQDVHSPNLTV----------------------REALRFSALlrG---------LSVEQRKRLTIGVELAAKPSIL 130

                       170
                ....*....|
gi 16129400 157 LLDEPLGALD 166
Cdd:cd03232 131 FLDEPTSGLD 140
PLN03232 PLN03232
ABC transporter C family member; Provisional
 22-230 6.56e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 57.29  E-value: 6.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASN--LPPWERDVNTVFQDYALFPhmsildnvay 99
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFS---------- 1323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   100 GLMVKGVNKKQRHAMAQ--EALEKVALGFVHQRKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400   167 LKLREQMQLELKKLQQSlgITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
PTZ00243 PTZ00243
ABC transporter; Provisional
 23-236 9.53e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 57.10  E-value: 9.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    23 VSIAIKDGEFFSMLGPSGSGKTTCLR-LIAGFEQLSG---GAISIFGKPASnlpPWerDVNTVFQDYALFphmsiLDNVA 98
Cdd:PTZ00243  679 VSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEISEGrvwAERSIAYVPQQ---AW--IMNATVRGNILF-----FDEED 748

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    99 YGLMVKGVNKKQRHA-MAQEA--LEkVALGfvhqRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:PTZ00243  749 AARLADAVRVSQLEAdLAQLGggLE-TEIG----EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400   176 ELkKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDlYMrpRTPFVAGFVG 236
Cdd:PTZ00243  824 EC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD-FM--RTSLYATLAA 879
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 20-213 9.72e-09

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 54.58  E-value: 9.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  20 VDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeqLSGGAISIFGK-------PASNLPPWERDVNTVFQDYALFPHMS 92
Cdd:cd03233  23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDihyngipYKEFAEKYPGEIIYVSEEDVHFPTLT 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  93 ILDNVAYGLMVKGvnkkqrHAMAqealekvalgfvhqRKpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:cd03233 100 VRETLDFALRCKG------NEFV--------------RG---ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16129400 173 MQLELKKLQQSLGITfIFVTHDQ--GEALSMSDRVAVFNNGRI 213
Cdd:cd03233 157 ILKCIRTMADVLKTT-TFVSLYQasDEIYDLFDKVLVLYEGRQ 198
PLN03073 PLN03073
ABC transporter F family; Provisional
 34-213 4.24e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.48  E-value: 4.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   34 SMLGPSGSGKTTCLRLIAGFEQLSGGaiSIFGKPASNLppwerdvnTVFQDYalfpHMSILDNVAYGL--MVK---GV-- 106
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSG--TVFRSAKVRM--------AVFSQH----HVDGLDLSSNPLlyMMRcfpGVpe 604

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  107 NKKQRHAMAQEALEKVALGFVHQrkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgi 186
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGV-- 677

                        170       180
                 ....*....|....*....|....*..
gi 16129400  187 tfIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PLN03073 678 --LMVSHDEHLISGSVDELWVVSEGKV 702
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 17-166 7.29e-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: 7.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     17 VRAVDGVsiaIKDGEFFSMLGPSGSGKTTCLRLIA----GFEQLSGGAISIFGKPASNLPPWER-DVNTVFQDYALFPHM 91
Cdd:TIGR00956   77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVA------LGFVHQRKPS-------QLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:TIGR00956  154 TVGETLDFAARCKTPQNRPDGVSREEYAKHIAdvymatYGLSHTRNTKvgndfvrGVSGGERKRVSIAEASLGGAKIQCW 233


                   ....*...
gi 16129400    159 DEPLGALD 166
Cdd:TIGR00956  234 DNATRGLD 241
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 1-193 1.45e-07

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 52.97  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    1 MTYAVEFDNVSRLY-------------------GDVR-AVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGA 60
Cdd:PRK13545   1 MNYKVKFEHVTKKYkmynkpfdklkdlffrskdGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   61 ISIFGKPAsnlppwerdvnTVFQDYALFPHMSILDNVAY-GLMVkGVNKKQRHAMAQEALEKVALG-FVHQrkPSQ-LSG 137
Cdd:PRK13545  81 VDIKGSAA-----------LIAISSGLNGQLTGIENIELkGLMM-GLTKEKIKEIIPEIIEFADIGkFIYQ--PVKtYSS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400  138 GQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTH 193
Cdd:PRK13545 147 GMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISH 201
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 24-210 1.54e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 52.71  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGKPAsNLP----------PWERDvNTVF-----QDYAL 87
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQFSHIT-RLSfeqlqklvsdEWQRN-NTDMlspgeDDTGR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   88 FPHMSILDnvayglmvkGVNKKQRhamAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK10938 101 TTAEIIQD---------EVKDPAR---CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16129400  168 KLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNN 210
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 135-222 1.69e-07

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: 53.03  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    135 LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKklQQSLGITFIFVTHDQGEALSMSdRVAVFNNGRIE 214
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498


                   ....*...
gi 16129400    215 QVDSPRDL 222
Cdd:TIGR00957 1499 EFGAPSNL 1506
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 9-194 2.17e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 52.43  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    9 NVSRLYGDVRAV-DGVSIAikdgeFF-----SMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgKPASN-----LPpwerd 77
Cdd:PRK11819  11 RVSKVVPPKKQIlKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGEA----RPAPGikvgyLP----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   78 vntvfQDYALFPHMSILDNVAYGLMVKgVNKKQRH-----AMA----------------QEALEKV-------------- 122
Cdd:PRK11819  77 -----QEPQLDPEKTVRENVEEGVAEV-KAALDRFneiyaAYAepdadfdalaaeqgelQEIIDAAdawdldsqleiamd 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400  123 ALgfvhqRKP------SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDlklREQMQ-LElKKLQQSLGiTFIFVTHD 194
Cdd:PRK11819 151 AL-----RCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAwLE-QFLHDYPG-TVVAVTHD 219
PLN03073 PLN03073
ABC transporter F family; Provisional
 130-193 2.40e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 52.17  E-value: 2.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129400  130 RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslgiTFIFVTH 193
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
PTZ00243 PTZ00243
ABC transporter; Provisional
 22-230 2.68e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.47  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKP--ASNLPPWERDVNTVFQDYALFPHmSILDNVAY 99
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYGLRELRRQFSMIPQDPVLFDG-TVRQNVDP 1406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   100 GL---------MVKGVNKKQRHAMAQEALEKVALgfvhqRKPSQLSGGQRQRVAIARALVNEPR-VLLLDEPLGALDLKL 169
Cdd:PTZ00243 1407 FLeassaevwaALELVGLRERVASESEGIDSRVL-----EGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPAL 1481

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400   170 REQMQLELkkLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PTZ00243 1482 DRQIQATV--MSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 22-213 3.91e-07

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 50.56  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGKPASNLPPWERDVNTVFQdyaLFPHMSILDNVAY 99
Cdd:PRK09580  19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFM---AFQYPVEIPGVSN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  100 GLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQL---------------SGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK09580  96 QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129400  165 LD---LKLREQMQLELKKLQQSlgitFIFVTHDQgEALSM--SDRVAVFNNGRI 213
Cdd:PRK09580 176 LDidaLKIVADGVNSLRDGKRS----FIIVTHYQ-RILDYikPDYVHVLYQGRI 224
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 8-205 4.00e-07

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 49.24  E-value: 4.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   8 DNVSRLYgdVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLrliagfeqLSGGAISIFGKPASNLPPWERDvNTVFQDyal 87
Cdd:cd03238   1 LTVSGAN--VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--------NEGLYASGKARLISFLPKFSRN-KLIFID--- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  88 fphmsildnvayglmvkgvnkkQRHAMAQEALEKVALGfvhqRKPSQLSGGQRQRVAIARALVNEPR--VLLLDEPLGAL 165
Cdd:cd03238  67 ----------------------QLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 16129400 166 DLKLREQMQLELKKLQQsLGITFIFVTHDQgEALSMSDRV 205
Cdd:cd03238 121 HQQDINQLLEVIKGLID-LGNTVILIEHNL-DVLSSADWI 158
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 20-222 8.69e-07

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: 49.47  E-value: 8.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  20 VDGVSIAIKDGEFFSMLGPSGSGKTTclrLIAGFEQL--SGGAISIFGKPASNLP--PWERDVNTVFQDYALFPhmsild 95
Cdd:cd03289  20 LENISFSISPGQRVGLLGRTGSGKST---LLSAFLRLlnTEGDIQIDGVSWNSVPlqKWRKAFGVIPQKVFIFS------ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  96 nvayGLMVKGVNKKQRHAMAQ--EALEKVALGFVHQRKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03289  91 ----GTFRKNLDPYGKWSDEEiwKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 163 GALDlklREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03289 167 AHLD---PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
PLN03130 PLN03130
ABC transporter C family member; Provisional
 23-215 1.53e-06

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 50.12  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGKPAsnlppWERDVNTVFqdyalfpHMSILDNVAYGL 101
Cdd:PLN03130  636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVA-----YVPQVSWIF-------NATVRDNILFGS 703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   102 MVKGV--NKKQRHAMAQEALEKVALGFVHQ--RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ----- 172
Cdd:PLN03130  704 PFDPEryERAIDVTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQvfdkc 783

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 16129400   173 MQLELKklqqslGITFIFVThDQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PLN03130  784 IKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKE 819
PLN03232 PLN03232
ABC transporter C family member; Provisional
 135-215 5.10e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 48.43  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   135 LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ-----MQLELKklqqslGITFIFVThDQGEALSMSDRVAVFN 209
Cdd:PLN03232  741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVS 813


                  ....*.
gi 16129400   210 NGRIEQ 215
Cdd:PLN03232  814 EGMIKE 819
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 18-222 5.83e-06

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: 47.98  E-value: 5.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     18 RAV-DGVSIAIKDGEFFSMLGPSGSGKTTclrLIAGFEQL--SGGAISIFGKP--ASNLPPWERDVNTVFQDYALFPhms 92
Cdd:TIGR01271 1232 RAVlQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRLlsTEGEIQIDGVSwnSVTLQTWRKAFGVIPQKVFIFS--- 1305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     93 ildnvayGLMVKGVNKKQRHAMAQ--EALEKVALGFVHQRKPSQ-----------LSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:TIGR01271 1306 -------GTFRKNLDPYEQWSDEEiwKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLD 1378

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400    160 EPLGALDlklREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR01271 1379 EPSAHLD---PVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 23-237 6.89e-06

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: 46.83  E-value: 6.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  23 VSIAIKDGEFFSMLGPSGSGKTTC----LRLIAGFEqlsgGAISIFGKPASNLP--PWERDVNTVFQDYALFPHmSILDN 96
Cdd:cd03288  40 VKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFSG-SIRFN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  97 VayglmvkGVNKKQRHAMAQEALEKVALGFVHQRKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd03288 115 L-------DPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASI 187

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129400 166 DLKLREQMQlelKKLQQSLG-ITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLYMRPRTPFvAGFVGT 237
Cdd:cd03288 188 DMATENILQ---KVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF-ASLVRT 255
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 8-225 1.20e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 47.09  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    8 DNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI-----FGKPASNLPPWERDVNTVF 82
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYFAQHQLEFLRADESPL 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   83 QdyalfpHMSILDNVAYglmvkgvnkkqrhamaQEALEKVALGFVHQ-----RKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK10636 396 Q------HLARLAPQEL----------------EQKLRDYLGGFGFQgdkvtEETRRFSGGEKARLVLALIVWQRPNLLL 453

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129400  158 LDEPLGALDLKLREQMQLELKKLQQSLgitfIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMR 225
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
PLN03130 PLN03130
ABC transporter C family member; Provisional
 4-239 1.34e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 47.04  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400     4 AVEFDNVSRLY-GDVRAV-DGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWE--RDVN 79
Cdd:PLN03130 1237 SIKFEDVVLRYrPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLG 1316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    80 TVFQDYALFPhmsildnvayGLMVKGVNKKQRHAMAQ--EALEKVALGFVHQRKPSQL-----------SGGQRQRVAIA 146
Cdd:PLN03130 1317 IIPQAPVLFS----------GTVRFNLDPFNEHNDADlwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLA 1386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463

                         250
                  ....*....|....*.
gi 16129400   227 RTPFvAGFV---GTSN 239
Cdd:PLN03130 1464 GSAF-SKMVqstGAAN 1478
PLN03140 PLN03140
ABC transporter G family member; Provisional
 22-166 2.04e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 46.38  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400    22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfEQLSG---GAISIFGKPaSNLPPWERDVNTVFQDYALFPHMSILDNVA 98
Cdd:PLN03140  898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVRESLI 975

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129400    99 YGLMV---KGVNKKQRHAMAQEALEKVAL-----GFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PLN03140  976 YSAFLrlpKEVSKEEKMMFVDEVMELVELdnlkdAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 31-194 2.97e-05

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: 44.14  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  31 EFFSML----GPSGSGKTT---CLRLiagfeqlsggaiSIFG-KPASNlppwerdvntvfQDYALFPHM-SILDNVAY-G 100
Cdd:cd03240  19 EFFSPLtlivGQNGAGKTTiieALKY------------ALTGeLPPNS------------KGGAHDPKLiREGEVRAQvK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400 101 LMVKGVNKKQRHAM-AQEALEKVAlgFVHQ--------RKPSQLSGGQRQ------RVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd03240  75 LAFENANGKKYTITrSLAILENVI--FCHQgesnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNL 152

                       170       180       190
                ....*....|....*....|....*....|
gi 16129400 166 DLKLREQMQLELKKLQQSLGI-TFIFVTHD 194
Cdd:cd03240 153 DEENIEESLAEIIEERKSQKNfQLIVITHD 182
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 92-195 3.06e-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: 43.50  E-value: 3.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  92 SILDNVAYGL---MVKGVNKKQRHAMAQEALEKVAL-GFVHQrkpsqLSGGQRQRVAIARALVNE---PRVL-LLDEPLG 163
Cdd:cd03227  36 TILDAIGLALggaQSATRRRSGVKAGCIVAAVSAELiFTRLQ-----LSGGEKELSALALILALAslkPRPLyILDEIDR 110

                        90       100       110
                ....*....|....*....|....*....|....
gi 16129400 164 ALDlkLREQMQLE--LKKLQQSlGITFIFVTHDQ 195
Cdd:cd03227 111 GLD--PRDGQALAeaILEHLVK-GAQVIVITHLP 141
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-205 1.54e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  120 EKVALGFVHQ---RKPSQLSGGQRQ------RVAIARALVNEPRVLLLDEPLGALD----LKLREQMQLELKKLQQslgi 186
Cdd:PRK03918 771 NKVKLFVVYQgkeRPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQ---- 846

                         90
                 ....*....|....*....
gi 16129400  187 tFIFVTHDQgEALSMSDRV 205
Cdd:PRK03918 847 -VIIVSHDE-ELKDAADYV 863
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 26-57 1.56e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 43.15  E-value: 1.56e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 16129400   26 AIKDGEFFSML--GPSGSGKTTCLRLIAG-----FEQLS 57
Cdd:PRK13342  30 MIEAGRLSSMIlwGPPGTGKTTLARIIAGatdapFEALS 68
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 124-195 1.90e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 43.23  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129400  124 LGFVH---QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLklreQMQLELKKLQQSLGITFIFVTHDQ 195
Cdd:PRK10636 136 LGFSNeqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILISHDR 206
GguA NF040905
sugar ABC transporter ATP-binding protein;
135-213 2.02e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.85  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  135 LSGGQRQRVAIARALVNEPRVLLLDEP-----LGAldlklreqmQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVA 206
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIY 475


                 ....*..
gi 16129400  207 VFNNGRI 213
Cdd:NF040905 476 VMNEGRI 482
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 23-194 2.86e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 42.57  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifgkpasnLPPWERdVNTVFQDYALFPHMSILDNVAYGLM 102
Cdd:PRK15064  20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS--------LDPNER-LGKLRQDQFAFEEFTVLDTVIMGHT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400  103 VKGVNKKQRHA------MAQEALEKVA----------------------LGF-----VHQRKPSQLSGGQRQRVAIARAL 149
Cdd:PRK15064  91 ELWEVKQERDRiyalpeMSEEDGMKVAdlevkfaemdgytaearagellLGVgipeeQHYGLMSEVAPGWKLRVLLAQAL 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16129400  150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslgiTFIFVTHD 194
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHD 211
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 37-89 9.62e-04

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 39.01  E-value: 9.62e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129400  37 GPSGSGKTTCLRLIA---GFEQLSGGAISI--FGKPASN---LPPWERDVNTVFQDYALFP 89
Cdd:cd02020   6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTeeVGKLASEvaaIPEVRKALDERQRELAKKP 66
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 130-205 1.71e-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: 40.38  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   130 RKPSQLSGGQRQRVAIAR----ALVNeprVL-LLDEPlgALDLKLREQMQL--ELKKLqQSLGITFIFVTHDQgEALSMS 202
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATqigsGLTG---VLyVLDEP--SIGLHQRDNRRLinTLKRL-RDLGNTLIVVEHDE-DTIRAA 556


                  ...
gi 16129400   203 DRV 205
Cdd:TIGR00630 557 DYV 559
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 37-160 2.55e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 38.31  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129400   37 GPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLP-PWerdVNTVFQDYALFPHMSILDNVAYGLMVkgvnkKQRHAMA 115
Cdd:PRK13541  33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETL 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16129400  116 QEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 129-205 5.43e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 38.66  E-value: 5.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129400   129 QRKPSQLSGGQRQRVAIARALVNEPR--VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQgEALSMSDRV 205
Cdd:PRK00635  471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLADRI 547
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH