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Conserved domains on  [gi|1582545954|gb|TBD26661|]
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ABC transporter ATP-binding protein [Rhizobium ruizarguesonis]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 47-398 6.39e-164

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 464.19  E-value: 6.39e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:COG3842    86 YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGT 286
Cdd:COG3842   166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPGT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 287 VlrLDAESTLIGLAnDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTQPSESTLPVRMTVSVPLGPSLVHDLALEDGTGLR 366
Cdd:COG3842   246 V--LGDEGGGVRTG-GRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQELV 322

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1582545954 367 AsEVRGPSTFIPEPGTPLFAEIDTARCHAFPA 398
Cdd:COG3842   323 V-RVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 47-398 6.39e-164

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 464.19  E-value: 6.39e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:COG3842    86 YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGT 286
Cdd:COG3842   166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPGT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 287 VlrLDAESTLIGLAnDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTQPSESTLPVRMTVSVPLGPSLVHDLALEDGTGLR 366
Cdd:COG3842   246 V--LGDEGGGVRTG-GRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQELV 322

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1582545954 367 AsEVRGPSTFIPEPGTPLFAEIDTARCHAFPA 398
Cdd:COG3842   323 V-RVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
40-369 2.01e-118

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 349.25  E-value: 2.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  40 NMAERKRL-SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR 118
Cdd:PRK09452    7 QPSSLSPLvELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK09452   87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG 278
Cdd:PRK09452  167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 279 QANLLNGTVLRLDAESTLIGLANDRTLLLPRRLNFTLGSKVTITFRPEEVR---LSTQPSESTLPVRMTVSVPLGPSLVH 355
Cdd:PRK09452  247 EINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRveeINDDEHAEGLIGYVRERNYKGMTLDS 326

                         330
                  ....*....|....
gi 1582545954 356 DLALEDGTGLRASE 369
Cdd:PRK09452  327 VVELENGKMVMVSE 340
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 47-278 1.37e-117

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: 341.91  E-value: 1.37e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG 278
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 46-397 5.07e-109

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: 324.68  E-value: 5.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQ 125
Cdd:TIGR03265   4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:TIGR03265  84 SYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 206 ALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNG 285
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 286 TvlRLDAESTLIG---LANDRTLLLPrrlnftlGSKVTITFRPEEVRLST-QPSESTLPVRMTVSVPLGPSLVHDLALE- 360
Cdd:TIGR03265 244 T--RGGGSRARVGgltLACAPGLAQP-------GASVRLAVRPEDIRVSPaGNAANLLLARVEDMEFLGAFYRLRLRLEg 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 361 -DGTGLRA----SEVRGPSTfipEPGTPLFAEIDTARCHAFP 397
Cdd:TIGR03265 315 lPGQALVAdvsaSEVERLGI---RAGQPIWIELPAERLRAFA 353
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
62-338 2.28e-83

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 258.85  E-value: 2.28e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYALFPHLTVAENIAY 141
Cdd:NF040840   16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 142 PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLH 221
Cdd:NF040840   96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 222 LQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGTVlRLDAESTLIGlAN 301
Cdd:NF040840  176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVA-EKGGEGTILD-TG 253

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1582545954 302 DRTLLLPRRLNftlgSKVTITFRPEEVRLSTQPSEST 338
Cdd:NF040840  254 NIKIELPEEKK----GKVRIGIRPEDITISTEKVKTS 286
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 62-204 6.13e-52

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: 170.91  E-value: 6.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFPHLTVAENI 139
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 140 AYPLACQKLPRAERKARVEEMLSLVRLKDYGNRL----PRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
60-254 9.26e-46

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 157.19  E-value: 9.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  60 NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN------VSARSRGVGMVFQNYALFPHL 133
Cdd:NF038007   19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsysqkIILRRELIGYIFQSFNLIPHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD-RALR 212
Cdd:NF038007   99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDsKNAR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 213 FDLQvELLHLQKTlGITTLIVTHDQeEAQSLANRLVLMNKGN 254
Cdd:NF038007  179 AVLQ-QLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGK 217
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
55-250 1.49e-31

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 118.49  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElgdqdlanvSARSRGVGMVFQNYAL---FP 131
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 hLTVAENIAY----PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:NF040873   72 -LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1582545954 208 DRALRFDLQVELLHLQKTlGITTLIVTHDQEEAqSLANRLVLM 250
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
50-261 2.44e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 105.59  E-value: 2.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ--DLANVSARSRgVGMVFQNY 127
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATRRR-VGYMSQAF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 ALFPHLTVAENIAypLACQ--KLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:NF033858  349 SLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 206 ALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQsLANRLVLMNKGNVEQIDTP 261
Cdd:NF033858  427 GVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTP 481
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
48-261 1.41e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 97.12  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR--------- 118
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpriaymp 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 -GVGmvfQNyaLFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:NF033858   83 qGLG---KN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 198 LLLDEP-----------FGALDRALRfdlqvellhlQKTLGITTLIVTHDQEEAQSLaNRLVLMNKGNVEQIDTP 261
Cdd:NF033858  158 LILDEPttgvdplsrrqFWELIDRIR----------AERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
GguA NF040905
sugar ABC transporter ATP-binding protein;
47-259 1.65e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.07  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGlIQPK---NGRIELGDQDLANVSARS---RGV 120
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDseaLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENIAYPLACQK---LPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:NF040905   81 VIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 198 LLLDEPFGAL---DRALRFDLQVELlhlqKTLGITTLIVTHDQEEAQSLANRL-VLMNKGNVEQID 259
Cdd:NF040905  161 LILDEPTAALneeDSAALLDLLLEL----KAQGITSIIISHKLNEIRRVADSItVLRDGRTIETLD 222
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
44-255 7.08e-16

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 78.24  E-value: 7.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGcgkSTVLRAI--AGLIQPKNGRIELGDQD-LANVSARSRGV 120
Cdd:NF000106   11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G---AA**RGAlpAHV*GPDAGRRPWRF*TwCANRRALRRTI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQ-NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:NF000106   88 G*HRPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 200 LDEPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:NF000106  168 LDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 72-249 3.97e-13

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: 66.63  E-value: 3.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   72 GEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDlanvsarsrgvgmvfqnyalfphltvaeniayplacqklpra 151
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE------------------------------------------ 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  152 erkaRVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVE-----LLHLQKTL 226
Cdd:smart00382  40 ----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115

                          170       180
                   ....*....|....*....|...
gi 1582545954  227 GITTLIVTHDQEEAQSLANRLVL 249
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 47-398 6.39e-164

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 464.19  E-value: 6.39e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:COG3842    86 YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGT 286
Cdd:COG3842   166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPGT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 287 VlrLDAESTLIGLAnDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTQPSESTLPVRMTVSVPLGPSLVHDLALEDGTGLR 366
Cdd:COG3842   246 V--LGDEGGGVRTG-GRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQELV 322

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1582545954 367 AsEVRGPSTFIPEPGTPLFAEIDTARCHAFPA 398
Cdd:COG3842   323 V-RVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 41-399 5.47e-142

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 408.31  E-value: 5.47e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAErkrLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGV 120
Cdd:COG3839     1 MAS---LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:COG3839    78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 201 DEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG-- 278
Cdd:COG3839   158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGsp 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 279 QANLLNGTVLRLDAEstliglANDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTqPSESTLPVRMTVSVPLGPSLVHDLA 358
Cdd:COG3839   238 PMNLLPGTVEGGGVR------LGGVRLPLPAALAAAAGGEVTLGIRPEHLRLAD-EGDGGLEATVEVVEPLGSETLVHVR 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1582545954 359 LEDGTgLRAsevRGPSTFIPEPGTPLFAEIDTARCHAFPAE 399
Cdd:COG3839   311 LGGQE-LVA---RVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 47-392 1.69e-131

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 381.80  E-value: 1.69e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL-ANVSARSRGVGMVFQ 125
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:COG1118    83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 206 ALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNG 285
Cdd:COG1118   163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 286 TVLRLDAESTLIGLANDRTLllprrlnftLGSKVTITFRPEEVRLSTQPS-ESTLPVRMTVSVPLGPSLVHDLALEDGTG 364
Cdd:COG1118   243 RVIGGQLEADGLTLPVAEPL---------PDGPAVAGVRPHDIEVSREPEgENTFPATVARVSELGPEVRVELKLEDGEG 313

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1582545954 365 --LRAsEV--RGPSTFIPEPGTPLFAEIDTAR 392
Cdd:COG1118   314 qpLEA-EVtkEAWAELGLAPGDPVYLRPRPAR 344
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
40-369 2.01e-118

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 349.25  E-value: 2.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  40 NMAERKRL-SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR 118
Cdd:PRK09452    7 QPSSLSPLvELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK09452   87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG 278
Cdd:PRK09452  167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 279 QANLLNGTVLRLDAESTLIGLANDRTLLLPRRLNFTLGSKVTITFRPEEVR---LSTQPSESTLPVRMTVSVPLGPSLVH 355
Cdd:PRK09452  247 EINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRveeINDDEHAEGLIGYVRERNYKGMTLDS 326

                         330
                  ....*....|....
gi 1582545954 356 DLALEDGTGLRASE 369
Cdd:PRK09452  327 VVELENGKMVMVSE 340
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 47-278 1.37e-117

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: 341.91  E-value: 1.37e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG 278
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 46-397 5.07e-109

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: 324.68  E-value: 5.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQ 125
Cdd:TIGR03265   4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:TIGR03265  84 SYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 206 ALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNG 285
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 286 TvlRLDAESTLIG---LANDRTLLLPrrlnftlGSKVTITFRPEEVRLST-QPSESTLPVRMTVSVPLGPSLVHDLALE- 360
Cdd:TIGR03265 244 T--RGGGSRARVGgltLACAPGLAQP-------GASVRLAVRPEDIRVSPaGNAANLLLARVEDMEFLGAFYRLRLRLEg 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 361 -DGTGLRA----SEVRGPSTfipEPGTPLFAEIDTARCHAFP 397
Cdd:TIGR03265 315 lPGQALVAdvsaSEVERLGI---RAGQPIWIELPAERLRAFA 353
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 47-259 2.91e-107

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: 314.84  E-value: 2.91e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQID 259
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 77-371 8.51e-104

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: 310.19  E-value: 8.51e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  77 LLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKAR 156
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 157 VEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHD 236
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 237 QEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGTVLRLDAESTLIGLANDRTLLLPRRLNFTLG 316
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 317 SKVTITFRPEEVRLSTQP---SESTLPVRMTVSVPLGPSLVHDLALEDGTGLRASEVR 371
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDeanSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFF 298
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
41-399 2.14e-103

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 310.24  E-value: 2.14e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAErkrLSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG 119
Cdd:PRK11650    1 MAG---LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:PRK11650   78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 200 LDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG- 278
Cdd:PRK11650  158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGs 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 279 -QANLLNGTVlrlDAESTLIGLANDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTQpsESTLPVRMTVSVPLGP-SLVHd 356
Cdd:PRK11650  238 pAMNLLDGRV---SADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSA--EGGVPLTVDTVELLGAdNLAH- 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1582545954 357 laledgtGLRASE---VRGPSTFIPEPGTPLFAEIDTARCHAFPAE 399
Cdd:PRK11650  312 -------GRWGGQplvVRLPHQERPAAGSTLWLHLPANQLHLFDAD 350
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 49-279 1.83e-100

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: 298.48  E-value: 1.83e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYA 128
Cdd:cd03296     5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 129 LFPHLTVAENIAYPL----ACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:cd03296    85 LFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 205 GALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQ 279
Cdd:cd03296   165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 41-253 1.44e-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: 289.30  E-value: 1.44e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERK-RLSVQGLTHSY----GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDlanVSA 115
Cdd:COG1116     1 MSAAApALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP---VTG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 RSRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRP 195
Cdd:COG1116    78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 196 SLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:COG1116   158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
47-334 1.74e-96

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 293.67  E-value: 1.74e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:PRK11607  100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGt 286
Cdd:PRK11607  180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG- 258

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 287 VLRLDAESTLIglANDRTLLLPRRLNFTL----GSKVTITFRPEEVRLSTQP 334
Cdd:PRK11607  259 VLKERQEDGLV--IDSPGLVHPLKVDADAsvvdNVPVHVALRPEKIMLCEEP 308
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 49-283 2.71e-95

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 285.54  E-value: 2.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYA 128
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 129 LFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:TIGR00968  83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 209 RALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLL 283
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
49-350 4.14e-93

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 283.90  E-value: 4.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYA 128
Cdd:PRK10851    5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 129 LFPHLTVAENIAYPLACqkLPRAER------KARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:PRK10851   85 LFRHMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANL 282
Cdd:PRK10851  163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 283 LNGTVLrldAESTLIGLANdrtllLPrrLNFT--LGSKVTITFRPEEVRLSTQPS-ESTLPVRMTVSVPLG 350
Cdd:PRK10851  243 LQGTIR---GGQFHVGAHR-----WP--LGYTpaYQGPVDLFLRPWEVDISRRTSlDSPLPVQVLEVSPKG 303
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 47-259 1.25e-89

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: 269.89  E-value: 1.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQID 259
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 47-252 1.70e-89

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: 269.73  E-value: 1.70e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDlanVSARSRGVGM 122
Cdd:cd03293     1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---VTGPGPDRGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNK 252
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 50-279 1.99e-89

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 272.73  E-value: 1.99e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQN 126
Cdd:COG1125     5 ENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRL--KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:COG1125    85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 205 GALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQ 279
Cdd:COG1125   165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
41-337 8.13e-89

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 272.75  E-value: 8.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGV 120
Cdd:PRK11432    1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:PRK11432   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 201 DEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQA 280
Cdd:PRK11432  161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 281 NLLNGTvlrLDAESTLIGlandrTLLLPRRLNFTLG---SKVTITFRPEEVRLSTQPSES 337
Cdd:PRK11432  241 NIFPAT---LSGDYVDIY-----GYRLPRPAAFAFNlpdGECTVGVRPEAITLSEQGEES 292
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
62-338 2.28e-83

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 258.85  E-value: 2.28e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYALFPHLTVAENIAY 141
Cdd:NF040840   16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 142 PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLH 221
Cdd:NF040840   96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 222 LQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGTVlRLDAESTLIGlAN 301
Cdd:NF040840  176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVA-EKGGEGTILD-TG 253

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1582545954 302 DRTLLLPRRLNftlgSKVTITFRPEEVRLSTQPSEST 338
Cdd:NF040840  254 NIKIELPEEKK----GKVRIGIRPEDITISTEKVKTS 286
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 61-261 1.32e-82

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 258.11  E-value: 1.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA------RSRGVGMVFQNYALFPHLT 134
Cdd:COG4175    42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKkelrelRRKKMSMVFQHFALLPHRT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFD 214
Cdd:COG4175   122 VLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582545954 215 LQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:COG4175   202 MQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTP 248
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 47-283 1.45e-82

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 252.99  E-value: 1.45e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRGVGMV 123
Cdd:cd03295     1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRL--KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQAN 281
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240


                  ..
gi 1582545954 282 LL 283
Cdd:cd03295   241 LL 242
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 61-277 1.60e-81

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: 251.41  E-value: 1.60e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA------RSRGVGMVFQNYALFPHLT 134
Cdd:cd03294    39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMVFQSFALLPHRT 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFD 214
Cdd:cd03294   119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 215 LQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFI 277
Cdd:cd03294   199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
48-396 2.52e-81

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 254.18  E-value: 2.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNY 127
Cdd:PRK11000    5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 ALFPHLTVAENIAYPLACQKLPRAERKARVE---EMLSLVRLKDygnRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:PRK11000   85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 205 GALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIG--QANL 282
Cdd:PRK11000  162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNF 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 283 LNGTVLRLDAESTLIGLANDRTLLLP-RRLNFTLGSKVTITFRPEEVrLSTQPSESTLPVRMTVSVPLG-PSLVHdLALE 360
Cdd:PRK11000  242 LPVKVTATAIEQVQVELPNRQQVWLPvEGRGVQVGANMSLGIRPEHL-LPSDIADVTLEGEVQVVEQLGnETQIH-IQIP 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1582545954 361 dgtGLRASEV-RGPSTFIPEPGTPLFAEIDTARCHAF 396
Cdd:PRK11000  320 ---AIRQNLVyRQNDVVLVEEGATFAIGLPPERCHLF 353
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 47-261 5.95e-78

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: 241.04  E-value: 5.95e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGVG 121
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHLTVAENIAYPL-ACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:COG1127    86 MLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 201 DEPFGALD--RALRFDlqvEL-LHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:COG1127   166 DEPTAGLDpiTSAVID---ELiRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
47-256 2.26e-77

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 239.17  E-value: 2.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYG-GQN---AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA------R 116
Cdd:COG1136     5 LELRNLTKSYGtGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelarlR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPS 196
Cdd:COG1136    85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 197 LLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDqEEAQSLANRLVLMNKGNVE 256
Cdd:COG1136   165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 49-337 5.67e-77

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


Pssm-ID: 132302 [Multi-domain]  Cd Length: 362  Bit Score: 242.98  E-value: 5.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK--NGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:TIGR03258   8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPPHKRGLALLFQN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:TIGR03258  88 YALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 207 LDRALRFDLQVELLHLQKTL-GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNG 285
Cdd:TIGR03258 168 LDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 286 TVLRLDAESTLIGLANDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTQPSES 337
Cdd:TIGR03258 248 IALGITEAPGLVDVSCGGAVIFAFGDGRHDGRDKLACIRPEHLALTPRPAGE 299
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 64-367 1.44e-75

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: 238.85  E-value: 1.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA------NVSARSRGVGMVFQNYALFPHLTVAE 137
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiFLPPHRRRIGYVFQEARLFPHLSVRG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYplACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQV 217
Cdd:COG4148    97 NLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 218 ELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGTVLRLDAESTLI 297
Cdd:COG4148   175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGLT 254

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 298 GLA-NDRTLLLPrRLNFTLGSKVTITFRPEEVRLSTQPSEST-----LPVRMTVSVPLGPSLVhDLALE-DGTGLRA 367
Cdd:COG4148   255 RLAlGGGRLWVP-RLDLPPGTRVRVRIRARDVSLALEPPEGSsilniLPGRVVEIEPADGGQV-LVRLDlGGQTLLA 329
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 47-282 1.49e-74

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: 232.23  E-value: 1.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGgQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:cd03299     1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANL 282
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 47-270 1.50e-74

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 232.19  E-value: 1.50e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL----ANVSARSRGVGM 122
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAY-PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 202 EPFGALDRALrfdlqV-ELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKT 270
Cdd:COG1126   162 EPTSALDPEL-----VgEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 47-269 7.59e-73

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: 236.72  E-value: 7.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-----GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS---- 117
Cdd:COG1123   261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 -RGVGMVFQN--YALFPHLTVAENIAYPLACQK-LPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIA 192
Cdd:COG1123   341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 193 GRPSLLLLDEPFGALDRALRFDLqVELL-HLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:COG1123   421 LEPKLLILDEPTSALDVSVQAQI-LNLLrDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 47-255 5.23e-72

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: 225.06  E-value: 5.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA------R 116
Cdd:cd03255     1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPS 196
Cdd:cd03255    81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 197 LLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAqSLANRLVLMNKGNV 255
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 64-259 4.14e-71

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: 222.56  E-value: 4.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEaGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL------ANVSARSRGVGMVFQNYALFPHLTVAE 137
Cdd:cd03297    16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQRKIGLVFQQYALFPHLNVRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLacQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQV 217
Cdd:cd03297    95 NLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 218 ELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQID 259
Cdd:cd03297   173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
50-255 5.34e-71

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 222.62  E-value: 5.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGVGMV 123
Cdd:COG2884     5 ENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:COG2884    85 FQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 204 FGALDRALRFDLqVELLH-LQKtLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG2884   165 TGNLDPETSWEI-MELLEeINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
46-250 4.00e-70

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 221.66  E-value: 4.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARsRGVg 121
Cdd:COG4525     3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-RGV- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 mVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:COG4525    81 -VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLM 250
Cdd:COG4525   160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
47-261 1.58e-69

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 219.16  E-value: 1.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRgVGMVF 124
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdPAEVRRR-IGYVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:COG1131    80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 205 GALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:COG1131   160 SGLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 47-271 3.10e-69

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: 218.36  E-value: 3.10e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL--ANVSARSRGVGMV 123
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQN--YALFpHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:COG1122    81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:COG1122   160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 47-253 1.41e-68

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: 214.74  E-value: 1.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA----NVSARSRGVGM 122
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAYPlacqklpraerkarveemlslvrlkdygnrlpreLSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
47-314 3.34e-68

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 219.18  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS----- 117
Cdd:COG1135     2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 198 LLLDEPFGALD----RALrfdLQVeLLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIdtpmTVYD---RPK 269
Cdd:COG1135   162 LLCDEATSALDpettRSI---LDL-LKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRiVEQG----PVLDvfaNPQ 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 270 TLFVNTFIGQanlLNGTVLRLDAESTLIGLANDRTLLlprRLNFT 314
Cdd:COG1135   234 SELTRRFLPT---VLNDELPEELLARLREAAGGGRLV---RLTFV 272
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
47-255 2.62e-66

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 210.77  E-value: 2.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDvaFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQN 126
Cdd:COG3840     2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARA-IAGRPsLLLLDEPFG 205
Cdd:COG3840    80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARClVRKRP-ILLLDEPFS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 206 ALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG3840   159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 47-253 4.22e-66

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: 209.69  E-value: 4.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL----ANVSARSRGVGM 122
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAY-PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 202 EPFGALDRALRFD-LQVeLLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03262   161 EPTSALDPELVGEvLDV-MKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 47-261 5.82e-66

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: 210.05  E-value: 5.82e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGVG 121
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHLTVAENIAYPL-ACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 201 DEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 47-257 1.04e-65

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 209.28  E-value: 1.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA-----RS 117
Cdd:cd03257     2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkiRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNY--ALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRL---KDYGNRLPRELSGGQQQRVAVARAIA 192
Cdd:cd03257    82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 193 GRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQ 257
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 48-253 5.72e-65

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: 206.55  E-value: 5.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRGVGMV 123
Cdd:cd03225     1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTklSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQN--YALFpHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:cd03225    81 FQNpdDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03225   160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 47-260 1.45e-64

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: 206.96  E-value: 1.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYG----GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGV 120
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNY--ALFPHLTVAENIAYPLACQKLPRAERkaRVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 198 LLLDEPFGALDRAlrfdLQVELLHL----QKTLGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIDT 260
Cdd:COG1124   160 LLLDEPTSALDVS----VQAEILNLlkdlREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRiVEELTV 223
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 47-269 2.30e-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: 198.19  E-value: 2.30e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS-----ARS 117
Cdd:cd03258     2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 198 LLLDEPFGALDRALRFDLqVELLH-LQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:cd03258   162 LLCDEATSALDPETTQSI-LALLRdINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 41-261 8.01e-61

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 197.23  E-value: 8.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARsrgV 120
Cdd:COG1121     1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---I 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYAL---FPhLTVAENIAYPLACQ----KLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAG 193
Cdd:COG1121    78 GYVPQRAEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 194 RPSLLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNK-----GNVEQIDTP 261
Cdd:COG1121   157 DPDLLLLDEPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRglvahGPPEEVLTP 228
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 47-249 1.19e-60

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 195.39  E-value: 1.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK---NGRIELGDQDLANVSARSRGVGMV 123
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLAcQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:COG4136    82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1582545954 204 FGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVL 249
Cdd:COG4136   161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 47-271 2.91e-60

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: 203.60  E-value: 2.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK---NGRIELGDQDLANVSARSRG-- 119
Cdd:COG1123     5 LEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQN--YALFPhLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:COG1123    85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 198 LLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:COG1123   164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 47-253 3.25e-59

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: 192.40  E-value: 3.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLI-----QPKNGRIELGDQDLA----NVSARS 117
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdldvDVLELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNYALFPhLTVAENIAYPLACQ-KLPRAERKARVEEMLSLVRLKDYGNR--LPRELSGGQQQRVAVARAIAGR 194
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 195 PSLLLLDEPFGALDRALRFDLQvELLH-LQKTlgITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIE-ELIAeLKKE--YTIVIVTHNMQQAARVADRTAFLLNG 216
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 46-264 1.02e-58

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: 191.80  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR--SRGVGMV 123
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelARRIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIA---YP-LACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:COG1120    81 PQEPPAPFGLTVRELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 200 LDEPFGALDraLRFdlQVELLHLQKTL----GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:COG1120   161 LDEPTSHLD--LAH--QLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 47-270 2.05e-58

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 191.00  E-value: 2.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ--DLAN------VSARSR 118
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtpsdkaIRELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAEN-IAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 198 LLLDEPFGALDRALRFDLqVELLH-LQKTlGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIDTpmTVYDRPKT 270
Cdd:PRK11124  163 LLFDEPTAALDPEITAQI-VSIIReLAET-GITQVIVTHEVEVARKTASRVVYMENGHiVEQGDA--SCFTQPQT 233
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
47-270 7.32e-58

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 189.45  E-value: 7.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL---ANVSARS-----R 118
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllrQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAEN-IAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:COG4161    83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 198 LLLDEPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIDTpmTVYDRPKT 270
Cdd:COG4161   163 LLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRiIEQGDA--SHFTQPQT 233
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
47-253 3.79e-57

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 187.98  E-value: 3.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSArSRGVgmVFQN 126
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGV--VFQN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:PRK11248   79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582545954 207 LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK11248  159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 47-255 6.65e-57

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 186.49  E-value: 6.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR---SRGVGMV 123
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiaRLGIGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAypLACQ----------KLPRAERKAR--VEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAI 191
Cdd:cd03219    81 FQIPRLFPELTVLENVM--VAAQartgsglllaRARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03219   159 ATDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 47-267 7.60e-57

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: 186.60  E-value: 7.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRgVGMVF 124
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARRQ-IGVLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:COG4555    81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 205 GALD----RALRfdlqvELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDR 267
Cdd:COG4555   161 NGLDvmarRLLR-----EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 47-253 1.91e-56

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: 186.01  E-value: 1.91e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR---SRGVGMV 123
Cdd:COG0411     5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriaRLGIART 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIA----------YPLACQKLPRAERK-----ARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVA 188
Cdd:COG0411    85 FQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRARREerearERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLqVELLH-LQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:COG0411   165 RALATEPKLLLLDEPAAGLNPEETEEL-AELIRrLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 47-268 1.06e-55

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 184.10  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGV 120
Cdd:COG3638     3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENI---------AYPLACQKLPRAERkARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAI 191
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 192 AGRPSLLLLDEPFGALDRAL-RfdlQV-ELL-HLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVeqidtpmtVYDRP 268
Cdd:COG3638   162 VQEPKLILADEPVASLDPKTaR---QVmDLLrRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGP 230
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 47-255 1.08e-55

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: 183.02  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR---GVGMV 123
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAypLACQKLPRAERKARVEEMLSLV-RLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:cd03224    81 PEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03224   159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 47-261 1.45e-55

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: 184.17  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQ--NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA----RSRgV 120
Cdd:TIGR04520   1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlweiRKK-V 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNyalfPH-----LTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRP 195
Cdd:TIGR04520  80 GMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 196 SLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAqSLANRLVLMNKGNVEQIDTP 261
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTP 220
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 62-269 2.50e-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: 182.67  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANvSARSRGVgmVFQNYALFPHLTVAENIAY 141
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 142 PLAC--QKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVEL 219
Cdd:TIGR01184  78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 220 LHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV-YDRPK 269
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 47-269 3.31e-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: 184.87  E-value: 3.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKN---GRIELGDQDLANVSA---- 115
Cdd:COG0444     2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEkelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 --RSRGVGMVFQN-Y-ALFPHLTVAENIAYPL-ACQKLPRAERKARVEEMLSLVRL---KDYGNRLPRELSGGQQQRVAV 187
Cdd:COG0444    82 kiRGREIQMIFQDpMtSLNPVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 188 ARAIAGRPSLLLLDEPFGALD---RAlrfdlQV-ELLH-LQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIDTP 261
Cdd:COG0444   162 ARALALEPKLLIADEPTTALDvtiQA-----QIlNLLKdLQRELGLAILFITHDLGVVAEIADRVAVMYAGRiVEEGPVE 236


                  ....*...
gi 1582545954 262 mTVYDRPK 269
Cdd:COG0444   237 -ELFENPR 243
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 47-271 5.00e-55

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: 183.04  E-value: 5.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGG-----QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA-----NVSAR 116
Cdd:TIGR04521   1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQN--YALFpHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAG 193
Cdd:TIGR04521  81 RKKVGLVFQFpeHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 194 RPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
47-255 9.82e-55

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 180.01  E-value: 9.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA---RSRgVGMV 123
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewRRQ-VAYV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHlTVAENIAYPLACQKLPRAErkARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:COG4619    80 PQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG4619   157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
50-268 1.03e-54

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 181.06  E-value: 1.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGV----GMVFQ 125
Cdd:PRK09493    5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAY-PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:PRK09493   85 QFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 205 GALDRALRFdlqvELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRP 268
Cdd:PRK09493  165 SALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 48-255 1.08e-54

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: 180.04  E-value: 1.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARsrgVGMVFQNY 127
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 AL---FPhLTVAENIA----YPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:cd03235    78 SIdrdFP-ISVRDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 201 DEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03235   157 DEPFAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 64-388 1.54e-54

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: 184.55  E-value: 1.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR------SRGVGMVFQNYALFPHLTVAE 137
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppeKRRIGYVFQEARLFPHLSVRG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLA-CQKLPRAERKARVEEMLSLVRLKDygnRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQ 216
Cdd:TIGR02142  95 NLRYGMKrARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 217 VELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRP--KTLFVNTfigQANLLNGTVLRLDAES 294
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPdlPWLARED---QGSLIEGVVAEHDQHY 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 295 TLIGLA-NDRTLLLPRRLNfTLGSKVTITFRPEEVRLSTQPSEST-----LPVRM-------TVSVPLGPSLVHDLALED 361
Cdd:TIGR02142 249 GLTALRlGGGHLWVPENLG-PTGARLRLRVPARDVSLALQKPEATsirniLPARVveiedsdIGRVGVVLESGGKTLWAR 327

                         330       340
                  ....*....|....*....|....*..
gi 1582545954 362 GTGLRASEVRgpstfiPEPGTPLFAEI 388
Cdd:TIGR02142 328 ITRWARDELG------IAPGTPVFAQI 348
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 47-269 3.15e-53

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 179.93  E-value: 3.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQ-----------NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA 115
Cdd:COG4608     8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 RS-----RGVGMVFQN-YA-LFPHLTVAENIAYPLACQKL-PRAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVA 186
Cdd:COG4608    88 RElrplrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 187 VARAIAGRPSLLLLDEPFGALD---RAlrfdlQV--ELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:COG4608   168 IARALALNPKLIVCDEPVSALDvsiQA-----QVlnLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242


                  ....*...
gi 1582545954 262 MTVYDRPK 269
Cdd:COG4608   243 DELYARPL 250
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 47-255 1.29e-52

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: 173.35  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG-VGMVFQ 125
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIayplacqklpraerkarveemlslvrlkdygnrlprELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 206 ALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 62-204 6.13e-52

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: 170.91  E-value: 6.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFPHLTVAENI 139
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 140 AYPLACQKLPRAERKARVEEMLSLVRLKDYGNRL----PRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 47-261 1.46e-51

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 172.30  E-value: 1.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGG--QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA-NVSARSRGVGMV 123
Cdd:cd03263     1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtDRKAARQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 204 FGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:cd03263   161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 47-246 2.41e-50

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: 169.54  E-value: 2.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQ----NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS------AR 116
Cdd:COG4181     9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARveEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPS 196
Cdd:COG4181    89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 197 LLLLDEPFGALDRA-------LRFDlqvellhLQKTLGITTLIVTHDQEeaqsLANR 246
Cdd:COG4181   167 ILFADEPTGNLDAAtgeqiidLLFE-------LNRERGTTLVLVTHDPA----LAAR 212
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
41-261 2.62e-50

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 170.97  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKrLSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL--ANVSAR 116
Cdd:PRK13635    1 MKEEI-IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETVWDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNY-ALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRP 195
Cdd:PRK13635   80 RRQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 196 SLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTP 261
Cdd:PRK13635  160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 48-255 7.01e-50

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: 166.46  E-value: 7.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRgvgmvfqny 127
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 alfphltvAENIAYplacqklpraerkarVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:cd03214    72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 208 DralrFDLQVELLHLQKTL----GITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03214   129 D----IAHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRI 176
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 50-278 9.54e-50

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 171.52  E-value: 9.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSYGGQ----NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGV 120
Cdd:PRK11153    5 KNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:PRK11153   85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 201 DEPFGALD----RALrfdlqVELL-HLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNT 275
Cdd:PRK11153  165 DEATSALDpattRSI-----LELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239


                  ...
gi 1582545954 276 FIG 278
Cdd:PRK11153  240 FIQ 242
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 47-268 1.00e-49

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: 168.13  E-value: 1.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYG-GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANV------SARSRg 119
Cdd:cd03256     1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkalrQLRRQ- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYALFPHLTVAENIAYPLACQK---------LPRAErKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARA 190
Cdd:cd03256    80 IGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 191 IAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVeqidtpmtVYDRP 268
Cdd:cd03256   159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGP 228
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 47-255 1.17e-49

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: 167.85  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR---GVGMV 123
Cdd:COG0410     4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENI---AYPLAcqklPRAERKARVEEMLSLV-RLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:COG0410    84 PEGRRIFPSLTVEENLllgAYARR----DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 200 LDEP------------FGALdRALRfdlqvellhlqkTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG0410   160 LDEPslglapliveeiFEII-RRLN------------REGVTILLVEQNARFALEIADRAYVLERGRI 214
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
67-301 1.26e-49

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 167.84  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  67 FDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYALFPHLTVAENIAYPLACQ 146
Cdd:PRK10771   20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 147 KLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRfdlqVELLHLQKTL 226
Cdd:PRK10771  100 LKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR----QEMLTLVSQV 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 227 ----GITTLIVTHDQEEAQSLANRLVLMNKGNVeqidtpmtVYDRPKtlfvntfigqANLLNGTVlrldAESTLIGLAN 301
Cdd:PRK10771  176 cqerQLTLLMVSHSLEDAARIAPRSLVVADGRI--------AWDGPT----------DELLSGKA----SASALLGIKS 232
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 49-279 1.34e-49

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 168.39  E-value: 1.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGD----------QDLANVSARSR 118
Cdd:PRK11264    6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsQQKGLIRQLRQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAEN-IAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:PRK11264   86 HVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 198 LLLDEPFGALDRalrfDLQVELLHLQKTLG---ITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK----T 270
Cdd:PRK11264  166 ILFDEPTSALDP----ELVGEVLNTIRQLAqekRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQqprtR 241


                  ....*....
gi 1582545954 271 LFVNTFIGQ 279
Cdd:PRK11264  242 QFLEKFLLQ 250
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 52-253 1.81e-49

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: 166.65  E-value: 1.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  52 LTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGVGMVFQ 125
Cdd:TIGR02673   7 VSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:TIGR02673  87 DFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 206 ALDRalrfDLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:TIGR02673 167 NLDP----DLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDG 213
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 55-255 2.57e-49

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: 166.13  E-value: 2.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNAISDVAFdiEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYALFPHLT 134
Cdd:cd03298     9 SYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFD 214
Cdd:cd03298    87 VEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1582545954 215 LQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03298   167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 57-255 1.63e-48

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: 164.12  E-value: 1.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  57 GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGVGMVFQNYALFP 131
Cdd:cd03292    12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGVVFQDFRLLP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:cd03292    92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1582545954 212 RFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03292   172 TWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
47-270 2.59e-48

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 164.97  E-value: 2.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA----------- 115
Cdd:COG4598     9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpadrr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 -----RSRgVGMVFQNYALFPHLTVAEN-IAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVAR 189
Cdd:COG4598    89 qlqriRTR-LGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 190 AIAGRPSLLLLDEPFGALDRalrfDLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYD 266
Cdd:COG4598   168 ALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243


                  ....
gi 1582545954 267 RPKT 270
Cdd:COG4598   244 NPKS 247
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 35-274 3.87e-48

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 164.44  E-value: 3.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  35 MLGIPNMAERKrLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLI--QPKN---GRIELGDQD 109
Cdd:COG1117     1 MTAPASTLEPK-IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 110 LAN-----VSARSRgVGMVFQNYALFPHlTVAENIAYPLACQ-KLPRAERKARVEEMLSLVRL----KDYGNRLPRELSG 179
Cdd:COG1117    80 IYDpdvdvVELRRR-VGMVFQKPNPFPK-SIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 180 GQQQRVAVARAIAGRPSLLLLDEPFGALD--RALRFDlqvELLH-LQKTLGIttLIVTHDQEEAQSLANRLVLMNKGN-V 255
Cdd:COG1117   158 GQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE---ELILeLKKDYTI--VIVTHNMQQAARVSDYTAFFYLGElV 232

                         250
                  ....*....|....*....
gi 1582545954 256 EqidtpmtvYDRPKTLFVN 274
Cdd:COG1117   233 E--------FGPTEQIFTN 243
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 47-268 1.15e-47

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: 162.85  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN-AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGV 120
Cdd:TIGR02315   2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENI-----AYPLACQKL----PRAErKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAI 191
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLlgrfSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVeqidtpmtVYDRP 268
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI--------VFDGA 229
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 47-255 5.14e-47

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 160.79  E-value: 5.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN--VSARSR-GVGMV 123
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRARlGIGYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:cd03218    81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 204 FGALDRALRFDLQvELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03218   161 FAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 61-270 8.49e-47

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: 167.94  E-value: 8.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIqPKNGRIELGDQDLANVSARS-----RGVGMVFQN-YA-LFPHL 133
Cdd:COG4172   301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRM 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLA--CQKLPRAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRA 210
Cdd:COG4172   380 TVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 211 LRFDLqVELL-HLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIDTPmTVYDRPKT 270
Cdd:COG4172   460 VQAQI-LDLLrDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKvVEQGPTE-QVFDAPQH 519
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 49-241 1.78e-46

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


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 158.55  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANV-SARSRG-----VGM 122
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnSKKASKfrrekLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582545954 203 PFGALDRALRfDLQVELLHLQKTLGITTLIVTHDQEEAQ 241
Cdd:TIGR03608 161 PTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDPEVAK 198
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 47-253 2.83e-46

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: 158.15  E-value: 2.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIE-LGDQDLANVSARSRgVGMVFQ 125
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRR-IGALIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYpLACQKLpraERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:cd03268    80 APGFYPNLTARENLRL-LARLLG---IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 206 ALD----RALRfdlqvELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03268   156 GLDpdgiKELR-----ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 46-240 2.87e-46

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: 158.03  E-value: 2.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG-VGMVF 124
Cdd:COG4133     2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYALFPHLTVAENIAypLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:COG4133    82 HADGLKPELTVRENLR--FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 205 GALDRAlrfdlQVELL------HLQKtlGITTLIVTHDQEEA 240
Cdd:COG4133   160 TALDAA-----GVALLaeliaaHLAR--GGAVLLTTHQPLEL 194
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 46-255 3.02e-46

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 159.04  E-value: 3.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN--VSARSR-GVGM 122
Cdd:COG1137     3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKRARlGIGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:COG1137    83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 203 PFGALDRALRFDLQVELLHLqKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG1137   163 PFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKV 214
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 48-253 3.23e-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: 156.25  E-value: 3.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--ARSRGVGMVFQ 125
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPleELRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 nyalfphltvaeniayplacqklpraerkarveemlslvrlkdygnrlpreLSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:cd00267    81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1582545954 206 ALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd00267   110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
45-276 3.23e-46

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 163.67  E-value: 3.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS------ARSR 118
Cdd:PRK10070   27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelreVRRK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK10070  107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTF 276
Cdd:PRK10070  187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 69-258 3.45e-46

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 158.10  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  69 IEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVFQNYALFPHLTVAENIAYPLACQKL 148
Cdd:TIGR01277  21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGLK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 149 PRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRfdlqVELLHLQKTLG- 227
Cdd:TIGR01277 101 LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR----EEMLALVKQLCs 176

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1582545954 228 ---ITTLIVTHDQEEAQSLANRLVLMNKGNVEQI 258
Cdd:TIGR01277 177 erqRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 47-255 4.50e-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: 157.74  E-value: 4.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGeIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQD-LANVSARSRGVGMVFQ 125
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvLKQPQKLRRRIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 206 ALDRALRfdlqVELLHLQKTLGITTLIV--THDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03264   160 GLDPEER----IRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKL 207
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
60-254 9.26e-46

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 157.19  E-value: 9.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  60 NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN------VSARSRGVGMVFQNYALFPHL 133
Cdd:NF038007   19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsysqkIILRRELIGYIFQSFNLIPHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD-RALR 212
Cdd:NF038007   99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDsKNAR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 213 FDLQvELLHLQKTlGITTLIVTHDQeEAQSLANRLVLMNKGN 254
Cdd:NF038007  179 AVLQ-QLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGK 217
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 44-261 1.41e-45

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: 167.32  E-value: 1.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQ--NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RG 119
Cdd:COG2274   471 KGDIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQ 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYALFpHLTVAENIAypLACQKLPRAErkarVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVA 188
Cdd:COG2274   551 IGVVLQDVFLF-SGTIRENIT--LGDPDATDEE----IIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQsLANRLVLMNKGNVEQIDTP 261
Cdd:COG2274   624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTH 693
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 37-255 1.99e-45

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 157.53  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  37 GIPnmaerkrLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR 116
Cdd:PRK11247   10 GTP-------LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRgvgMVFQNYALFPHLTVAENIAYPLacqklpRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPS 196
Cdd:PRK11247   83 TR---LMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 197 LLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK11247  154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
cbiO PRK13637
energy-coupling factor transporter ATPase;
49-271 2.58e-45

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 158.29  E-value: 2.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYG-----GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL----ANVSARSRG 119
Cdd:PRK13637    5 IENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLSDIRKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQ--NYALFPHlTVAENIAYPLACQKLPRAERKARVEEMLSLVRLK--DYGNRLPRELSGGQQQRVAVARAIAGRP 195
Cdd:PRK13637   85 VGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 196 SLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13637  164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 47-260 4.32e-45

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: 156.89  E-value: 4.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY---------GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS 117
Cdd:TIGR02769   3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 -----RGVGMVFQNY--ALFPHLTVAENIAYPLA-CQKLPRAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVAVA 188
Cdd:TIGR02769  83 rrafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN-VEQIDT 260
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQiVEECDV 235
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 47-269 6.08e-45

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


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 155.92  E-value: 6.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGL-----IQPKNGRIELGDQDL----ANVSARS 117
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIydkkIDVVELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNYALFPhLTVAENIAYPLACQKL-PRAERKARVEEMLSLV--------RLKDYGNRLprelSGGQQQRVAVA 188
Cdd:TIGR00972  82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAalwdevkdRLHDSALGL----SGGQQQRLCIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRfdLQVELL--HLQKTLgiTTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYD 266
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIAT--GKIEELiqELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFT 232


                  ...
gi 1582545954 267 RPK 269
Cdd:TIGR00972 233 NPK 235
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 47-251 1.01e-44

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 154.43  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYG-GQNAI---SDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG--- 119
Cdd:TIGR02211   2 LKCENLGKRYQeGKLDTrvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 ---VGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPS 196
Cdd:TIGR02211  82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 197 LLLLDEPFGALDRALR---FDLqveLLHLQKTLGITTLIVTHDQEEAQSLANRLVLMN 251
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAkiiFDL---MLELNRELNTSFLVVTHDLELAKKLDRVLEMKD 216
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 49-261 1.80e-44

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: 153.68  E-value: 1.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDlanVSARSRGV----GMVF 124
Cdd:cd03265     3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD---VVREPREVrrriGIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:cd03265    80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 205 GALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:cd03265   160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 47-253 4.42e-44

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: 151.00  E-value: 4.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGM 122
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFpHLTVAENIayplacqklpraerkarveemlslvrlkdygnrlpreLSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:cd03228    81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQsLANRLVLMNKG 253
Cdd:cd03228   123 ATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDG 170
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 47-255 1.21e-43

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: 151.75  E-value: 1.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY----GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA-NVSARSRGVG 121
Cdd:cd03266     2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkEPAEARRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 202 EPFGALD----RALRfdlqvELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03266   162 EPTTGLDvmatRALR-----EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 47-255 1.35e-43

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: 151.91  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR---GVGMV 123
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLACqkLPRAERKaRVEEMLSLVR-LKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLAA--LPRRSRK-IPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 48-253 2.58e-43

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: 150.10  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYG-GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANvSARSRGVGMVFQN 126
Cdd:cd03226     1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 --YALFPHlTVAENIAYPLacqKLPrAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:cd03226    80 vdYQLFTD-SVREELLLGL---KEL-DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 205 GALDRAlRFDLQVEL-LHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03226   155 SGLDYK-NMERVGELiRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
cbiO PRK13650
energy-coupling factor transporter ATPase;
62-271 5.14e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 151.81  E-value: 5.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRGVGMVFQNY-ALFPHLTVAEN 138
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 139 IAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVE 218
Cdd:PRK13650  103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 219 LLHLQKTLGITTLIVTHDQEEAqSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13650  183 IKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
47-264 9.70e-43

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 150.27  E-value: 9.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS----ARSRGVgm 122
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelARRRAV-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYAL-FPhLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIA-------GR 194
Cdd:COG4559    80 LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 195 PSLLLLDEPFGALDRAlrfdLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:COG4559   159 PRWLFLDEPTSALDLA----HQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 47-261 1.56e-42

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: 156.84  E-value: 1.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMV 123
Cdd:COG4988   337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFpHLTVAENIAypLACqklPRAERkARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARAIA 192
Cdd:COG4988   417 PQNPYLF-AGTIRENLR--LGR---PDASD-EELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 193 GRPSLLLLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTHDqEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:COG4988   490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTH 555
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 47-264 4.61e-42

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 148.77  E-value: 4.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS----ARSRGVgm 122
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelARRRAV-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYAL-FPhLTVAENIA---YPLAcqkLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIA------ 192
Cdd:PRK13548   81 LPQHSSLsFP-FTVEEVVAmgrAPHG---LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 193 GRPSLLLLDEPFGALDraLRFdlQVELLHLQKTL----GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:PRK13548  157 GPPRWLLLDEPTSALD--LAH--QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 41-269 7.95e-42

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: 154.46  E-value: 7.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSYGG----QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKN----GRIELGDQDLAN 112
Cdd:COG4172     1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 113 VSARS----RG--VGMVFQN--YALFPHLTVAENIAYPLAC-QKLPRAERKARVEEMLSLVRLKDYGNRL---PRELSGG 180
Cdd:COG4172    81 LSERElrriRGnrIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 181 QQQRVAVARAIAGRPSLLLLDEPFGALD---RAlrfdlQV-ELLH-LQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN- 254
Cdd:COG4172   161 QRQRVMIAMALANEPDLLIADEPTTALDvtvQA-----QIlDLLKdLQRELGMALLLITHDLGVVRRFADRVAVMRQGEi 235

                         250
                  ....*....|....*
gi 1582545954 255 VEQIDTPmTVYDRPK 269
Cdd:COG4172   236 VEQGPTA-ELFAAPQ 249
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
47-253 9.85e-42

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 148.30  E-value: 9.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGG---------QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--- 114
Cdd:PRK10419    4 LNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 115 --ARSRGVGMVFQNY--ALFPHLTVAENIAYPLA-CQKLPRAERKARVEEMLSLVRLKD-YGNRLPRELSGGQQQRVAVA 188
Cdd:PRK10419   84 rkAFRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK10419  164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 47-253 2.12e-41

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: 145.50  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAnVSARSRgVGMVFQN 126
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNR-IGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03269    79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582545954 207 LDRALRfDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03269   159 LDPVNV-ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
44-261 7.42e-41

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 152.63  E-value: 7.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGV 120
Cdd:COG1132   337 RGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQI 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFpHLTVAENIAYPlacqkLPRAERkARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVAR 189
Cdd:COG1132   417 GVVPQDTFLF-SGTIRENIRYG-----RPDATD-EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 190 AIAGRPSLLLLDEPFGALD--------RALRfdlqvELLHlqktlGITTLIVTHdqeeaqSL-----ANRLVLMNKGNVE 256
Cdd:COG1132   490 ALLKDPPILILDEATSALDtetealiqEALE-----RLMK-----GRTTIVIAH------RLstirnADRILVLDDGRIV 553


                  ....*
gi 1582545954 257 QIDTP 261
Cdd:COG1132   554 EQGTH 558
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
 47-277 1.66e-40

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


Pssm-ID: 132050 [Multi-domain]  Cd Length: 252  Bit Score: 144.59  E-value: 1.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-GDQ--------------DLA 111
Cdd:TIGR03005   1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQlyhmpgrngplvpaDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 112 NVSARSRGVGMVFQNYALFPHLTVAENIAY-PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARA 190
Cdd:TIGR03005  81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 191 IAGRPSLLLLDEPFGALDRalrfDLQVELLHLQKTLG----ITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYD 266
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDP----ELVGEVLNVIRRLAsehdLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236

                         250
                  ....*....|.
gi 1582545954 267 RPKTLFVNTFI 277
Cdd:TIGR03005 237 QPKEERTREFL 247
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
47-270 5.03e-39

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 140.74  E-value: 5.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGG---------QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSA 115
Cdd:COG4167     5 LEVRNLSKTFKYrtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 RSRGVGMVFQ--NYALFPHLTVAENIAYPLACQ-KLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAI 191
Cdd:COG4167    85 RCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARAL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKT 270
Cdd:COG4167   165 ILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQH 243
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
47-250 1.16e-38

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 145.16  E-value: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRGVGMV 123
Cdd:COG1129     5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAAGIAII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIA---YPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:COG1129    85 HQELNLVPNLSVAENIFlgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 201 DEPFGALDRAlrfdlQVELLH-----LqKTLGITTLIVTHDQEEAQSLANRLVLM 250
Cdd:COG1129   165 DEPTASLTER-----EVERLFriirrL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 47-253 1.39e-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: 136.40  E-value: 1.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRGVGMV 123
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASprdARRAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQnyalfphltvaeniayplacqklpraerkarveemlslvrlkdygnrlpreLSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:cd03216    81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 204 FGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03216   110 TAALTPAEVERL-FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
64-344 1.93e-38

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 141.55  E-value: 1.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA------NVSARSRGVGMVFQNYALFPHLTVAE 137
Cdd:PRK11144   16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEKRRIGYVFQDARLFPHYKVRG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLACQklpRAERKARVEEMLSLVRLKDygnRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQV 217
Cdd:PRK11144   96 NLRYGMAKS---MVAQFDKIVALLGIEPLLD---RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 218 ELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFIGQANLLNGTVLRLDAESTLI 297
Cdd:PRK11144  170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVLEHHPHYAMT 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 298 GLANDRTLLLPRRLNFTLGSKVTITFRPEEVRLSTQPSEST-----LPVRMT 344
Cdd:PRK11144  250 ALALGDQHLWVNKLDAPLGTALRIRIQASDVSLVLQPPQQSsirniLRAKVV 301
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 47-255 2.45e-38

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 139.86  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLaNVSARSRgVGmvfqn 126
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDRRR-IG----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 Y-----ALFPHLTVAENIAYpLACQK-LPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:COG4152    75 YlpeerGLYPKMKVGEQLVY-LARLKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 201 DEPFGALD---RALrfdLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG4152   154 DEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 61-269 3.50e-38

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 140.61  E-value: 3.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR-----GVGMVFQN--YALFPHL 133
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLAC--QKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRA 210
Cdd:PRK15079  116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 211 LRFDLqVELLH-LQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:PRK15079  196 IQAQV-VNLLQqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 61-271 6.35e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 138.61  E-value: 6.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA------NVSARSRGVGMVFQ--NYALFPH 132
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQfpEHQLFEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 133 lTVAENIAYPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PRK13634  102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 212 RFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13634  181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
41-280 7.90e-38

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 137.41  E-value: 7.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKrLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANV------- 113
Cdd:PRK10619    1 MSENK-LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 114 ---------SARSRgVGMVFQNYALFPHLTVAENI-AYPLACQKLPRAERKARVEEMLSLVRLKDYGN-RLPRELSGGQQ 182
Cdd:PRK10619   80 kvadknqlrLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 183 QRVAVARAIAGRPSLLLLDEPFGALDRalrfDLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQID 259
Cdd:PRK10619  159 QRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234

                         250       260
                  ....*....|....*....|.
gi 1582545954 260 TPMTVYDRPKTLFVNTFIGQA 280
Cdd:PRK10619  235 APEQLFGNPQSPRLQQFLKGS 255
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 46-257 9.36e-38

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: 143.74  E-value: 9.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNA--ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG--VG 121
Cdd:COG4618   330 RLSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIG 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHlTVAENIA-YPLA-CQKLPRAERKARVEEM-LSL-----VRLKDYGNRlpreLSGGQQQRVAVARAIAG 193
Cdd:COG4618   410 YLPQDVELFDG-TIAENIArFGDAdPEKVVAAAKLAGVHEMiLRLpdgydTRIGEGGAR----LSGGQRQRIGLARALYG 484

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 194 RPSLLLLDEPFGALD----RALrfdlqVELLHLQKTLGITTLIVTHDQeEAQSLANRLVLMNKGNVEQ 257
Cdd:COG4618   485 DPRLVVLDEPNSNLDdegeAAL-----AAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQA 546
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 44-268 1.20e-37

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 137.04  E-value: 1.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS----ARsRG 119
Cdd:PRK11300    3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiAR-MG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYALFPHLTVAENIaypLACQ-------------KLP---RAERKA--RVEEMLSLVRLKDYGNRLPRELSGGQ 181
Cdd:PRK11300   82 VVRTFQHVRLFREMTVIENL---LVAQhqqlktglfsgllKTPafrRAESEAldRAATWLERVGLLEHANRQAGNLAYGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 182 QQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:PRK11300  159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238


                  ....*..
gi 1582545954 262 MTVYDRP 268
Cdd:PRK11300  239 EEIRNNP 245
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 48-261 1.39e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 137.04  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGG--QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL--ANVSARSRGVGMV 123
Cdd:PRK13632    9 KVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKEIRKKIGII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNY-ALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:PRK13632   89 FQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTlGITTLI-VTHDQEEAqSLANRLVLMNKGNVEQIDTP 261
Cdd:PRK13632  169 STSMLDPKGKREIKKIMVDLRKT-RKKTLIsITHDMDEA-ILADKVIVFSEGKLIAQGKP 226
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
64-262 1.42e-37

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 136.10  E-value: 1.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA------RSRGVGMVFQNYALFPHLTVAE 137
Cdd:PRK11629   27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFTALE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDrALRFDLQV 217
Cdd:PRK11629  107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD-ARNADSIF 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1582545954 218 ELL-HLQKTLGITTLIVTHDQEEAQSLaNRLVLMNKGNVEQIDTPM 262
Cdd:PRK11629  186 QLLgELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSLM 230
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 46-261 1.55e-37

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: 142.98  E-value: 1.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--ARSRGVG 121
Cdd:COG4987   333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDedDLRRRIA 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFpHLTVAENIAypLACQKLPRAErkarVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARA 190
Cdd:COG4987   413 VVPQRPHLF-DTTLRENLR--LARPDATDEE----LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARA 485

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 191 IAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQsLANRLVLMNKGNVEQIDTP 261
Cdd:COG4987   486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTH 553
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 47-255 2.97e-37

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 133.11  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNA--ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG--VGM 122
Cdd:cd03246     1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHlTVAENIayplacqklpraerkarveemlslvrlkdygnrlpreLSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:cd03246    81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSlANRLVLMNKGNV 255
Cdd:cd03246   123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
47-264 2.91e-36

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 133.22  E-value: 2.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGvgmvfQN 126
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----RR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFP--HLT-----VAENIAY---P-LACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRP 195
Cdd:PRK11231   78 LALLPqhHLTpegitVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 196 SLLLLDEPFGALDralrFDLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:PRK11231  158 PVVLLDEPTTYLD----INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 61-269 4.75e-36

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 134.71  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN-----VSARSRGVGMVFQN-YA-LFPHL 133
Cdd:PRK11308   30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaQKLLRQKIQIVFQNpYGsLNPRK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLACQ-KLPRAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PRK11308  110 KVGQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 212 RFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:PRK11308  190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 47-316 1.76e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 131.74  E-value: 1.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL-----ANVSARSRgV 120
Cdd:PRK13639    2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVRKT-V 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNY--ALFPHlTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK13639   81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 199 LLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTlfvntfIG 278
Cdd:PRK13639  160 VLDEPTSGLDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET------IR 232

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1582545954 279 QANllngtvLRLDAESTLIGLANDRTlLLPRRLNFTLG 316
Cdd:PRK13639  233 KAN------LRLPRVAHLIEILNKED-NLPIKMGYTIG 263
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 47-260 2.12e-35

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: 130.43  E-value: 2.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGG--QNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGM 122
Cdd:cd03251     1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFpHLTVAENIAYplacqKLPRAERkARVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQRVAVARAI 191
Cdd:cd03251    81 VSQDVFLF-NDTVAENIAY-----GRPGATR-EEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDT 260
Cdd:cd03251   154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 42-250 2.18e-35

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: 136.65  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  42 AERKRLSVQGLTHSYGGQ-NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--R 118
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrD 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHlTVAENIAypLACQKLPRAErkarVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAV 187
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIR--LARPDASDAE----IREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 188 ARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQsLANRLVLM 250
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
49-245 2.92e-35

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 131.04  E-value: 2.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSaRSR------GVGM 122
Cdd:PRK11831   10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMS-RSRlytvrkRMSM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAYPL-ACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:PRK11831   89 LFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 202 EPFGALDrALRFDLQVELL-HLQKTLGITTLIVTHDQEEAQSLAN 245
Cdd:PRK11831  169 EPFVGQD-PITMGVLVKLIsELNSALGVTCVVVSHDVPEVLSIAD 212
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
57-255 3.88e-35

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 129.22  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  57 GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS-----RGVGMVFQNYALFP 131
Cdd:PRK10908   13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLM 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PRK10908   93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1582545954 212 RFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK10908  173 SEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 61-271 4.94e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 130.26  E-value: 4.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ--DLANVSARSRGVGMVFQN-YALFPHLTVAE 137
Cdd:PRK13648   24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaiTDDNFEKLRKHIGIVFQNpDNQFVGSIVKY 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQV 217
Cdd:PRK13648  104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 218 ELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13648  184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 61-255 6.50e-35

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 129.82  E-value: 6.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA--RSRGVGMVFQNYAL--FPHLTVA 136
Cdd:COG1101    21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykRAKYIGRVFQDPMMgtAPSMTIE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 137 ENIAypLACQK-----LPRA---ERKARVEEMLSLVRLkdyG--NRLPRE---LSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:COG1101   101 ENLA--LAYRRgkrrgLRRGltkKRRELFRELLATLGL---GleNRLDTKvglLSGGQRQALSLLMATLTKPKLLLLDEH 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 204 FGALD--RALRfdlqveLLHLQKTL----GITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG1101   176 TAALDpkTAAL------VLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 46-253 1.99e-34

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 127.32  E-value: 1.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQ--NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRGVG 121
Cdd:cd03245     2 RIEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFpHLTVAENIAYplacqKLPRAErKARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARA 190
Cdd:cd03245    82 YVPQDVTLF-YGTLRDNITL-----GAPLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 191 IAGRPSLLLLDEPFGALDRAlrfdLQVELLH-LQKTL-GITTLIVTHDQeEAQSLANRLVLMNKG 253
Cdd:cd03245   155 LLNDPPILLLDEPTSAMDMN----SEERLKErLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSG 214
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 46-253 2.28e-34

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 133.23  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRGVGM 122
Cdd:COG3845     5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprdAIALGIGM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAY---PLACQKLPRAERKARVEEmLSlvrlKDYG-----NRLPRELSGGQQQRVAVARAIAGR 194
Cdd:COG3845    85 VHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRE-LS----ERYGldvdpDAKVEDLSVGEQQRVEILKALYRG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 195 PSLLLLDEP------------FGALdRALrfdlqvellhlqKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:COG3845   160 ARILILDEPtavltpqeadelFEIL-RRL------------AAEGKSIIFITHKLREVMAIADRVTVLRRG 217
cbiO PRK13640
energy-coupling factor transporter ATPase;
61-271 4.48e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 127.99  E-value: 4.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGR--------IELGDQDLANVSARsrgVGMVFQNY-ALFP 131
Cdd:PRK13640   22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIREK---VGIVFQNPdNQFV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PRK13640   99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 212 RFDLQVELLHLQKTLGITTLIVTHDQEEAqSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13640  179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 46-264 5.95e-34

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 126.55  E-value: 5.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQD--LANVSARS-RGVGM 122
Cdd:PRK10895    3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARArRGIGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHLTVAENIAYPLACQK-LPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:PRK10895   83 LPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:PRK10895  163 EPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 48-266 1.08e-33

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 126.35  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR--SRGVGMVFQ 125
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelAKRLAILRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIA---YPlACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:COG4604    83 ENHINSRLTVRELVAfgrFP-YSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 203 PFGALD--------RALRfdlqvellHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP---MT------VY 265
Cdd:COG4604   162 PLNNLDmkhsvqmmKLLR--------RLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPeeiITpevlsdIY 233


                  .
gi 1582545954 266 D 266
Cdd:COG4604   234 D 234
cbiO PRK13642
energy-coupling factor transporter ATPase;
45-265 1.18e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 126.75  E-value: 1.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLTHSYGGQ---NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRG 119
Cdd:PRK13642    3 KILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNY-ALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK13642   83 IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTPMTVY 265
Cdd:PRK13642  163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 44-257 1.26e-33

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: 132.15  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RG 119
Cdd:TIGR02203 328 RGDVEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQ 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYALFPHlTVAENIAYplacqKLPRAERKARVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQRVAVA 188
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIA 481

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQSlANRLVLMNKGN-VEQ 257
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRiVER 548
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 41-251 1.46e-33

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 125.28  E-value: 1.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSYG-GQNAIS---DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA- 115
Cdd:PRK10584    1 MPAENIVEVHHLKKSVGqGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 -----RSRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARA 190
Cdd:PRK10584   81 araklRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 191 IAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMN 251
Cdd:PRK10584  161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
47-255 7.25e-33

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 130.61  E-value: 7.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAIS---DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA------R 116
Cdd:PRK10535    5 LELKDIRRSYpSGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPS 196
Cdd:PRK10535   85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 197 LLLLDEPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSlANRLVLMNKGNV 255
Cdd:PRK10535  165 VILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
61-271 1.46e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 124.04  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS----ARSRGvGMVFQNyalfPH---- 132
Cdd:PRK13633   25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdIRNKA-GMVFQN----PDnqiv 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 133 -LTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PRK13633  100 aTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 212 RFDLQVELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13633  180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 47-268 2.16e-32

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 122.73  E-value: 2.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-----GDQDLANVS-ARSRGV 120
Cdd:PRK11701    7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSeAERRRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 -----GMVFQNYA--LFPHLTVAENIAYPL--------------ACQKLpraerkARVEemLSLVRLKDygnrLPRELSG 179
Cdd:PRK11701   87 lrtewGFVHQHPRdgLRMQVSAGGNIGERLmavgarhygdiratAGDWL------ERVE--IDAARIDD----LPTTFSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 180 GQQQRVAVARAIAGRPSLLLLDEPFGALD---RALRFDLqveLLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVe 256
Cdd:PRK11701  155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvQARLLDL---LRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV- 230

                         250
                  ....*....|....
gi 1582545954 257 qIDTPMT--VYDRP 268
Cdd:PRK11701  231 -VESGLTdqVLDDP 243
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 47-253 3.30e-32

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: 121.39  E-value: 3.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLT-----HSYGGQ--NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ----DLANVSA 115
Cdd:COG4778     5 LEVENLSktftlHLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 ------RSRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSlvRLkdygnRLPREL--------SGGQ 181
Cdd:COG4778    85 reilalRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLA--RL-----NLPERLwdlppatfSGGE 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 182 QQRVAVARAIAGRPSLLLLDEPFGALDRALRfDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:COG4778   158 QQRVNIARGFIADPPLLLLDEPTASLDAANR-AVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 44-253 9.44e-32

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 118.69  E-value: 9.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLThsygGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRGV 120
Cdd:cd03215     2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdAIRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMV---FQNYALFPHLTVAENIAyplacqklpraerkarveemlslvrlkdygnrLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:cd03215    78 AYVpedRKREGLVLDLSVAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRV 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 198 LLLDEPFGALDRALRFDLQvELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03215   126 LILDEPTRGVDVGAKAEIY-RLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 18-269 1.26e-31

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 126.89  E-value: 1.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  18 PETAQQSVTstqnQGGPMLGIPNMAERKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQ 97
Cdd:PRK10261  300 PPIEQDTVV----DGEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  98 PKNGRIELGDQDLANVSARS-----RGVGMVFQN-YA-LFPHLTVAENIAYPLACQKLPRAERKA-RVEEMLSLVRLK-D 168
Cdd:PRK10261  376 SQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLpE 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 169 YGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLV 248
Cdd:PRK10261  456 HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVA 535

                         250       260
                  ....*....|....*....|.
gi 1582545954 249 LMNKGNVEQIDTPMTVYDRPK 269
Cdd:PRK10261  536 VMYLGQIVEIGPRRAVFENPQ 556
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
55-250 1.49e-31

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 118.49  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElgdqdlanvSARSRGVGMVFQNYAL---FP 131
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 hLTVAENIAY----PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:NF040873   72 -LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1582545954 208 DRALRFDLQVELLHLQKTlGITTLIVTHDQEEAqSLANRLVLM 250
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 61-259 1.52e-31

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: 119.56  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqdlanvsaRSRGVGMVFQNYALFPHLTVAENIA 140
Cdd:cd03220    37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSLLGLGGGFNPELTGRENIY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 141 YPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELL 220
Cdd:cd03220   107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582545954 221 HLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQID 259
Cdd:cd03220   187 ELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 51-255 1.80e-31

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: 126.52  E-value: 1.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  51 GLTHSYGGQ--NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRGVGMVFQN 126
Cdd:TIGR03375 468 NVSFAYPGQetPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPADLRRNIGYVPQD 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFpHLTVAENIAY--PLAC-QKLPRAERKARVEEmlsLVRLKDYGNRLP-----RELSGGQQQRVAVARAIAGRPSLL 198
Cdd:TIGR03375 548 PRLF-YGTLRDNIALgaPYADdEEILRAAELAGVTE---FVRRHPDGLDMQigergRSLSGGQRQAVALARALLRDPPIL 623

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 199 LLDEPFGALDRALRFDLqveLLHLQKTL-GITTLIVTHDQeEAQSLANRLVLMNKGNV 255
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERF---KDRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 56-269 3.76e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 119.56  E-value: 3.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  56 YGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQ-PKNGRIElGDQDLANVSARS---------RGVGMVFQ 125
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElNEEARVE-GEVRLFGRNIYSpdvdpievrREVGMVFQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKL--PRAERKARVEEMLSLVRL----KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:PRK14267   93 YPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 200 LDEPFGALDRALRFDLQVELLHLQKTLgiTTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:PRK14267  173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 47-271 1.10e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 118.75  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL--ANVSARSRGVGMV 123
Cdd:PRK13652    4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNY--ALFPHlTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:PRK13652   84 FQNPddQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13652  163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
51-253 1.17e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 120.32  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  51 GLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIE-LGDQDLANVSARSRGVGMVFQNYAL 129
Cdd:PRK13536   46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPARARLARARIGVVPQFDNL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 130 FPHLTVAEN-IAYPLACQKLPRaERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:PRK13536  126 DLEFTVRENlLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 209 RALRfDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK13536  205 PHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 47-255 1.71e-30

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: 117.49  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQP-KNGRIELGDQDLANVSA---RSRgVGM 122
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVwelRKR-IGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 V---FQNYaLFPHLTVAENIA---------YplacqKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARA 190
Cdd:COG1119    83 VspaLQLR-FPRDETVLDVVLsgffdsiglY-----REPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 191 IAGRPSLLLLDEPFGALDRALRFDLqVELL-HLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG1119   157 LVKDPELLILDEPTAGLDLGARELL-LALLdKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 61-264 2.25e-30

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: 122.22  E-value: 2.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIE--LGDQ--DLANVSARSRG-----VGMVFQNYALFP 131
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEwvDMTKPGPDGRGrakryIGILHQEYDLYP 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HLTVAENIAYPLACQkLPR--AERKArveemlsLVRLKDYG----------NRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:TIGR03269 379 HRTVLDNLTEAIGLE-LPDelARMKA-------VITLKMVGfdeekaeeilDKYPDELSEGERHRVALAQVLIKEPRIVI 450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 200 LDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 44-269 2.41e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 117.32  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQ--PK---NGRIELGDQDL--ANVSAR 116
Cdd:PRK14247    1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIfkMDVIEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNYALFPHLTVAENIAYPLACQKL--PRAERKARVEEMLSLVRLKD-YGNRL---PRELSGGQQQRVAVARA 190
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDeVKDRLdapAGKLSGGQQQRLCIARA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 191 IAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGIttLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:PRK14247  161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 58-235 3.61e-30

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: 116.18  E-value: 3.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  58 GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFpHLTV 135
Cdd:cd03253    13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVLF-NDTI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIAY--PLAC-QKLPRAERKARVEEmlSLVRLKD-Y----GNRLPReLSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:cd03253    92 GYNIRYgrPDATdEEVIEAAKAAQIHD--KIMRFPDgYdtivGERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSAL 168

                         170       180
                  ....*....|....*....|....*...
gi 1582545954 208 DRALRFDLQVELLHLQKtlGITTLIVTH 235
Cdd:cd03253   169 DTHTEREIQAALRDVSK--GRTTIVIAH 194
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 61-269 4.83e-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: 115.93  E-value: 4.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK----NGRIELGDQDLANVSARSRGVGMVFQN--YALFPHLT 134
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRL---PRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:TIGR02770  81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 212 RFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPK 218
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 47-274 7.10e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 116.03  E-value: 7.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAI--AGLIQPK---NGRIELGDQDLAN-----VSAR 116
Cdd:PRK14239    6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSprtdtVDLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 sRGVGMVFQNYALFPhLTVAENIAYPLacqKLPRAERKARVEEML--SLV------RLKDYGNRLPRELSGGQQQRVAVA 188
Cdd:PRK14239   86 -KEIGMVFQQPNPFP-MSIYENVVYGL---RLKGIKDKQVLDEAVekSLKgasiwdEVKDRLHDSALGLSGGQQQRVCIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLgiTTLIVTHDQEEAQSLANRLVLMNKGNVEQidtpmtvYDRP 268
Cdd:PRK14239  161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIE-------YNDT 231


                  ....*.
gi 1582545954 269 KTLFVN 274
Cdd:PRK14239  232 KQMFMN 237
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
47-253 9.48e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 116.83  E-value: 9.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRG-VGMVFQ 125
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:PRK13537   88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1582545954 206 ALDRALRfDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK13537  168 GLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 64-235 1.99e-29

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: 114.17  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTvlraIAGLIQ----PKNGRIELGDQDLA--NVSARSRGVGMVFQNYALFPhLTVAE 137
Cdd:cd03249    21 GLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDIRdlNLRWLRSQIGLVSQEPVLFD-GTIAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLACQKLPRAERKARVEEMLSLVR-LKDYGNRL--PR--ELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRalr 212
Cdd:cd03249    96 NIRYGKPDATDEEVEEAAKKANIHDFIMsLPDGYDTLvgERgsQLSGGQKQRIAIARALLRNPKILLLDEATSALDA--- 172

                         170       180
                  ....*....|....*....|....*...
gi 1582545954 213 fdlQVELLhLQKTL-----GITTLIVTH 235
Cdd:cd03249   173 ---ESEKL-VQEALdramkGRTTIVIAH 196
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 46-243 2.13e-29

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 113.43  E-value: 2.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL--GDQDLANVSARSRGVGmv 123
Cdd:PRK13539    2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACHYLG-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNyALFPHLTVAENIAYPLACqklpRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVAR-AIAGRPsLLLLDE 202
Cdd:PRK13539   80 HRN-AMKPALTVAENLEFWAAF----LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARlLVSNRP-IWILDE 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 203 PFGALDRAlrfdlQVELL------HLQKtlGITTLIVTH---DQEEAQSL 243
Cdd:PRK13539  154 PTAALDAA-----AVALFaeliraHLAQ--GGIVIAATHiplGLPGAREL 196
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 47-269 2.58e-29

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


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 114.54  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS------ARSRGV 120
Cdd:TIGR02323   4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlseAERRRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 -----GMVFQNYA--LFPHLTVAENIA-YPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAI 191
Cdd:TIGR02323  84 mrtewGFVHQNPRdgLRMRVSAGANIGeRLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 62-277 3.93e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 113.99  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ------DLANVSA--RSRGVGMVFQNYALFPHL 133
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikLRKEVGMVFQQPNPFPHL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLACQKLP-RAERKARVEEMLSLVRL-KDYGNRL---PRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:PRK14246  106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 209 RALRFDLQVELLHLQKTlgITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTLFVNTFI 277
Cdd:PRK14246  186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 47-274 4.15e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 113.98  E-value: 4.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKN-----GRIELGDQDL----ANVSARS 117
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNYALFPhLTVAENIAYPLacqKL----PRAERKARVEEMLSLVRLKD-YGNRLPR---ELSGGQQQRVAVAR 189
Cdd:PRK14258   88 RQVSMVHPKPNLFP-MSVYDNVAYGV---KIvgwrPKLEIDDIVESALKDADLWDeIKHKIHKsalDLSGGQQQRLCIAR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 190 AIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMnKGNVEQIdTPMTVYDRPK 269
Cdd:PRK14258  164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFF-KGNENRI-GQLVEFGLTK 241


                  ....*
gi 1582545954 270 TLFVN 274
Cdd:PRK14258  242 KIFNS 246
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
47-255 4.64e-29

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 113.95  E-value: 4.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLI---QPKNGRIEL------GDQDLANVSARS 117
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELlgrtvqREGRLARDIRKS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RG-VGMVFQNYALFPHLTVAENI------AYPL--ACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVA 188
Cdd:PRK09984   85 RAnTGYIFQQFNLVNRLSVLENVligalgSTPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK09984  165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 49-255 9.51e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 113.29  E-value: 9.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRgVGMVF 124
Cdd:PRK13647    7 VEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwVRSK-VGLVF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNY--ALFPhLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDE 202
Cdd:PRK13647   86 QDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 203 PFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK13647  165 PMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 34-255 1.11e-28

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 117.83  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  34 PMLGIPNmaERKRLSVQGLTHSYGGQNA--ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA 111
Cdd:TIGR01842 306 PAMPLPE--PEGHLSVENVTIVPPGGKKptLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 112 NVSARSRG--VGMVFQNYALFPHlTVAENIAY---PLACQKLPRAERKARVEEMLSlvrlkdygnRLPR----------- 175
Cdd:TIGR01842 384 QWDRETFGkhIGYLPQDVELFPG-TVAENIARfgeNADPEKIIEAAKLAGVHELIL---------RLPDgydtvigpgga 453

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 176 ELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTlGITTLIVTHdQEEAQSLANRLVLMNKGNV 255
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRI 531
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 42-235 1.23e-28

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 117.60  E-value: 1.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  42 AERKRLSVQGLT-HSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIelgdqdlanvsARSRGV 120
Cdd:COG4178   358 SEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-----------ARPAGA 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVF---QNYalFPHLTVAENIAYPLACQKLPRAErkarVEEMLSLVRLKDYGNRL------PRELSGGQQQRVAVARAI 191
Cdd:COG4178   427 RVLFlpqRPY--LPLGTLREALLYPATAEAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLL 500

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLqveLLHLQKTLGITTLI-VTH 235
Cdd:COG4178   501 LHKPDWLFLDEATSALDEENEAAL---YQLLREELPGTTVIsVGH 542
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 47-235 1.27e-28

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 110.91  E-value: 1.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA-RSRGVGMVFQ 125
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYplaCQKLPRAERKArVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:TIGR01189  81 LPGLKPELSALENLHF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1582545954 206 ALDRAlrfdlQVELL------HLQKtlGITTLIVTH 235
Cdd:TIGR01189 157 ALDKA-----GVALLagllraHLAR--GGIVLLTTH 185
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 47-264 1.50e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 115.71  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR--SRGVGMVF 124
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaaSRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYAL---FPHLTVAENIAYPLACQKLPRAER-KARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:PRK09536   84 QDTSLsfeFDVRQVVEMGRTPHRSRFDTWTETdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 201 DEPFGALDralrFDLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:PRK09536  164 DEPTASLD----INHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 62-255 1.55e-28

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: 111.59  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQP---KNGRIelgdqdLANVSARSRG-----VGMVFQNYALFPHL 133
Cdd:cd03234    23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQI------LFNGQPRKPDqfqkcVAYVRQDDILLPGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLACqKLPR----AERKARVEEM-LSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:cd03234    97 TVRETLTYTAIL-RLPRkssdAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582545954 209 RALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03234   176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
cbiO PRK13645
energy-coupling factor transporter ATPase;
61-271 1.60e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 113.18  E-value: 1.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGD-------QDLANVSARSRGVGMVFQ--NYALFP 131
Cdd:PRK13645   26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HlTVAENIAYPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRA 210
Cdd:PRK13645  106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 211 LRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13645  185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 61-253 1.83e-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: 111.66  E-value: 1.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQD-LANVSARSRGVGMVF-QNYALFPHLTVAEN 138
Cdd:cd03267    36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLRRIGVVFgQKTQLWWDLPVIDS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 139 IAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVE 218
Cdd:cd03267   116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1582545954 219 LLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03267   196 LKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 47-274 5.20e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 111.03  E-value: 5.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRA---IAGLIQP--KNGRI-----ELGDQDLANVSAR 116
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVtfhgkNLYAPDVDPVEVR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRgVGMVFQNYALFPHlTVAENIAYPlacqklPR-----------AERKARVEEMLSLVR--LKDYGnrlpRELSGGQQQ 183
Cdd:PRK14243   91 RR-IGMVFQKPNPFPK-SIYDNIAYG------ARingykgdmdelVERSLRQAALWDEVKdkLKQSG----LSLSGGQQQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 184 RVAVARAIAGRPSLLLLDEPFGALD--RALRFDlqvELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMnkgNVEQIDTP 261
Cdd:PRK14243  159 RLCIARAIAVQPEVILMDEPCSALDpiSTLRIE---ELMHELKE-QYTIIIVTHNMQQAARVSDMTAFF---NVELTEGG 231

                         250
                  ....*....|....*...
gi 1582545954 262 -----MTVYDRPKTLFVN 274
Cdd:PRK14243  232 grygyLVEFDRTEKIFNS 249
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 46-236 1.42e-27

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 114.38  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQN-AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--ARSRGVGM 122
Cdd:TIGR02868 334 TLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFpHLTVAENIAypLACQKLPRAErkarVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARAI 191
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLR--LARPDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLqVELLhLQKTLGITTLIVTHD 236
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADEL-LEDL-LAALSGRTVVLITHH 529
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 62-255 1.61e-27

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 108.02  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK--NGRIELGDQDLANVSARSRgVGMVFQNYALFPHLTVAENI 139
Cdd:cd03213    25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 140 AYPLACqklpraerkarveemlslvrlkdygnrlpRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVEL 219
Cdd:cd03213   104 MFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1582545954 220 LHLQKTlGITTLIVTHD-QEEAQSLANRLVLMNKGNV 255
Cdd:cd03213   155 RRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 61-267 2.16e-27

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 109.02  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqdlanvsaRSR-----GVGMVFQnyalfPHLTV 135
Cdd:COG1134    41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------NGRvsallELGAGFH-----PELTG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNrLP-RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFD 214
Cdd:COG1134   106 RENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 215 LQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDR 267
Cdd:COG1134   185 CLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
cbiO PRK13643
energy-coupling factor transporter ATPase;
61-265 3.30e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 109.82  E-value: 3.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS------RGVGMVFQ--NYALFPH 132
Cdd:PRK13643   21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQfpESQLFEE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 133 lTVAENIAYPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PRK13643  101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 212 RFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVY 265
Cdd:PRK13643  180 RIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 47-255 5.02e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 109.17  E-value: 5.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYG-GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLaNVSARS-----RGV 120
Cdd:PRK13636    6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQ--NYALFPhLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK13636   85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK13636  164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
cbiO PRK13649
energy-coupling factor transporter ATPase;
61-265 1.45e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 107.52  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS------RGVGMVFQnyalFPHL- 133
Cdd:PRK13649   22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirKKVGLVFQ----FPESq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 ----TVAENIAYPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:PRK13649   98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 209 RALRfdlqVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVY 265
Cdd:PRK13649  178 PKGR----KELMTLFKKLhqsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 47-269 1.48e-26

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 108.68  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQ-PknGRI-----ELGDQDLANVSAR 116
Cdd:PRK11022    4 LNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklEFNGQDLQRISEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SR------GVGMVFQN--YALFPHLTVAENIAYPLAC-QKLPRAERKARVEEMLSLVRLKDYGNRL---PRELSGGQQQR 184
Cdd:PRK11022   82 ERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 185 VAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:PRK11022  162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241


                  ....*
gi 1582545954 265 YDRPK 269
Cdd:PRK11022  242 FRAPR 246
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
46-253 1.98e-26

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 110.88  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHsyggQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRGVGM 122
Cdd:COG1129   256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdAIRAGIAY 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQN---YALFPHLTVAENIAypLACQK-------LPRAERKARVEEMLSLVRLKDYGNRLP-RELSGGQQQRVAVARAI 191
Cdd:COG1129   332 VPEDrkgEGLVLDLSIRENIT--LASLDrlsrgglLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWL 409

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 192 AGRPSLLLLDEPF-----GAldralrfdlQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:COG1129   410 ATDPKVLILDEPTrgidvGA---------KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREG 470
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 41-257 2.75e-26

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 105.57  E-value: 2.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKR-LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--ARS 117
Cdd:PRK10247    1 MQENSPlLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGVGMVFQNYALFPHlTVAENIAYPLACqklpraeRKARVEEMLSLVRLKDYGnrLPR--------ELSGGQQQRVAVAR 189
Cdd:PRK10247   81 QQVSYCAQTPTLFGD-TVYDNLIFPWQI-------RNQQPDPAIFLDDLERFA--LPDtiltkniaELSGGEKQRISLIR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 190 AIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:PRK10247  151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQ 218
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 60-255 2.90e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 107.48  E-value: 2.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  60 NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQD--------------------------LANV 113
Cdd:PRK13651   21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkkIKKI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 114 SARSRGVGMVFQ--NYALFPHlTVAENIAYPLACQKLPRAERKARVEEMLSLVRL-KDYGNRLPRELSGGQQQRVAVARA 190
Cdd:PRK13651  101 KEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 191 IAGRPSLLLLDEPFGALDRAlrfdLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK13651  180 LAMEPDFLVFDEPTAGLDPQ----GVKEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
cbiO PRK13641
energy-coupling factor transporter ATPase;
62-271 3.22e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 106.84  E-value: 3.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-GDQDLANVSARS-----RGVGMVFQnyalFPHL-- 133
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGNKNlkklrKKVSLVFQ----FPEAql 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 ---TVAENIAY-PLacqKLPRAERKARVE--EMLSLVRLK-DYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:PRK13641   99 fenTVLKDVEFgPK---NFGFSEDEAKEKalKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 207 LDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13641  176 LDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 55-235 3.38e-26

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: 110.68  E-value: 3.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNAI-SDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFp 131
Cdd:COG5265   366 GYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF- 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HLTVAENIAY--PLAcqklPRAErkarVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQRVAVARAIAGRPSLL 198
Cdd:COG5265   445 NDTIAYNIAYgrPDA----SEEE----VEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPIL 516

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTH 235
Cdd:COG5265   517 IFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH 551
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 55-235 4.03e-26

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: 105.00  E-value: 4.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQN-AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFP 131
Cdd:cd03254    11 SYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HlTVAENIAY--PLAcqklpraeRKARVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQRVAVARAIAGRPSLL 198
Cdd:cd03254    91 G-TIMENIRLgrPNA--------TDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKIL 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTH 235
Cdd:cd03254   162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH 196
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 50-257 4.24e-26

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 110.18  E-value: 4.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSYGGQN-AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKnGRIELGDQDLANVSARS-----RGVGMV 123
Cdd:PRK15134  289 KGILKRTVDHNvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQllpvrHRIQVV 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQ--NYALFPHLTVAENIAYPLACQK--LPRAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK15134  368 FQdpNSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV-EQ 257
Cdd:PRK15134  448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVvEQ 507
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 47-265 6.92e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 106.47  E-value: 6.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN-----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGD-------------- 107
Cdd:PRK13631   22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelit 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 108 ----QDLANVSARSRGVGMVFQ--NYALFPHlTVAENIAY-PLACqKLPRAERKARVEEMLSLVRLKD-YGNRLPRELSG 179
Cdd:PRK13631  102 npysKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 180 GQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQID 259
Cdd:PRK13631  180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258


                  ....*.
gi 1582545954 260 TPMTVY 265
Cdd:PRK13631  259 TPYEIF 264
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 49-236 1.01e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 109.00  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElgdqdlanvsaRSRG--VGMVFQN 126
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-----------IPKGlrIGYLPQE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAYPLA-----CQKLPRAERK---------------------------ARVEEMLSLVRLK-DYGNRL 173
Cdd:COG0488    70 PPLDDDLTVLDTVLDGDAelralEAELEELEAKlaepdedlerlaelqeefealggweaeARAEEILSGLGFPeEDLDRP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 174 PRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD-RALRFdLQVELLHLQKTLgittLIVTHD 236
Cdd:COG0488   150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDlESIEW-LEEFLKNYPGTV----LVVSHD 208
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 58-257 2.19e-25

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: 103.33  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  58 GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFpHLTV 135
Cdd:cd03252    14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlrRQVGVVLQENVLF-NRSI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIAypLACQKLPRaerkARVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQRVAVARAIAGRPSLLLLDEPF 204
Cdd:cd03252    93 RDNIA--LADPGMSM----ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEAT 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 205 GALDRALRFDLQVELLHLQKtlGITTLIVTHDQEEAQSlANRLVLMNKGN-VEQ 257
Cdd:cd03252   167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRiVEQ 217
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 46-253 3.65e-25

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 107.03  E-value: 3.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLT-HSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR---GVG 121
Cdd:COG3845   257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVA 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MV---FQNYALFPHLTVAENIA------YPLAcqKLPRAERKARVEEMLSLVrlKDYGNRLP------RELSGGQQQRVA 186
Cdd:COG3845   337 YIpedRLGRGLVPDMSVAENLIlgryrrPPFS--RGGFLDRKAIRAFAEELI--EEFDVRTPgpdtpaRSLSGGNQQKVI 412

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 187 VARAIAGRPSLLLLDEP-----FGAldralrfdlqVELLHlqKTL------GITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:COG3845   413 LARELSRDPKLLIAAQPtrgldVGA----------IEFIH--QRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEG 478
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 47-267 1.09e-24

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: 106.04  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGL--IQPKNGRI--------------------- 103
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 104 ---------ELGDQDLANVSA------RSRGVGMVFQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKD 168
Cdd:TIGR03269  81 pcpvcggtlEPEEVDFWNLSDklrrriRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 169 YGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLV 248
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250
                  ....*....|....*....
gi 1582545954 249 LMNKGNVEQIDTPMTVYDR 267
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAV 259
cbiO PRK13644
energy-coupling factor transporter ATPase;
47-268 1.23e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 101.99  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS---RGVGM 122
Cdd:PRK13644    2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQN-YALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:PRK13644   82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 202 EPFGALDRalrfDLQVELLHLQKTL---GITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTPMTVYDRP 268
Cdd:PRK13644  162 EVTSMLDP----DSGIAVLERIKKLhekGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
46-255 1.41e-24

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 101.99  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR--SRGVGMV 123
Cdd:PRK10253    7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevARRIGLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIA---YPLacQKLP---RAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:PRK10253   87 AQNATTPGDITVQELVArgrYPH--QPLFtrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 198 LLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK10253  165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 60-266 1.91e-24

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 102.47  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  60 NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIE-LG----DQDLANVsarsRGVGMVF-QNYALFPHL 133
Cdd:COG4586    36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpfKRRKEFA----RRIGVVFgQRSQLWWDL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD----R 209
Cdd:COG4586   112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvskE 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 210 ALR-FdlqveLLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVeqidtpmtVYD 266
Cdd:COG4586   192 AIReF-----LKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI--------IYD 236
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
60-255 2.25e-24

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 101.40  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  60 NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLA--NVSARSRGVGMVFQN--YALFPHLTV 135
Cdd:PRK15112   27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIAYPLACQ-KLPRAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRF 213
Cdd:PRK15112  107 SQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 214 DLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK15112  187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
50-261 2.44e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 105.59  E-value: 2.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ--DLANVSARSRgVGMVFQNY 127
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATRRR-VGYMSQAF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 ALFPHLTVAENIAypLACQ--KLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:NF033858  349 SLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 206 ALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQsLANRLVLMNKGNVEQIDTP 261
Cdd:NF033858  427 GVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTP 481
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 58-262 4.95e-24

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: 105.10  E-value: 4.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   58 GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL-ANVSARSRGVGMVFQNYALFPHLTVA 136
Cdd:TIGR01257  942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVA 1021

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  137 ENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQ 216
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1582545954  217 VELLHLQKtlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPM 262
Cdd:TIGR01257 1102 DLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
cbiO PRK13646
energy-coupling factor transporter ATPase;
61-271 2.57e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 98.70  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSA-------RSRgVGMVFQnyalFPHL 133
Cdd:PRK13646   22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvRKR-IGMVFQ----FPES 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 -----TVAENIAYPLACQKLPRAERKARVEEML-SLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:PRK13646   97 qlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 208 DRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTL 271
Cdd:PRK13646  177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 47-256 2.91e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 101.68  E-value: 2.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDqdlaNVSarsrgVGMVFQN 126
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE----TVK-----IGYFDQH 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALF-PHLTVAENIAYplACQKLPRAERKARVEEML-SlvrlKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP- 203
Cdd:COG0488   387 QEELdPDKTVLDELRD--GAPGGTEQEVRGYLGRFLfS----GDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPt 460

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 204 -------FGALDRALR-FDlqvellhlqktlGiTTLIVTHDQEEAQSLANRLVLMNKGNVE 256
Cdd:COG0488   461 nhldietLEALEEALDdFP------------G-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 47-253 1.17e-22

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: 92.90  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDqdlanvsarsrgvgmvfqn 126
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 yalfphltvAENIAYplacqkLPRaerkarveemlslvrlkdygnrlpreLSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:cd03221    62 ---------TVKIGY------FEQ--------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582545954 207 LDRALRFDLQVELLHLQKTLgittLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:cd03221   101 LDLESIEALEEALKEYPGTV----ILVSHDRYFLDQVATKIIELEDG 143
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 47-256 2.34e-22

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 93.15  E-value: 2.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS-ARSRGVGMV 123
Cdd:cd03247     1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkALSSLISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNyalfPHL---TVAENIAyplacqklpraerkarveemlslvrlkdygnrlpRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:cd03247    81 NQR----PYLfdtTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLL 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 201 DEPFGALDRalRFDLQVELLHLQKTLGITTLIVTHdQEEAQSLANRLVLMNKGNVE 256
Cdd:cd03247   123 DEPTVGLDP--ITERQLLSLIFEVLKDKTLIWITH-HLTGIEHMDKILFLENGKII 175
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 65-255 2.72e-22

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 94.91  E-value: 2.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  65 VAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIqPKNGRIELGDQDLANVS----ARSRGV---------GM-VFQNYALF 130
Cdd:COG4138    15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSaaelARHRAYlsqqqsppfAMpVFQYLALH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 131 PHltvaeniayplacQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAI---------AGRpsLLLLD 201
Cdd:COG4138    94 QP-------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinpEGQ--LLLLD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 202 EPFGALDRA--LRFDLQVELLHLQktlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:COG4138   159 EPMNSLDVAqqAALDRLLRELCQQ---GITVVMSSHDLNHTLRHADRVWLLKQGKL 211
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 47-210 2.73e-22

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: 93.71  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR-SRGVGMVFQ 125
Cdd:cd03231     1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYplacqkLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:cd03231    81 APGIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154


                  ....*
gi 1582545954 206 ALDRA 210
Cdd:cd03231   155 ALDKA 159
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 47-269 4.48e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 95.16  E-value: 4.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQP-----KNGRIELGDQDLAN---VSARSR 118
Cdd:PRK14271   22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNyrdVLEFRR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPhLTVAENIAYPLACQKL-PRAERKARVEEMLSLVRL----KDYGNRLPRELSGGQQQRVAVARAIAG 193
Cdd:PRK14271  102 RVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAV 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 194 RPSLLLLDEPFGALDRALRFDLQVELLHLQKTLgiTTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:PRK14271  181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 64-268 5.31e-22

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 98.26  E-value: 5.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFPHlTVAENIAY 141
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlhRQVALVGQEPVLFSG-SVRENIAY 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 142 PLacqklpraeRKARVEEMLSLVRL---KDYGNRLPR-----------ELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:TIGR00958 578 GL---------TDTPDEEIMAAAKAanaHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 208 DRALRFDLQvellHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTPMTVYDRP 268
Cdd:TIGR00958 649 DAECEQLLQ----ESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 43-258 6.17e-22

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 98.00  E-value: 6.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  43 ERKRLSVQGLT----HSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGR---------------I 103
Cdd:PRK10261    9 ARDVLAVENLNiafmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmllrrrsrqvI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 104 ELGDQDLANV-SARSRGVGMVFQN--YALFPHLTVAENIAYPLAC-QKLPRAERKARVEEMLSLVRLKDYG---NRLPRE 176
Cdd:PRK10261   89 ELSEQSAAQMrHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 177 LSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNK---- 252
Cdd:PRK10261  169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQgeav 248


                  ....*...
gi 1582545954 253 --GNVEQI 258
Cdd:PRK10261  249 etGSVEQI 256
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
61-265 8.65e-22

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 95.36  E-value: 8.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK----NGRIELGDQDLANVSARSR------GVGMVFQN--YA 128
Cdd:COG4170    22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSC 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 129 LFPHLTVAENIayplaCQKLP-----------RAERKARVEEMLSLVRLKDYG---NRLPRELSGGQQQRVAVARAIAGR 194
Cdd:COG4170   102 LDPSAKIGDQL-----IEAIPswtfkgkwwqrFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQ 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 195 PSLLLLDEPFGALD---RALRFDLqveLLHLQKTLGITTLIVTHDQEEAQSLANRLVLM------NKGNVEQI-DTPMTV 264
Cdd:COG4170   177 PRLLIADEPTNAMEsttQAQIFRL---LARLNQLQGTSILLISHDLESISQWADTITVLycgqtvESGPTEQIlKSPHHP 253


                  .
gi 1582545954 265 Y 265
Cdd:COG4170   254 Y 254
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
48-261 1.06e-21

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 93.70  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQ 125
Cdd:PRK10575   13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIA---YPL--ACQKLPRAERKaRVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:PRK10575   93 QLPAAEGMTVRELVAigrYPWhgALGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 201 DEPFGALDRAlrfdLQVELLHLQKTL----GITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTP 261
Cdd:PRK10575  172 DEPTSALDIA----HQVDVLALVHRLsqerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
48-261 1.41e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 97.12  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR--------- 118
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpriaymp 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 -GVGmvfQNyaLFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:NF033858   83 qGLG---KN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 198 LLLDEP-----------FGALDRALRfdlqvellhlQKTLGITTLIVTHDQEEAQSLaNRLVLMNKGNVEQIDTP 261
Cdd:NF033858  158 LILDEPttgvdplsrrqFWELIDRIR----------AERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 47-294 1.47e-21

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 94.41  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN----AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQpKNGRIE------------LGDQDL 110
Cdd:PRK09473   13 LDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGgsatfngreilnLPEKEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 111 ANVsaRSRGVGMVFQN--YALFPHLTVAENIAYPLACQK-LPRAERKARVEEMLSLVRLKDYGNRL---PRELSGGQQQR 184
Cdd:PRK09473   92 NKL--RAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 185 VAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTV 264
Cdd:PRK09473  170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249

                         250       260       270
                  ....*....|....*....|....*....|
gi 1582545954 265 YDRPKTLFVntfIGqanLLNGtVLRLDAES 294
Cdd:PRK09473  250 FYQPSHPYS---IG---LLNA-VPRLDAEG 272
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 51-255 1.67e-21

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 91.94  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  51 GLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLI--QPKNGRIELGDQDLANVsarsrgvgmvfqnya 128
Cdd:COG2401    35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE--------------- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 129 lfphLTVAENIayplacqklPRAERKARVEEMLSLVRLKDYGN--RLPRELSGGQQQRVAVARAIAGRPSLLLLDEpFGA 206
Cdd:COG2401   100 ----ASLIDAI---------GRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCS 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 207 -LDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLA-NRLVLMNKGNV 255
Cdd:COG2401   166 hLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGV 216
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 50-255 2.46e-21

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: 91.76  E-value: 2.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  50 QGLTHSYGGQ---NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR--SRGVGMVF 124
Cdd:cd03248    15 QNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYALFPHlTVAENIAYPLAC---QKLPRAERKARVEEMLSLVRL---KDYGNRlPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:cd03248    95 QEPVLFAR-SLQDNIAYGLQScsfECVKEAAQKAHAHSFISELASgydTEVGEK-GSQLSGGQKQRVAIARALIRNPQVL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 199 LLDEPFGALDraLRFDLQVELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNV 255
Cdd:cd03248   173 ILDEATSALD--AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
47-235 2.99e-21

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 95.86  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTvlraIAGLI----QPKNGRIELGDQDLANVSARS--R 118
Cdd:PRK11176  342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKST----IANLLtrfyDIDEGEILLDGHDLRDYTLASlrN 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFpHLTVAENIAYPlACQKLPRAErkarVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQRVAV 187
Cdd:PRK11176  418 QVALVSQNVHLF-NDTIANNIAYA-RTEQYSREQ----IEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAI 491

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1582545954 188 ARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLgiTTLIVTH 235
Cdd:PRK11176  492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH 537
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 47-253 5.28e-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: 94.89  E-value: 5.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGlIQPK---NGRIELGDQDLANVSAR---SRGV 120
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRdteRAGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENI----AYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLP-RELSGGQQQRVAVARAIAGRP 195
Cdd:TIGR02633  81 VIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 196 SLLLLDEPFGALDRAlrfDLQVeLLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:TIGR02633 161 RLLILDEPSSSLTEK---ETEI-LLDIIRDLkahGVACVYISHKLNEVKAVCDTICVIRDG 217
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 47-255 5.97e-21

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 94.73  E-value: 5.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRGVGMV 123
Cdd:PRK15439   12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLGIYLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENIAYPLAcqklPRAERKARVEEMLSLVrlkdyGNRLPRELSGG-----QQQRVAVARAIAGRPSLL 198
Cdd:PRK15439   92 PQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAAL-----GCQLDLDSSAGslevaDRQIVEILRGLMRDSRIL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 199 LLDEPFGALDRA--LRFDLQVELLhLQKTLGIttLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK15439  163 ILDEPTASLTPAetERLFSRIREL-LAQGVGI--VFISHKLPEIRQLADRISVMRDGTI 218
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 62-254 1.65e-20

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 87.59  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-GDQDLANVSARSrgvgmvfqnYalFPHLTVAENIA 140
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQRP---------Y--LPLGTLREQLI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 141 YPLAcqklpraerkarveemlslvrlkdygnrlpRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDralrFDLQVELL 220
Cdd:cd03223    86 YPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLY 131

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1582545954 221 HLQKTLGITTLIVTHdQEEAQSLANR-LVLMNKGN 254
Cdd:cd03223   132 QLLKELGITVISVGH-RPSLWKFHDRvLDLDGEGG 165
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 62-255 1.88e-20

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 88.47  E-value: 1.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK---NGRIELGDQDLANVSARSRG-VGMVFQNYALFPHLTVAE 137
Cdd:cd03233    23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGeIIYVSEEDVHFPTLTVRE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 138 NIAYPLACQklpraerkarveemlslvrlkdyGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQV 217
Cdd:cd03233   103 TLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582545954 218 ELLHLQKTLGITTLI-VTHDQEEAQSLANRLVLMNKGNV 255
Cdd:cd03233   160 CIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
41-255 2.11e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 90.33  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLaNVSARSRG 119
Cdd:PRK15056    1 MMQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYAL---FPHLTvaENIAY-----PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAI 191
Cdd:PRK15056   80 VAYVPQSEEVdwsFPVLV--EDVVMmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVlMNKGNV 255
Cdd:PRK15056  158 AQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTV 219
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 47-238 2.88e-20

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: 87.97  E-value: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK--NGRIELGDQDLANVSA--RSR-GVG 121
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPeeRARlGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHLTVAEniayplacqklpraerkarveemlsLVRLKDYGnrlpreLSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:cd03217    81 LAFQYPPEIPGVKNAD-------------------------FLRYVNEG------FSGGEKKRNEILQLLLLEPDLAILD 129

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1582545954 202 EPFGALD-RALRfdLQVELLHLQKTLGITTLIVTHDQE 238
Cdd:cd03217   130 EPDSGLDiDALR--LVAEVINKLREEGKSVLIITHYQR 165
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
47-210 3.06e-20

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 87.94  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLanvsARSRGVgmVFQN 126
Cdd:PRK13538    2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDE--YHQD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPH-------LTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDygnrLP-RELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK13538   76 LLYLGHqpgikteLTALENLRFYQRLHGPGDDEALWEALAQVGLAGFED----VPvRQLSAGQQRRVALARLWLTRAPLW 151

                         170
                  ....*....|..
gi 1582545954 199 LLDEPFGALDRA 210
Cdd:PRK13538  152 ILDEPFTAIDKQ 163
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 47-257 3.17e-20

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 92.58  E-value: 3.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSY--GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGM 122
Cdd:PRK11160  339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISV 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHlTVAENIAypLACqklPRA--ERKARVEEMLSLVRLKDYGNRLP-------RELSGGQQQRVAVARAIAG 193
Cdd:PRK11160  419 VSQRVHLFSA-TLRDNLL--LAA---PNAsdEALIEVLQQVGLEKLLEDDKGLNawlgeggRQLSGGEQRRLGIARALLH 492

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 194 RPSLLLLDEPFGALDRalRFDLQVELLHLQKTLGITTLIVTHdqeEAQSLA--NRLVLMNKGN-VEQ 257
Cdd:PRK11160  493 DAPLLLLDEPTEGLDA--ETERQILELLAEHAQNKTVLMITH---RLTGLEqfDRICVMDNGQiIEQ 554
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 61-253 4.00e-20

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: 87.91  E-value: 4.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqdlanvsarSRGVGMVFQNYALFPhLTVAENI- 139
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----------PGSIAYVSQEPWIQN-GTIRENIl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 140 -AYPLacqklpraeRKARVEEMLSLVRLKDYGNRLPR-------E----LSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:cd03250    88 fGKPF---------DEERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 208 D----RALRFDLQVELLHLQKtlgiTTLIVTHdQEEAQSLANRLVLMNKG 253
Cdd:cd03250   159 DahvgRHIFENCILGLLLNNK----TRILVTH-QLQLLPHADQIVVLDNG 203
PLN03211 PLN03211
ABC transporter G-25; Provisional
 29-230 4.93e-20

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 92.25  E-value: 4.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  29 QNQGG---PMLGIPNMAERKRLSVQGLThsyggqnAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKN--GRI 103
Cdd:PLN03211   55 KNKGSnikRILGHKPKISDETRQIQERT-------ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 104 ELGDQDLANVSARSrgVGMVFQNYALFPHLTVAENIAYpLACQKLPRA---ERKARVEEM----LSLVRLKD--YGNRLP 174
Cdd:PLN03211  128 LANNRKPTKQILKR--TGFVTQDDILYPHLTVRETLVF-CSLLRLPKSltkQEKILVAESviseLGLTKCENtiIGNSFI 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 175 RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHL-QKTLGITT 230
Cdd:PLN03211  205 RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLaQKGKTIVT 261
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
47-293 5.72e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.91  E-value: 5.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLaNVSARS-----RGVG 121
Cdd:PRK13638    2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGllalrQQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQN--YALFpHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:PRK13638   81 TVFQDpeQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 200 LDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDRPKTlfvntfIGQ 279
Cdd:PRK13638  160 LDEPTAGLDPAGRTQM-IAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA------MEQ 232

                         250
                  ....*....|....
gi 1582545954 280 ANLLNGTVLRLDAE 293
Cdd:PRK13638  233 AGLTQPWLVKLHTQ 246
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 46-261 7.20e-20

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: 87.08  E-value: 7.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSYGGQ--NAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVG 121
Cdd:cd03369     6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHlTVAENiayplacqkLPRAERKARVEEMLSLvRLKDYGNrlprELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:cd03369    86 IIPQDPTLFSG-TIRSN---------LDPFDEYSDEEIYGAL-RVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 202 EPFGALDRALRFDLQvELLHlQKTLGITTLIVTHdqeEAQSLA--NRLVLMNKGNVEQIDTP 261
Cdd:cd03369   151 EATASIDYATDALIQ-KTIR-EEFTNSTILTIAH---RLRTIIdyDKILVMDAGEVKEYDHP 207
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 59-255 1.24e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 90.88  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  59 QNAISDVAfdiEAGEIVALLGPSGCGKSTVLRAIAGLIQP---KNGRIELGDQ--DLANVSARSrgvGMVFQNYALFPHL 133
Cdd:TIGR00955  41 LKNVSGVA---KPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMpiDAKEMRAIS---AYVQQDDLFIPTL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYpLACQKLPRA----ERKARVEEMLSLVRLKDYGNRL------PRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:TIGR00955 115 TVREHLMF-QAHLRMPRRvtkkEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 204 FGALDRALRFDLQVELLHL-QKTlgiTTLIVTHDQEEAQ--SLANRLVLMNKGNV 255
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLaQKG---KTIICTIHQPSSElfELFDKIILMAEGRV 245
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 47-239 1.44e-19

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 90.37  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGlIQPK---NGRIELGDQDLANVSAR---SRGV 120
Cdd:PRK13549    6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRdteRAGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENI---AYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:PRK13549   85 AIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 198 LLLDEPFGALDRAlrfDLQVeLLHLQKTL---GITTLIVTHDQEE 239
Cdd:PRK13549  165 LILDEPTASLTES---ETAV-LLDIIRDLkahGIACIYISHKLNE 205
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
43-260 1.59e-19

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 86.86  E-value: 1.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  43 ERKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN-VSAR--SRG 119
Cdd:PRK11614    2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKimREA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 VGMVFQNYALFPHLTVAENIAY-PLACQKLPRAERKARVEEMLSlvRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK11614   82 VAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 199 LLDEPfgALDRALRFDLQV-ELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDT 260
Cdd:PRK11614  160 LLDEP--SLGLAPIIIQQIfDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
53-235 2.42e-19

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 90.02  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  53 THSYGGQN-AISDVAFDIEAGEIVALLGPSGCGKSTVLraiaGLIQ----PKNGRIELGDQDLANVSARS--RGVGMVFQ 125
Cdd:PRK13657  341 SFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQrvfdPQSGRILIDGTDIRTVTRASlrRNIAVVFQ 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHlTVAENI--AYPLAC-QKLPRAERKARVEEMLsLVRLKDY----GNRlPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK13657  417 DAGLFNR-SIEDNIrvGRPDATdEEMRAAAERAQAHDFI-ERKPDGYdtvvGER-GRQLSGGERQRLAIARALLKDPPIL 493

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1582545954 199 LLDEPFGALDRALRFDLQVELLHLQKtlGITTLIVTH 235
Cdd:PRK13657  494 ILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH 528
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
47-203 3.72e-19

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 89.20  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS---RGVGMV 123
Cdd:PRK11288    5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAGVAII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENI---AYPLACQKLPRAERKARVEEMLSLVRLK-DYGNRLpRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:PRK11288   85 YQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDiDPDTPL-KYLSIGQRQMVEIAKALARNARVIA 163


                  ....
gi 1582545954 200 LDEP 203
Cdd:PRK11288  164 FDEP 167
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 47-257 5.11e-19

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: 89.41  E-value: 5.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYG-GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--ARSRGVGMV 123
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHlTVAENIayplacqkLPRAERKARVEEM---LSLVRLKD--------YGNRLPRE---LSGGQQQRVAVAR 189
Cdd:TIGR01193 554 PQEPYIFSG-SILENL--------LLGAKENVSQDEIwaaCEIAEIKDdienmplgYQTELSEEgssISGGQKQRIALAR 624

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 190 AIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTlgiTTLIVTHDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 34-257 5.50e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.99  E-value: 5.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  34 PMLGIPNmaerkrLSVqGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKS-TVLRAIAGLIQPK----NGRIELGDQ 108
Cdd:PRK15134    4 PLLAIEN------LSV-AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 109 DLANVSARS-RGV-----GMVFQN--YALFPHLTVAENIAYPLACQKLPRaeRKARVEEMLSLV----------RLKDYg 170
Cdd:PRK15134   77 SLLHASEQTlRGVrgnkiAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMR--REAARGEILNCLdrvgirqaakRLTDY- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 171 nrlPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLM 250
Cdd:PRK15134  154 ---PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230


                  ....*...
gi 1582545954 251 NKGN-VEQ 257
Cdd:PRK15134  231 QNGRcVEQ 238
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 55-257 5.73e-19

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 88.75  E-value: 5.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIqPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFpH 132
Cdd:PRK11174  359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-H 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 133 LTVAENI--AYPLAC-QKLPRAERKARVEEMLSLVRLK-DY--GNRLPReLSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:PRK11174  437 GTLRDNVllGNPDASdEQLQQALENAWVSEFLPLLPQGlDTpiGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTAS 515

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 207 LDRalrfdlQVELLHLQK----TLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:PRK11174  516 LDA------HSEQLVMQAlnaaSRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
47-253 6.67e-19

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 88.69  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQD---LANVSARSRGVGMV 123
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIGII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENiaypLACQKLPR-----------AERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIA 192
Cdd:PRK09700   86 YQELSVIDELTVLEN----LYIGRHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 193 GRPSLLLLDEPFGALDRAlrfdlQVELLHL----QKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK09700  162 LDAKVIIMDEPTSSLTNK-----EVDYLFLimnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 47-236 9.04e-19

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 85.17  E-value: 9.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElgdqdlanvsaRSRG--VGMVF 124
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKlrIGYVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QNYALFPHLtvaeniayPLACQKLPR---AERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLD 201
Cdd:PRK09544   74 QKLYLDTTL--------PLTVNRFLRlrpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1582545954 202 EPFGALDRALRFDLQVELLHLQKTLGITTLIVTHD 236
Cdd:PRK09544  146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
39-208 3.65e-18

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 82.59  E-value: 3.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  39 PNMAERKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgDQDLANVSARSR 118
Cdd:PRK13543    4 PLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 119 GVGMVFQNYALFPHLTVAENIAYPLACQKLpRAERKArvEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLL 198
Cdd:PRK13543   83 FMAYLGHLPGLKADLSTLENLHFLCGLHGR-RAKQMP--GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159

                         170
                  ....*....|
gi 1582545954 199 LLDEPFGALD 208
Cdd:PRK13543  160 LLDEPYANLD 169
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 67-255 1.60e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 81.52  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  67 FDIEAGEIVALLGPSGCGKSTVLRAIAGLIqPKNGRIELGDQDLANVS----ARSRG---------VGM-VFQNYALFPH 132
Cdd:PRK03695   17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaaelARHRAylsqqqtppFAMpVFQYLTLHQP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 133 ltvaeniayplacQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAI-----AGRPS--LLLLDEPFG 205
Cdd:PRK03695   96 -------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMN 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954 206 ALDRALRFDLQvELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK03695  163 SLDVAQQAALD-RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
GguA NF040905
sugar ABC transporter ATP-binding protein;
47-259 1.65e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.07  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGlIQPK---NGRIELGDQDLANVSARS---RGV 120
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDseaLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHLTVAENIAYPLACQK---LPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:NF040905   81 VIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 198 LLLDEPFGAL---DRALRFDLQVELlhlqKTLGITTLIVTHDQEEAQSLANRL-VLMNKGNVEQID 259
Cdd:NF040905  161 LILDEPTAALneeDSAALLDLLLEL----KAQGITSIIISHKLNEIRRVADSItVLRDGRTIETLD 222
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 46-261 2.77e-17

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: 80.23  E-value: 2.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSY--GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---ARSRgV 120
Cdd:cd03244     2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlhdLRSR-I 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQNYALFPHlTVAENIAyplacqklPRAER-KARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVA 188
Cdd:cd03244    81 SIIPQDPVLFSG-TIRSNLD--------PFGEYsDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALrfDLQVellhlQKTL-----GITTLIVTH------DqeeaqslANRLVLMNKGNVEQ 257
Cdd:cd03244   152 RALLRKSKILVLDEATASVDPET--DALI-----QKTIreafkDCTVLTIAHrldtiiD-------SDRILVLDKGRVVE 217


                  ....
gi 1582545954 258 IDTP 261
Cdd:cd03244   218 FDSP 221
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
34-250 3.37e-17

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 81.77  E-value: 3.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  34 PMLGIPNmaerkrLSVQGLThSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGlIQPKNGRI-----ELGDQ 108
Cdd:PRK15093    2 PLLDIRN------LTIEFKT-SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVtadrmRFDDI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 109 DLANVSARSR------GVGMVFQNyalfPH--LTVAENIAYPLAcQKLPRAE-----------RKARVEEMLSLVRLKDY 169
Cdd:PRK15093   74 DLLRLSPRERrklvghNVSMIFQE----PQscLDPSERVGRQLM-QNIPGWTykgrwwqrfgwRKRRAIELLHRVGIKDH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 170 GNRL---PRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANR 246
Cdd:PRK15093  149 KDAMrsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228


                  ....
gi 1582545954 247 LVLM 250
Cdd:PRK15093  229 INVL 232
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 62-269 3.99e-17

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 80.51  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQP----KNGRIELGDQDLANVSARSRGVGMVFQN--YALFPHLTV 135
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIAYplACQKLPRAERKARVEEMLSLVRLKDYGNRL---PRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD---R 209
Cdd:PRK10418   99 HTHARE--TCLALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDvvaQ 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 210 ALRFDLQVELLHlQKTLGIttLIVTHDQEEAQSLANRLVLMNKGN-VEQIDTpMTVYDRPK 269
Cdd:PRK10418  177 ARILDLLESIVQ-KRALGM--LLVTHDMGVVARLADDVAVMSHGRiVEQGDV-ETLFNAPK 233
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 47-237 4.81e-17

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 80.11  E-value: 4.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLI--QPKNGRIELGDQDLANVSA--RSR-GVG 121
Cdd:COG0396     1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPdeRARaGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHLTVAE--NIAY-PLACQKLPRAERKARVEEMLSLVRL-KDYGNR-LPRELSGGQQQRVAVARAIAGRPS 196
Cdd:COG0396    81 LAFQYPVEIPGVSVSNflRTALnARRGEELSAREFLKLLKEKMKELGLdEDFLDRyVNEGFSGGEKKRNEILQMLLLEPK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582545954 197 LLLLDEPFGALD----RALRfdLQVELLHLQKTlgiTTLIVTHDQ 237
Cdd:COG0396   161 LAILDETDSGLDidalRIVA--EGVNKLRSPDR---GILIITHYQ 200
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 45-259 4.83e-17

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 83.10  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLTHSYGGQN-AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ--DLANVSARSRGVG 121
Cdd:PRK10522  321 QTLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvTAEQPEDYRKLFS 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHLTVAENIAYPlacqklpraerKARVEEMLSLVRLKDY----GNRLPR-ELSGGQQQRVAVARAIAGRPS 196
Cdd:PRK10522  401 AVFTDFHLFDQLLGPEGKPAN-----------PALVEKWLERLKMAHKleleDGRISNlKLSKGQKKRLALLLALAEERD 469

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 197 LLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQID 259
Cdd:PRK10522  470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELT 531
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 42-253 5.94e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 82.41  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  42 AERKRLSVQGLThsygGQnAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR-GV 120
Cdd:PRK15439  264 AGAPVLTVEDLT----GE-GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlAR 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVF-----QNYALFPHLTVAENIaYPLACQKLP----RAERKARVEEMLSLVRLK-DYGNRLPRELSGGQQQRVAVARA 190
Cdd:PRK15439  339 GLVYlpedrQSSGLYLDAPLAWNV-CALTHNRRGfwikPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKC 417

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 191 IAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK15439  418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQG 479
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 38-211 2.12e-16

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: 81.13  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  38 IPNmAER---KRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ-DLANV 113
Cdd:TIGR03719 312 IPP-GPRlgdKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYV 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 114 SaRSRGvgmvfqnyALFPHLTVAENIAYPLACQKLPRAERKARVeeMLSLVRLK--DYGNRLpRELSGGQQQRVAVARAI 191
Cdd:TIGR03719 391 D-QSRD--------ALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKgsDQQKKV-GQLSGGERNRVHLAKTL 458

                         170       180
                  ....*....|....*....|....
gi 1582545954 192 AGRPSLLLLDEPFGALD----RAL 211
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDvetlRAL 482
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 47-208 4.63e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 76.14  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDL-ANVSARSRGVGMVFQ 125
Cdd:PRK13540    2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYALFPHLTVAENIAYPLACqklprAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFG 205
Cdd:PRK13540   82 RSGINPYLTLRENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156


                  ...
gi 1582545954 206 ALD 208
Cdd:PRK13540  157 ALD 159
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 44-248 6.47e-16

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 79.55  E-value: 6.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQdlANvsarsrgVGMV 123
Cdd:PRK15064  317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--AN-------IGYY 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYAL-FPH-LTVAENIayplaCQ-KLPRAERKArVEEMLSlvRL---KDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:PRK15064  388 AQDHAYdFENdLTLFDWM-----SQwRQEGDDEQA-VRGTLG--RLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 198 LLLDEPFGALDRALRFDLQVELLHLQKTLgittLIVTHDQEEAQSLANRLV 248
Cdd:PRK15064  460 LVMDEPTNHMDMESIESLNMALEKYEGTL----IFVSHDREFVSSLATRII 506
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
44-255 7.08e-16

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 78.24  E-value: 7.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  44 RKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGcgkSTVLRAI--AGLIQPKNGRIELGDQD-LANVSARSRGV 120
Cdd:NF000106   11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G---AA**RGAlpAHV*GPDAGRRPWRF*TwCANRRALRRTI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 121 GMVFQ-NYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:NF000106   88 G*HRPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 200 LDEPFGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:NF000106  168 LDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 62-253 1.84e-15

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 78.61  E-value: 1.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQ----PKNGRIELGDQDLANVSARSRG-VGMVFQNYALFPHLTVA 136
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGdVVYNAETDVHFPHLTVG 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  137 ENIAYPLACQK-------LPRAERKARVEEM------LSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:TIGR00956  157 ETLDFAARCKTpqnrpdgVSREEYAKHIADVymatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954  204 FGALDRALRFDLqVELLHLQKTLGITTLIVTHDQ--EEAQSLANRLVLMNKG 253
Cdd:TIGR00956  237 TRGLDSATALEF-IRALKTSANILDTTPLVAIYQcsQDAYELFDKVIVLYEG 287
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 62-235 2.48e-15

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: 74.67  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRI-----ELGDQDLANVSARSRG-VGMVFQNYALFpHLTV 135
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYsVAYAAQKPWLL-NATV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIAY--PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPR--ELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:cd03290    96 EENITFgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175

                         170       180
                  ....*....|....*....|....*
gi 1582545954 212 RFDL-QVELLHLQKTLGITTLIVTH 235
Cdd:cd03290   176 SDHLmQEGILKFLQDDKRTLVLVTH 200
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 47-207 3.63e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 76.97  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSR---GVGMV 123
Cdd:PRK10762    5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaGIGII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQNYALFPHLTVAENI------AYPLACQKLPRAERKArvEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSL 197
Cdd:PRK10762   85 HQELNLIPQLTIAENIflgrefVNRFGRIDWKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162

                         170
                  ....*....|
gi 1582545954 198 LLLDEPFGAL 207
Cdd:PRK10762  163 IIMDEPTDAL 172
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 45-261 6.70e-15

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: 76.38  E-value: 6.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLTHSYGGQNAisDVAF-------DIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDlanVSARS 117
Cdd:COG4615   326 QTLELRGVTYRYPGEDG--DEGFtlgpidlTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADN 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 RGV-----GMVFQNYALFPHLtvaeniaYPLACQKLPraerkARVEEMLSL------VRLKDyGNRLPRELSGGQQQRVA 186
Cdd:COG4615   401 REAyrqlfSAVFSDFHLFDRL-------LGLDGEADP-----ARARELLERleldhkVSVED-GRFSTTDLSQGQRKRLA 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 187 VARAIA-GRPsLLLLDE------PfgaldrALRfdlQV---ELLHLQKTLGITTLIVTHDqEEAQSLANRLVLMNKGNVE 256
Cdd:COG4615   468 LLVALLeDRP-ILVFDEwaadqdP------EFR---RVfytELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536


                  ....*
gi 1582545954 257 QIDTP 261
Cdd:COG4615   537 ELTGP 541
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 47-260 1.34e-14

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: 76.21  E-value: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   47 LSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-GDQDLANVSARSRGVGMV 123
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMGYC 2017

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  124 FQNYALFPHLTVAENIAYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEP 203
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954  204 FGALDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDT 260
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
41-257 1.57e-14

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 75.13  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSYGGQN--AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANV---SA 115
Cdd:PRK10789  308 PEGRGELDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSW 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 116 RSRgVGMVFQNYALFPHlTVAENIAypLACqklPRAErKARVEEMLSLVRLKDYGNRLPR-----------ELSGGQQQR 184
Cdd:PRK10789  388 RSR-LAVVSQTPFLFSD-TVANNIA--LGR---PDAT-QQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQR 459

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 185 VAVARAIAGRPSLLLLDEPFGALDRalRFDLQVeLLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:PRK10789  460 ISIARALLLNAEILILDDALSAVDG--RTEHQI-LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 64-269 1.87e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 75.45  E-value: 1.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGD-QDLANVSA---RSRgVGMVFQNYALFPHlTVAENI 139
Cdd:PTZ00265   403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLkwwRSK-IGVVSQDPLLFSN-SIKNNI 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  140 AYPLACQK--------------------LPRAERKARVEEMLSL-------------------------------VRLKD 168
Cdd:PTZ00265   481 KYSLYSLKdlealsnyynedgndsqenkNKRNSCRAKCAGDLNDmsnttdsneliemrknyqtikdsevvdvskkVLIHD 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  169 YGNRLP-----------RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQ 237
Cdd:PTZ00265   561 FVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1582545954  238 EEAQSLANRLVLMNKGNVEQIDTPMTVYDRPK 269
Cdd:PTZ00265   641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTK 672
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 48-236 2.65e-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: 74.59  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  48 SVQGLTHSYGGQNAI-SDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIelgdqdlanVSARSRGVGMVFQN 126
Cdd:TIGR03719   6 TMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENIAypLACQKL----------------PRAERKARVEEMLSLVRLKDYGN---------------RLP- 174
Cdd:TIGR03719  77 PQLDPTKTVRENVE--EGVAEIkdaldrfneisakyaePDADFDKLAAEQAELQEIIDAADawdldsqleiamdalRCPp 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 175 -----RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAlrfdlQVELL--HLQKTLGiTTLIVTHD 236
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-----SVAWLerHLQEYPG-TVVAVTHD 217
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 68-248 3.30e-14

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 71.67  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  68 DIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqDLANVSARSRGVGMVFQnyalfphLTVaeniaYPLACQK 147
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYE-------GTV-----RDLLSSI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 148 LPRAERKA--RVEEM--LSLVRLKDygnRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD--------RAL-RFd 214
Cdd:cd03237    86 TKDFYTHPyfKTEIAkpLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmasKVIrRF- 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1582545954 215 lqveLLHLQKtlgiTTLIVTHDQEEAQSLANRLV 248
Cdd:cd03237   162 ----AENNEK----TAFVVEHDIIMIDYLADRLI 187
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 49-238 1.57e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 72.29  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  49 VQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ-DLAnvsarsrgvgmVFQNY 127
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA-----------YFDQH 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 --ALFPHLTVAENIayplacqklprAERKARVE----EMLSLVRLKDY-----GNRLP-RELSGGQQQRVAVARAIAgRP 195
Cdd:PRK11147  391 raELDPEKTVMDNL-----------AEGKQEVMvngrPRHVLGYLQDFlfhpkRAMTPvKALSGGERNRLLLARLFL-KP 458

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1582545954 196 S-LLLLDEPFGaldralrfDLQVELLHLQKTL-----GiTTLIVTHDQE 238
Cdd:PRK11147  459 SnLLILDEPTN--------DLDVETLELLEELldsyqG-TVLLVSHDRQ 498
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
40-258 2.80e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 71.35  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  40 NMAERKRLSVQGLTHSYGGQnaISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS---AR 116
Cdd:PRK09700  259 NLAHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldAV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRGVGMVFQNY---ALFPHLTVAENIAYPLACQKL----------PRAERKArVEEMLSLVRLKDYG-NRLPRELSGGQQ 182
Cdd:PRK09700  337 KKGMAYITESRrdnGFFPNFSIAQNMAISRSLKDGgykgamglfhEVDEQRT-AENQRELLALKCHSvNQNITELSGGNQ 415

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 183 QRVAVARAIAGRPSLLLLDEPfgalDRALRFDLQVELLHLQKTL---GITTLIVTHDQEEAQSLANRLVLMNKGNVEQI 258
Cdd:PRK09700  416 QKVLISKWLCCCPEVIIFDEP----TRGIDVGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 72-249 3.97e-13

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: 66.63  E-value: 3.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   72 GEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDlanvsarsrgvgmvfqnyalfphltvaeniayplacqklpra 151
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE------------------------------------------ 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  152 erkaRVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVE-----LLHLQKTL 226
Cdd:smart00382  40 ----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115

                          170       180
                   ....*....|....*....|...
gi 1582545954  227 GITTLIVTHDQEEAQSLANRLVL 249
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 58-235 4.41e-13

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 70.93  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  58 GQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-GDQDLANVSAR---SRGvgmvfqnyalfphl 133
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpAKGKLFYVPQRpymTLG-------------- 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 134 TVAENIAYPLAC-QKLPRAERKARVEEMLSLVRLkdyGNRLPRE------------LSGGQQQRVAVARAIAGRPSLLLL 200
Cdd:TIGR00954 530 TLRDQIIYPDSSeDMKRRGLSDKDLEQILDNVQL---THILEREggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAIL 606

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1582545954 201 DEpfgaLDRALRFDLQVELLHLQKTLGITTLIVTH 235
Cdd:TIGR00954 607 DE----CTSAVSVDVEGYMYRLCREFGITLFSVSH 637
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 52-236 9.18e-13

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: 69.81  E-value: 9.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  52 LTHSYGgQNAisdvaFDI------EAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElGDQDLANVSARSRGVgmvfq 125
Cdd:COG1245    79 PVHRYG-ENG-----FRLyglpvpKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEVLKRFRGT----- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 nyALFPHLT-VAEN---IAY-PLACQKLPRA-------------ERKArVEEMLSLVRLKDYGNRLPRELSGGQQQRVAV 187
Cdd:COG1245   147 --ELQDYFKkLANGeikVAHkPQYVDLIPKVfkgtvrellekvdERGK-LDELAEKLGLENILDRDISELSGGELQRVAI 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 188 ARAIAGRPSLLLLDEPFGALD--------RALRfdlqvELLHLQKTLgittLIVTHD 236
Cdd:COG1245   224 AAALLRDADFYFFDEPSSYLDiyqrlnvaRLIR-----ELAEEGKYV----LVVEHD 271
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
46-233 2.87e-12

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 68.21  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSY-GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGM 122
Cdd:PRK10790  340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlrQGVAM 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 123 VFQNYALFPHlTVAENIAyplacqkLPRAERKARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARAI 191
Cdd:PRK10790  420 VQQDPVVLAD-TFLANVT-------LGRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVL 491

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582545954 192 AGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTlgiTTLIV 233
Cdd:PRK10790  492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVV 530
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
46-255 4.39e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 67.63  E-value: 4.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLThsygGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqDLANVSARSRG----VG 121
Cdd:PRK11288  257 RLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL---DGKPIDIRSPRdairAG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVF-----QNYALFPHLTVAENIAY-------PLACQKLPRAERKaRVEEMLSLVRLKDYGNRLP-RELSGGQQQRVAVA 188
Cdd:PRK11288  330 IMLcpedrKAEGIIPVHSVADNINIsarrhhlRAGCLINNRWEAE-NADRFIRSLNIKTPSREQLiMNLSGGNQQKAILG 408

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 189 RAIAGRPSLLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNV 255
Cdd:PRK11288  409 RWLSEDMKVILLDEPTRGIDVGAKHEI-YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 19-208 5.54e-12

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: 66.03  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  19 ETAQQSVTSTQNQGgpmlgIPNMAERKRLSVQGLTHSYGGQNA------------ISDVAFDIEAGEIVALLGPSGCGKS 86
Cdd:cd03291     3 GVIMENVTAFWDEG-----FGELLEKAKQENNDRKHSSDDNNLffsnlclvgapvLKNINLKIEKGEMLAITGSTGSGKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  87 TVLRAIAGLIQPKNGRIElgdqdlanvsaRSRGVGMVFQNYALFPHlTVAENIAYPL------------ACQklpraerk 154
Cdd:cd03291    78 SLLMLILGELEPSEGKIK-----------HSGRISFSSQFSWIMPG-TIKENIIFGVsydeyryksvvkACQ-------- 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582545954 155 arVEEMLSLVRLKDygNRLPRE----LSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:cd03291   138 --LEEDITKFPEKD--NTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 45-253 8.87e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 66.57  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLTHSyggqnAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS------- 117
Cdd:PRK10762  256 VRLKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangiv 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 118 ------RGVGMVFQnyalfphLTVAENIAYPlACQKLPR--------AERKArVEEMLSLVRLKDYGNRLP-RELSGGQQ 182
Cdd:PRK10762  331 yisedrKRDGLVLG-------MSVKENMSLT-ALRYFSRaggslkhaDEQQA-VSDFIRLFNIKTPSMEQAiGLLSGGNQ 401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 183 QRVAVARAIAGRPSLLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK10762  402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
52-236 1.09e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 66.37  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  52 LTHSYGgQNAisdvaFDI------EAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElGDQDLANVSARSRGVGMvfQ 125
Cdd:PRK13409   79 PVHRYG-VNG-----FKLyglpipKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE-EEPSWDEVLKRFRGTEL--Q 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 126 NYalFPHL-----TVAENIAYplaCQKLPRA-------------ERKArVEEMLSLVRLKDYGNRLPRELSGGQQQRVAV 187
Cdd:PRK13409  150 NY--FKKLyngeiKVVHKPQY---VDLIPKVfkgkvrellkkvdERGK-LDEVVERLGLENILDRDISELSGGELQRVAI 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954 188 ARAIAGRPSLLLLDEPFGALD--------RALRfdlqvELlhlqkTLGITTLIVTHD 236
Cdd:PRK13409  224 AAALLRDADFYFFDEPTSYLDirqrlnvaRLIR-----EL-----AEGKYVLVVEHD 270
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 38-211 1.45e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.91  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  38 IPNmAER---KRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQ-DLANV 113
Cdd:PRK11819  314 IPP-GPRlgdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKLAYV 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 114 SaRSRGvgmvfqnyALFPHLTVAENIAYPLACQKLPRAERKARVeemlslvrlkdYGNR----------LPRELSGGQQQ 183
Cdd:PRK11819  393 D-QSRD--------ALDPNKTVWEEISGGLDIIKVGNREIPSRA-----------YVGRfnfkggdqqkKVGVLSGGERN 452

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1582545954 184 RVAVARAIAGRPSLLLLDEPFGALD----RAL 211
Cdd:PRK11819  453 RLHLAKTLKQGGNVLLLDEPTNDLDvetlRAL 484
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 72-208 2.13e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 65.90  E-value: 2.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   72 GEIVALLGPSGCGKSTVLRAIAGliQPKNGRIELGDQdLANVSAR----SRGVGMVFQNYALFPHLTVAENI---AYPLA 144
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDR-LVNGRPLdssfQRSIGYVQQQDLHLPTSTVRESLrfsAYLRQ 865

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954  145 CQKLPRAERKARVEEMLSLVRLKDYGNRL---PRE-LSGGQQQRVAVARAIAGRPSLLL-LDEPFGALD 208
Cdd:TIGR00956  866 PKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 16-260 2.22e-11

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 66.09  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   16 LVPETAQQSVTSTQNQGGPMLGIPNMAERK------RLSVQGLTHSY--GGQNAISDVAFDIEAGEIVALLGPSGCGKST 87
Cdd:TIGR01271 1181 LPQEEPRPSGGGGKYQLSTVLVIENPHAQKcwpsggQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST 1260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   88 VLRAIAGLIQpKNGRIELGDQDLANVSARS--RGVGMVFQNYALF---------PH--------LTVAENIAYPLACQKL 148
Cdd:TIGR01271 1261 LLSALLRLLS-TEGEIQIDGVSWNSVTLQTwrKAFGVIPQKVFIFsgtfrknldPYeqwsdeeiWKVAEEVGLKSVIEQF 1339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  149 PraerkarveEMLSLVrLKDYGnrlpRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAlrfDLQVELLHLQKTLGI 228
Cdd:TIGR01271 1340 P---------DKLDFV-LVDGG----YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV---TLQIIRKTLKQSFSN 1402

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1582545954  229 TTLIVTHDQEEAQSLANRLVLMNKGNVEQIDT 260
Cdd:TIGR01271 1403 CTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 62-253 2.97e-11

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 65.70  E-value: 2.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElgdqdlanvsaRSRGVGMVFQNYALFPHlTVAENIAY 141
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------HSGRISFSPQTSWIMPG-TIKDNIIF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  142 PLACQKLP-RAERKA-RVEEMLSLVRLKDygNRLPRE----LSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDL 215
Cdd:TIGR01271  510 GLSYDEYRyTSVIKAcQLEEDIALFPEKD--KTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1582545954  216 QVELlhLQKTLGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:TIGR01271  588 FESC--LCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
hmuV PRK13547
heme ABC transporter ATP-binding protein;
47-264 3.21e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 63.31  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAG-LIQPK-------NGRIELGDQDLANVS---- 114
Cdd:PRK13547    2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDaprl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 115 ARSRGVgmvfqnyalfphLTVAENIAYPLACQKL------PRAERKAR--------VEEMLSLVRLKDYGNRLPRELSGG 180
Cdd:PRK13547   82 ARLRAV------------LPQAAQPAFAFSAREIvllgryPHARRAGAlthrdgeiAWQALALAGATALVGRDVTTLSGG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 181 QQQRVAVARAIA---------GRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMN 251
Cdd:PRK13547  150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229

                         250
                  ....*....|...
gi 1582545954 252 KGNVEQIDTPMTV 264
Cdd:PRK13547  230 DGAIVAHGAPADV 242
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 47-258 3.38e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 64.75  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSygGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR---SRGVGMV 123
Cdd:PRK10982  251 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeaiNHGFALV 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 124 FQ---NYALFPHLTVAEN--IA----YPLACQKLPRAERKARVEEMLSLVRLKDYGNRLP-RELSGGQQQRVAVARAIAG 193
Cdd:PRK10982  329 TEerrSTGIYAYLDIGFNslISnirnYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLT 408

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 194 RPSLLLLDEPFGALDRALRFDLQVELLHL-QKTLGIttLIVTHDQEEAQSLANRLVLMNKGNVEQI 258
Cdd:PRK10982  409 QPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVAGI 472
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
61-276 3.55e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 63.30  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElgdqdlanvsaRSRGVGMVFQNYALFPHLTVAENIA 140
Cdd:PRK13546   39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQLTGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 141 YPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRfDLQVELL 220
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA-QKCLDKI 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 221 HLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQ---IDTPMTVYDRpktlFVNTF 276
Cdd:PRK13546  187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDygeLDDVLPKYEA----FLNDF 241
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 47-267 3.96e-11

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 64.81  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqdlanvsarSRGVGMVFQN 126
Cdd:PRK10636  313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIKLGYFA 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 YALFPHLTVAENiayPLacQKLpraerkARVEEMLSLVRLKDY-------GNRLP---RELSGGQQQRVAVARAIAGRPS 196
Cdd:PRK10636  382 QHQLEFLRADES---PL--QHL------ARLAPQELEQKLRDYlggfgfqGDKVTeetRRFSGGEKARLVLALIVWQRPN 450

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 197 LLLLDEPFGALDRALRFDLQVELLHLQKTLgittLIVTHDQEEAQSLANRLVLMNKGNVEQIDTPMTVYDR 267
Cdd:PRK10636  451 LLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 53-236 4.39e-11

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: 62.77  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  53 THSYGgQNAISDVAFDI-EAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIElGDQDLANVSARSRGVGMvfQNYalFP 131
Cdd:cd03236     7 VHRYG-PNSFKLHRLPVpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFRGSEL--QNY--FT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 132 HLTVAE--NIAYPLACQKLPRAeRKARVEEMLS----------LVRLKDYGNRLPRE---LSGGQQQRVAVARAIAGRPS 196
Cdd:cd03236    81 KLLEGDvkVIVKPQYVDLIPKA-VKGKVGELLKkkdergkldeLVDQLELRHVLDRNidqLSGGELQRVAIAAALARDAD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1582545954 197 LLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHD 236
Cdd:cd03236   160 FYFFDEPSSYLDIKQRLNA-ARLIRELAEDDNYVLVVEHD 198
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 45-238 5.90e-11

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: 61.47  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLTHSYggqnAISDVAFDieaGEIVALLGPSGCGKSTVLRAI-AGL--IQPKNGRIELGDQDLANVSARSRGVG 121
Cdd:cd03240     2 DKLSIRNIRSFH----ERSEIEFF---SPLTLIVGQNGAGKTTIIEALkYALtgELPPNSKGGAHDPKLIREGEVRAQVK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQN-----YALFPHLTVAENIAYplacqklpraerkARVEEMLSLvrlkdygnrLPRE---LSGGQQQ------RVAV 187
Cdd:cd03240    75 LAFENangkkYTITRSLAILENVIF-------------CHQGESNWP---------LLDMrgrCSGGEKVlasliiRLAL 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 188 ARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLGITTLIV-THDQE 238
Cdd:cd03240   133 AETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNFQLIViTHDEE 184
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 57-255 6.48e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 64.20  E-value: 6.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  57 GGQNAISDVA------FDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgDQDLanVSAR-----SRGV-GMVF 124
Cdd:PRK11147    8 GAWLSFSDAPlldnaeLHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDL--IVARlqqdpPRNVeGTVY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 qNYalfphltVAENIAYplACQKLPR----------------AERKARVEEMLS--------------LVRLKDYGNRLP 174
Cdd:PRK11147   85 -DF-------VAEGIEE--QAEYLKRyhdishlvetdpseknLNELAKLQEQLDhhnlwqlenrinevLAQLGLDPDAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 175 RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDralrFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGN 254
Cdd:PRK11147  155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230


                  .
gi 1582545954 255 V 255
Cdd:PRK11147  231 L 231
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 77-236 6.93e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.98  E-value: 6.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  77 LLGPSGCGKSTVLRAIAGLIQPKNGRIELGDqdlaNVSarsrgVGMVFQNYALFPHLTVAENI----------------- 139
Cdd:PRK11819   38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAP----GIK-----VGYLPQEPQLDPEKTVRENVeegvaevkaaldrfnei 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 140 ----AYPLA-CQKLprAERKARVEEMLSLVRLKDYGN---------RLP------RELSGGQQQRVAVARAIAGRPSLLL 199
Cdd:PRK11819  109 yaayAEPDAdFDAL--AAEQGELQEIIDAADAWDLDSqleiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLL 186

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582545954 200 LDEPFGALDRAlrfdlQVELL--HLQKTLGiTTLIVTHD 236
Cdd:PRK11819  187 LDEPTNHLDAE-----SVAWLeqFLHDYPG-TVVAVTHD 219
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 69-208 9.39e-11

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: 60.72  E-value: 9.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  69 IEAGEIVALLGPSGCGKSTVL-----RAIAGLIQpknGRIELGDQdlANVSARSRGVGMVFQNYALFPHLTVAENIAYPL 143
Cdd:cd03232    30 VKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGR--PLDKNFQRSTGYVEQQDVHSPNLTVREALRFSA 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582545954 144 ACqklpraerkarveemlslvrlkdygnrlpRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:cd03232   105 LL-----------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
52-236 1.12e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 63.29  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  52 LTHSYGGqnaisdvaFDIEA-------GEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIelgDQDLanvsarsrgvgmvf 124
Cdd:PRK13409  346 LTKKLGD--------FSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL-------------- 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 qnyalfphltvaeNIAY-PlacQKLpRAERKARVEEMLSLVRlKDYGN-----------RLPR-------ELSGGQQQRV 185
Cdd:PRK13409  401 -------------KISYkP---QYI-KPDYDGTVEDLLRSIT-DDLGSsyykseiikplQLERlldknvkDLSGGELQRV 462

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954 186 AVARAIAGRPSLLLLDEPFGALD--------RALRfdlqvellHLQKTLGITTLIVTHD 236
Cdd:PRK13409  463 AIAACLSRDADLYLLDEPSAHLDveqrlavaKAIR--------RIAEEREATALVVDHD 513
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 74-235 1.99e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 59.89  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  74 IVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSrgVGMVFQNYALFPHLTVAENIAYplacqklpRAER 153
Cdd:PRK13541   28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFENLKF--------WSEI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 154 KARVEEMLSLV---RLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRfDLQVELLHLQKTLGITT 230
Cdd:PRK13541   98 YNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLNNLIVMKANSGGIV 176


                  ....*
gi 1582545954 231 LIVTH 235
Cdd:PRK13541  177 LLSSH 181
PLN03130 PLN03130
ABC transporter C family member; Provisional
 55-257 2.22e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.83  E-value: 2.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   55 SYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGrielgdqdlANVSARSRgVGMVFQNYALFpHLT 134
Cdd:PLN03130   626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD---------ASVVIRGT-VAYVPQVSWIF-NAT 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  135 VAENIAY--PLACQKLPRAERKARVEEMLSLV---RLKDYGNRlPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDR 209
Cdd:PLN03130   695 VRDNILFgsPFDPERYERAIDVTALQHDLDLLpggDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1582545954  210 ALrfDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:PLN03130   774 HV--GRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 68-236 4.50e-10

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: 61.34  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  68 DIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGdqdlanvsarsrgvgmvfqnyalfphltvaENIAY-PlacQ 146
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------------------------LKISYkP---Q 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 147 KLpRAERKARVEEMLSLVRLKDYG------------------NRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:COG1245   409 YI-SPDYDGTVEEFLRSANTDDFGssyykteiikplglekllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1582545954 209 --------RALRfdlqvellHLQKTLGITTLIVTHD 236
Cdd:COG1245   488 veqrlavaKAIR--------RFAENRGKTAMVVDHD 515
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 65-208 7.32e-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: 61.11  E-value: 7.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   65 VAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqdlanvsarSRGVGMVFQNyALFPHLTVAENIAYPLA 144
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLRENILFGKA 724

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954  145 CQKlPRAERKARVEEMLSLVRLKDYGNRLP-----RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:TIGR00957  725 LNE-KYYQQVLEACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 62-256 8.78e-10

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 60.22  E-value: 8.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPK-NGRIELGDQDLANVS---ARSRGVGMVFQN---YALFPHLT 134
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpaqAIRAGIAMVPEDrkrHGIVPILG 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENI------AYPLACQKLPRAERKARVEEMLSLvRLKDYGNRLP-RELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:TIGR02633 356 VGKNItlsvlkSFCFKMRIDAAAELQIIGSAIQRL-KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1582545954 208 DRALRFDLqVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVE 256
Cdd:TIGR02633 435 DVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
PLN03232 PLN03232
ABC transporter C family member; Provisional
 65-272 1.05e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 60.76  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   65 VAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLAN--VSARSRGVGMVFQNYALFPHlTVAENIAyp 142
Cdd:PLN03232  1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFNID-- 1331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  143 lacqklPRAERK-ARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDra 210
Cdd:PLN03232  1332 ------PFSEHNdADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVD-- 1403

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954  211 LRFDLQVELLHLQKTLGITTLIVTHDQEEAQSlANRLVLMNKGNVEQIDTPMTVYDRPKTLF 272
Cdd:PLN03232  1404 VRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 46-260 1.30e-09

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: 58.71  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLTHSY--GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKnGRIELGDQDLANVSARS--RGVG 121
Cdd:cd03289     2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKwrKAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPHlTVAENIAyPLACQKlprAERKARVEEMlslVRLKDYGNRLPRE-----------LSGGQQQRVAVARA 190
Cdd:cd03289    81 VIPQKVFIFSG-TFRKNLD-PYGKWS---DEEIWKVAEE---VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARS 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 191 IAGRPSLLLLDEPFGALDralRFDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQIDT 260
Cdd:cd03289   153 VLSKAKILLLDEPSAHLD---PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 68-249 1.57e-09

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: 56.81  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  68 DIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELgdqDLANVSARSRGVgmvfqnyalfphltvaeniayplacqk 147
Cdd:cd03222    21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---DGITPVYKPQYI--------------------------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 148 lpraerkarveemlslvrlkdygnrlprELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQKTLG 227
Cdd:cd03222    71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122

                         170       180
                  ....*....|....*....|..
gi 1582545954 228 ITTLIVTHDQEEAQSLANRLVL 249
Cdd:cd03222   123 KTALVVEHDLAVLDYLSDRIHV 144
PLN03232 PLN03232
ABC transporter C family member; Provisional
 62-257 2.45e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 59.60  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGliqpkngriELGDQDLANVSARSrGVGMVFQNYALFpHLTVAENIAY 141
Cdd:PLN03232   633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSVVIRG-SVAYVPQVSWIF-NATVRENILF 701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  142 --PLACQKLPRAERKARVEEMLSLVRLKDYGNRLPR--ELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALR---FD 214
Cdd:PLN03232   702 gsDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAhqvFD 781

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1582545954  215 LQVEllhlQKTLGITTLIVThDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:PLN03232   782 SCMK----DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKE 819
PLN03130 PLN03130
ABC transporter C family member; Provisional
 65-261 8.19e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 57.83  E-value: 8.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   65 VAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFPHlTVAENIAyp 142
Cdd:PLN03130  1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFSG-TVRFNLD-- 1334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  143 lacqklPRAERK-ARVEEMLSLVRLKDYGNRLPREL-----------SGGQQQRVAVARAIAGRPSLLLLDEPFGALDra 210
Cdd:PLN03130  1335 ------PFNEHNdADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD-- 1406

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954  211 LRFDLQVellhlQKTL-----GITTLIVTH------DqeeaqslANRLVLMNKGNVEQIDTP 261
Cdd:PLN03130  1407 VRTDALI-----QKTIreefkSCTMLIIAHrlntiiD-------CDRILVLDAGRVVEFDTP 1456
PLN03073 PLN03073
ABC transporter F family; Provisional
 57-271 1.20e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 57.18  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  57 GGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIelgdqdlanvsARSRGVGMVFQNYALFPHLTVA 136
Cdd:PLN03073  520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVFSQHHVDGLDLS 588

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 137 EN-IAYPLACqkLPRA-ERKARVEemlsLVRLKDYGNRLPRE---LSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRAL 211
Cdd:PLN03073  589 SNpLLYMMRC--FPGVpEQKLRAH----LGSFGVTGNLALQPmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 212 RFDLQVELLHLQKtlGIttLIVTHDQEEAQSLANRLVLMNKGNVeqidTPM--TVYDRPKTL 271
Cdd:PLN03073  663 VEALIQGLVLFQG--GV--LMVSHDEHLISGSVDELWVVSEGKV----TPFhgTFHDYKKTL 716
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 61-257 2.38e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 56.05  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  61 AISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIEL-GDQDLANVSARSRGvgmvfqnyalfpHLTVAENI 139
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNG------------QLTGIENI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 140 AYPLACQKLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRfDLQVEL 219
Cdd:PRK13545  107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT-KKCLDK 185

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1582545954 220 LHLQKTLGITTLIVTHDQEEAQSLANRLVLMNKGNVEQ 257
Cdd:PRK13545  186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
PLN03140 PLN03140
ABC transporter G family member; Provisional
 72-210 3.04e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 56.01  E-value: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   72 GEIVALLGPSGCGKSTVLRAIAGliQPKNGRIElGDQDLANVSAR----SRGVGMVFQNYALFPHLTVAENIAYPlACQK 147
Cdd:PLN03140   906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKKqetfARISGYCEQNDIHSPQVTVRESLIYS-AFLR 981

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954  148 LPR---AERKAR----VEEMLSLVRLKDYGNRLP--RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD-RA 210
Cdd:PLN03140   982 LPKevsKEEKMMfvdeVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDaRA 1054
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 41-237 3.06e-08

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 54.26  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  41 MAERKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGliQPK----NGRIELGDQDLANVSAR 116
Cdd:CHL00131    2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SR---GVGMVFQNYALFPHLTVAE--NIAYplacqklpRAERKAR-------------VEEMLSLVRLKD-YGNRLPRE- 176
Cdd:CHL00131   80 ERahlGIFLAFQYPIEIPGVSNADflRLAY--------NSKRKFQglpeldplefleiINEKLKLVGMDPsFLSRNVNEg 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 177 LSGGQQQRVAVARAIAGRPSLLLLDEPFGALD-RALRfdlQV-ELLHLQKTLGITTLIVTHDQ 237
Cdd:CHL00131  152 FSGGEKKRNEILQMALLDSELAILDETDSGLDiDALK---IIaEGINKLMTSENSIILITHYQ 211
PTZ00243 PTZ00243
ABC transporter; Provisional
 64-256 6.62e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 54.78  E-value: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   64 DVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIelgdqdlanVSARSrgVGMVFQNyALFPHLTVAENIAY-- 141
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS--IAYVPQQ-AWIMNATVRGNILFfd 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  142 PLACQKLPRAERKARVEEMLSLVrlkdyGNRLPRE-------LSGGQQQRVAVARAIAGRPSLLLLDEPFGALDrALRFD 214
Cdd:PTZ00243   746 EEDAARLADAVRVSQLEADLAQL-----GGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD-AHVGE 819

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1582545954  215 LQVELLHLQKTLGITTLIVTHdQEEAQSLANRLVLMNKGNVE 256
Cdd:PTZ00243   820 RVVEECFLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE 860
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 100-208 1.08e-07

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 54.26  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  100 NGRIELGDQDLANVSARS-RGV-GMVFQNYALFpHLTVAENIAY---PLACQKLPRAERKARVEEMLSLVRLKDYGNRLP 174
Cdd:PTZ00265  1276 SGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFgkeDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1582545954  175 --RELSGGQQQRVAVARAIAGRPSLLLLDEPFGALD 208
Cdd:PTZ00265  1355 ygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
PLN03073 PLN03073
ABC transporter F family; Provisional
 24-238 2.95e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 52.55  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  24 SVTSTQNQGGPMLgipnmaerKRLSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLR-----AIAGLiqP 98
Cdd:PLN03073  163 YVNHDGNGGGPAI--------KDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--P 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  99 KNGRI------ELGDQ----------DLANVSARSRGVGMVFQNYAL-FPHLTVAENIAYPLACQKLPRAERKARVEEML 161
Cdd:PLN03073  233 KNCQIlhveqeVVGDDttalqcvlntDIERTQLLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQRLEEIYKRL 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 162 SLVRL-----------------KDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDLQVELLHLQK 224
Cdd:PLN03073  313 ELIDAytaearaasilaglsftPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392

                         250
                  ....*....|....
gi 1582545954 225 TLgittLIVTHDQE 238
Cdd:PLN03073  393 TF----IVVSHARE 402
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 47-208 4.30e-07

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 50.95  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGL--IQPKNGRIELGDQDLANVSARSR---GVG 121
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRageGIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYALFPhltvaeNIAYPLACQKLPRAERKARVEEMLSLVRLKDYGN------RLPREL---------SGGQQQRVA 186
Cdd:PRK09580   82 MAFQYPVEIP------GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRND 155

                         170       180
                  ....*....|....*....|..
gi 1582545954 187 VARAIAGRPSLLLLDEPFGALD 208
Cdd:PRK09580  156 ILQMAVLEPELCILDESDSGLD 177
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 62-253 4.63e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 51.85  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKN-GRIELGDQDL---ANVSARSRGVGMVFQN---YALFPHLT 134
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVkirNPQQAIAQGIAMVPEDrkrDGIVPVMG 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENIAYPlACQKLPR-------AERKARVEEMLSLvRLKDYGNRLP-RELSGGQQQRVAVARAIAGRPSLLLLDEPFGA 206
Cdd:PRK13549  358 VGKNITLA-ALDRFTGgsriddaAELKTILESIQRL-KVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582545954 207 LDRALRFDLQVELLHLQKTlGITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK13549  436 IDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 51-253 5.25e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.65  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  51 GLTHSYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSAR---SRGVGMVFQNY 127
Cdd:PRK10982    3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 128 ALFPHLTVAENI---AYPLAC-----QKLPRaERKARVEEMLSLVRlkdygnrlPRE----LSGGQQQRVAVARAIAGRP 195
Cdd:PRK10982   83 NLVLQRSVMDNMwlgRYPTKGmfvdqDKMYR-DTKAIFDELDIDID--------PRAkvatLSVSQMQMIEIAKAFSYNA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582545954 196 SLLLLDEPFGALDralrfdlQVELLHLQKTL------GITTLIVTHDQEEAQSLANRLVLMNKG 253
Cdd:PRK10982  154 KIVIMDEPTSSLT-------EKEVNHLFTIIrklkerGCGIVYISHKMEEIFQLCDEITILRDG 210
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
45-236 6.52e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 49.62  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  45 KRLSVQGLThSYGGQNAIsdvafDIEAGeIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARSRGVGMVF 124
Cdd:COG0419     3 LRLRLENFR-SYRDTETI-----DFDDG-LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 125 QN----YALF-PHLTVAENIayplacqKLPRAERKARVEEMLSLVRLKDYGNRL-------------------------- 173
Cdd:COG0419    76 EHggkrYRIErRQGEFAEFL-------EAKPSERKEALKRLLGLEIYEELKERLkeleealesaleelaelqklkqeila 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 174 -------PRELSGGQQQRVAVARAIAgrpslLLLDepFGALDRAlRFDLQVELLHLQKtlgittlIVTHD 236
Cdd:COG0419   149 qlsgldpIETLSGGERLRLALADLLS-----LILD--FGSLDEE-RLERLLDALEELA-------IITHV 203
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 66-233 7.44e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 51.17  E-value: 7.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  66 AFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVS--ARSRGVGMVFQ---NYALFPH-----LTV 135
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeQLQKLVSDEWQrnnTDMLSPGeddtgRTT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 136 AENIayplacqkLPRAERKARVEEMLSLVRLKDYGNRLPRELSGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFDL 215
Cdd:PRK10938  103 AEII--------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174

                         170
                  ....*....|....*...
gi 1582545954 216 QvELLHLQKTLGITTLIV 233
Cdd:PRK10938  175 A-ELLASLHQSGITLVLV 191
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 46-250 8.01e-06

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 46.49  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  46 RLSVQGLtHSYGGQNAISdvaF-DIEAGEIVALLGPSGCGKSTVLRAIAGLI---QPKNGRIELGDQDLANVSARSRgVG 121
Cdd:cd03279     5 KLELKNF-GPFREEQVID---FtGLDNNGLFLICGPTGAGKSTILDAITYALygkTPRYGRQENLRSVFAPGEDTAE-VS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 122 MVFQNYalfphltvaeniayplacQKLPRAERKARVEE-------MLSLVRLKDYGNRLPRELSGGQQQRVAVARAIA-- 192
Cdd:cd03279    80 FTFQLG------------------GKKYRVERSRGLDYdqftrivLLPQGEFDRFLARPVSTLSGGETFLASLSLALAls 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582545954 193 --------GRPSLLLLDEPFGALDRALRfDLQVELLHLQKTLGITTLIVTHDQEEAQSLANRLVLM 250
Cdd:cd03279   142 evlqnrggARLEALFIDEGFGTLDPEAL-EAVATALELIRTENRMVGVISHVEELKERIPQRLEVI 206
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 69-272 8.49e-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: 8.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  69 IEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANV---SARSRgVGMVFQNYALFPHlTVAENIAYPLAC 145
Cdd:cd03288    44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-LSIILQDPILFSG-SIRFNLDPECKC 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 146 QKlpraerkARVEEMLSLVRLKDYGNRLPREL-----------SGGQQQRVAVARAIAGRPSLLLLDEPFGALDRALRFD 214
Cdd:cd03288   122 TD-------DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 215 LQ--VELLHLQKTLGITTLIVTHDQEeaqslANRLVLMNKGNVEQIDTPMTVYDRPKTLF 272
Cdd:cd03288   195 LQkvVMTAFADRTVVTIAHRVSTILD-----ADLVLVLSRGILVECDTPENLLAQEDGVF 249
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 62-261 2.13e-05

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: 46.86  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   62 ISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANV---SARSRgVGMVFQNYALFPHlTVAEN 138
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglhDLRFK-ITIIPQDPVLFSG-SLRMN 1379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  139 IAyPLAcqklprAERKARVEEMLSLVRLKDYGNRLP-----------RELSGGQQQRVAVARAIAGRPSLLLLDEPFGAL 207
Cdd:TIGR00957 1380 LD-PFS------QYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582545954  208 dralrfDLQVELLhLQKTL-----GITTLIVTHDQEEAQSLaNRLVLMNKGNVEQIDTP 261
Cdd:TIGR00957 1453 ------DLETDNL-IQSTIrtqfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAP 1503
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 55-247 2.94e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.16  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAIAGliqpkngrielgD--QDLAN---VSARSRG---------- 119
Cdd:PRK10938  269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DhpQGYSNdltLFGRRRGsgetiwdikk 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 120 -VGMVFQNYalfpHL-----TVAENI----------AYplacQKLPRAERKaRVEEMLSLVRLKDYGNRLP-RELSGGQQ 182
Cdd:PRK10938  337 hIGYVSSSL----HLdyrvsTSVRNVilsgffdsigIY----QAVSDRQQK-LAQQWLDILGIDKRTADAPfHSLSWGQQ 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582545954 183 QRVAVARAIAGRPSLLLLDEPFGALD---RAL--RFdlqVELLHLQktlGITTLI-VTHDQEEA-QSLANRL 247
Cdd:PRK10938  408 RLALIVRALVKHPTLLILDEPLQGLDplnRQLvrRF---VDVLISE---GETQLLfVSHHAEDApACITHRL 473
PTZ00243 PTZ00243
ABC transporter; Provisional
 65-272 1.47e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 44.38  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954   65 VAFDIEAGEIVALLGPSGCGKSTVLRAIAGLIQPKNGRIELGDQDLANVSARS--RGVGMVFQNYALFPHlTVAENIAyp 142
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVD-- 1405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  143 lacqklPRAE-RKARVEEMLSLVRLKDygnRLPRELSG--------------GQQQRVAVARAIAGRPS-LLLLDEPFGA 206
Cdd:PTZ00243  1406 ------PFLEaSSAEVWAALELVGLRE---RVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSgFILMDEATAN 1476

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582545954  207 LDRALrfDLQVELLHLQKTLGITTLIVTHD-QEEAQslANRLVLMNKGNVEQIDTPMTVYDRPKTLF 272
Cdd:PTZ00243  1477 IDPAL--DRQIQATVMSAFSAYTVITIAHRlHTVAQ--YDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 55-238 2.71e-04

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: 41.19  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  55 SYGGQNaisDVAFDieAGEIVALLGPSGCGKSTVLRAIaGLIqpkngrielgdqdlanvsarsrgVGMVFQNYALFPHLT 134
Cdd:cd03227     9 SYFVPN---DVTFG--EGSLTIITGPNGSGKSTILDAI-GLA-----------------------LGGAQSATRRRSGVK 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 135 VAENIAYPlacqklpraerkaRVEEMLSLVRLkdygnrlprelSGGQQQRVAVARAIA----GRPSLLLLDEPFGALD-- 208
Cdd:cd03227    60 AGCIVAAV-------------SAELIFTRLQL-----------SGGEKELSALALILAlaslKPRPLYILDEIDRGLDpr 115

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1582545954 209 --RALrfdLQVELLHLQKtlGITTLIVTHDQE 238
Cdd:cd03227   116 dgQAL---AEAILEHLVK--GAQVIVITHLPE 142
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 324-396 6.34e-04

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: 37.98  E-value: 6.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582545954 324 RPEEVRLSTQpsESTLPVRMTVSVPLGPSLVHDLALEDGTGLRASeVRGPSTFIPEPGTPLFAEIDTARCHAF 396
Cdd:pfam08402   4 RPEKIRLAAA--ANGLSGTVTDVEYLGDHTRYHVELAGGEELVVR-VPNAHARPPAPGDRVGLGWDPEDAHVL 73
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 64-253 7.51e-04

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 40.70  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  64 DVAFDIEAGEIVALLGPSGCGKSTV--------------------LRAIAGLIQ-PKNGRIE-LG-----DQDLANVSAR 116
Cdd:cd03270    13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayARQFLGQMDkPDVDSIEgLSpaiaiDQKTTSRNPR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 117 SRgVGMVFQNYALFPHLTVAENIayplacqklpraerKARVEEMLSlVRLkDY--GNRLPRELSGGQQQRVAVARAIAGR 194
Cdd:cd03270    93 ST-VGTVTEIYDYLRLLFARVGI--------------RERLGFLVD-VGL-GYltLSRSAPTLSGGEAQRIRLATQIGSG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 195 PS--LLLLDEPFGALDRALRFDLqVELLHLQKTLGITTLIVTHDqEEAQSLANRLVLMNKG 253
Cdd:cd03270   156 LTgvLYVLDEPSIGLHPRDNDRL-IETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIGPG 214
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 47-253 8.16e-04

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: 40.00  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954  47 LSVQGLTHsyggqNAISDVAFDIEAGEIVALLGPSGCGKSTVLRAiaGLIQPKNGRIelgdqdlanVSARSRgvgmvfqn 126
Cdd:cd03238     1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYASGKARL---------ISFLPK-------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 127 yaLFPHLTVAeniayplacqklpraerkarveeMLSLVRLKDYG------NRLPRELSGGQQQRVAVARAIAGRP--SLL 198
Cdd:cd03238    57 --FSRNKLIF-----------------------IDQLQFLIDVGlgyltlGQKLSTLSGGELQRVKLASELFSEPpgTLF 111

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582545954 199 LLDEPFGALDralrfdlQVELLHLQKTL------GITTLIVTHDqEEAQSLANRLVLMNKG 253
Cdd:cd03238   112 ILDEPSTGLH-------QQDINQLLEVIkglidlGNTVILIEHN-LDVLSSADWIIDFGPG 164
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 171-253 2.11e-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: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582545954 171 NRLPRELSGGQQQRVAVARAIAGRPS--LLLLDEPFGALDRALRFDLQVELLHLQKtLGITTLIVTHDqEEAQSLANRLV 248
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHD-EDTIRAADYVI 560


                  ....*
gi 1582545954 249 LMNKG 253
Cdd:TIGR00630 561 DIGPG 565
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 56-103 3.88e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 37.51  E-value: 3.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582545954  56 YGGQNAISDVAFDIEAGE--IVALLGPSGCGKSTVLRAIAGLIQPKNGRI 103
Cdd:cd00009     1 VGQEEAIEALREALELPPpkNLLLYGPPGTGKTTLARAIANELFRPGAPF 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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