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Conserved domains on  [gi|1219505750|ref|WP_089460196|]
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ABC transporter ATP-binding protein [Burkholderia sp. AU33647]

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 ...
 20-378 0e+00

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 547.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQ 99
Cdd:COG3842     5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:COG3842    85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEG 259
Cdd:COG3842   165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 260 RVVEDEPDHIFVESDDLEarmyVSHGITGPLGMPVGISVRPERIHVSREKPgskHNWARGVVTDIAYMGSYSLYHVRLPS 339
Cdd:COG3842   245 TVLGDEGGGVRTGGRTLE----VPADAGLAAGGPVTVAIRPEDIRLSPEGP---ENGLPGTVEDVVFLGSHVRYRVRLGD 317

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1219505750 340 GKTVVSNLSSSHlmnDNAPAWNDDVFVSWSPASGVVLTQ 378
Cdd:COG3842   318 GQELVVRVPNRA---ALPLEPGDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-378 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 547.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQ 99
Cdd:COG3842     5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:COG3842    85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEG 259
Cdd:COG3842   165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 260 RVVEDEPDHIFVESDDLEarmyVSHGITGPLGMPVGISVRPERIHVSREKPgskHNWARGVVTDIAYMGSYSLYHVRLPS 339
Cdd:COG3842   245 TVLGDEGGGVRTGGRTLE----VPADAGLAAGGPVTVAIRPEDIRLSPEGP---ENGLPGTVEDVVFLGSHVRYRVRLGD 317

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1219505750 340 GKTVVSNLSSSHlmnDNAPAWNDDVFVSWSPASGVVLTQ 378
Cdd:COG3842   318 GQELVVRVPNRA---ALPLEPGDRVGLSWDPEDVVVLPA 353
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
23-377 0e+00

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 513.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYA 102
Cdd:PRK11607   22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK11607  102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 183 KKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGRVV 262
Cdd:PRK11607  182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLK 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 263 EDEPDHIFVESDDLEARMYVSHGITGPLGMPVGISVRPERIHVSREKPGSKHNWARGVVTDIAYMGSYSLYHVRLPSGKT 342
Cdd:PRK11607  262 ERQEDGLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVIHIAYLGDLSIYHVRLKSGQM 341

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1219505750 343 VVSNLSSSHLMNDNAPAWNDDVFVSWSPASGVVLT 377
Cdd:PRK11607  342 ISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVLT 376
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 51-376 2.13e-142

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: 407.26  E-value: 2.13e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  51 LLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKER 130
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 131 VADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHD 210
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 211 QEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGRVVEDEPDHiFVESDDLEARMYVSHGITGPL 290
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQ-VVLAGVEGRRCDIYTDVPVEK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 291 GMPVGISVRPERIHVSREKPGSKHNWARGVVTDIAYMGSYSLYHVRLPSGKTVvsnLSSSHLMNDN---APAWNDDVFVS 367
Cdd:TIGR01187 240 DQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKV---LVSEFFNEDDphmSPSIGDRVGLT 316


                  ....*....
gi 1219505750 368 WSPASGVVL 376
Cdd:TIGR01187 317 WHPGSEVVL 325
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 21-252 3.07e-136

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: 387.75  E-value: 3.07e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIG 252
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
21-353 1.48e-91

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 278.50  E-value: 1.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDsTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:NF040840    2 IRIENLSKDWKE-FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGr 260
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEG- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 261 VVEDEPDHIFVESDDLeaRMYVSHGITGplgmPVGISVRPERIHVSREKPG-SKHNWARGVVTDIAYMGsySLYHVRLPS 339
Cdd:NF040840  240 VAEKGGEGTILDTGNI--KIELPEEKKG----KVRIGIRPEDITISTEKVKtSARNEFKGKVEEIEDLG--PLVKLTLDV 311

                         330
                  ....*....|....
gi 1219505750 340 GKTVVSNLSSSHLM 353
Cdd:NF040840  312 GIILVAFITRSSFL 325
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 36-177 5.77e-50

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: 164.74  E-value: 5.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--ASLPPYRRPVNMMFQSYALFPHMTVESNV 113
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 114 AFGLKQEGTPKNEIKERVADALALVQMSKYAQRK----PHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
21-229 3.73e-49

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 165.28  E-value: 3.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVK----KFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPpY------ 90
Cdd:NF038007    2 LNMQNAEKcyitKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-Ysqkiil 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 -RRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:NF038007   81 rRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 170 KLLLLDEPMSALDKKiRQKTQLELVNIIEKVDVTCVMVTHDQeEAMTMASRLAVMSEGKI 229
Cdd:NF038007  161 ALLLADEPTGNLDSK-NARAVLQQLKYINQKGTTIIMVTHSD-EASTYGNRIINMKDGKL 218
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-182 7.62e-34

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 132.94  E-value: 7.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSG--KIF---VDGEDLASlppyRRPVNMMF 98
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWLFgqpVDAGDIAT----RRRVGYMS 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVA-----FGLkqegtPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:NF033858  346 QAFSLYGELTVRQNLElharlFHL-----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420


                  ....*....
gi 1219505750 174 LDEPMSALD 182
Cdd:NF033858  421 LDEPTSGVD 429
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
30-215 5.86e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 119.26  E-value: 5.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  30 FGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNmmfqsyALFPhMTV 109
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAFGLKQE----GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:NF040873   75 RDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1219505750 186 RQKTqLELVNIIEKVDVTCVMVTHDQEEAM 215
Cdd:NF040873  155 RERI-IALLAEEHARGATVVVVTHDLELVR 183
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-240 1.97e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 87.10  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASlPPYRRPV------ 94
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVcpriay 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 -------NmmfqsyaLFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVK 167
Cdd:NF033858   81 mpqglgkN-------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 168 RPKLLLLDEPMSALDKKIRQktQL-ELVNII--EKVDVTcVMV-THDQEEamtmASR---LAVMSEGKIVQIGAPGEVYE 240
Cdd:NF033858  154 DPDLLILDEPTTGVDPLSRR--QFwELIDRIraERPGMS-VLVaTAYMEE----AERfdwLVAMDAGRVLATGTPAELLA 226
GguA NF040905
sugar ABC transporter ATP-binding protein;
25-231 2.17e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 83.30  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATS--GKIFVDGE-----DLASlpPYRRPVNMM 97
Cdd:NF040905    6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD--SEALGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGlkqegtpkNEIK-----------ERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:NF040905   84 HQELALIPYLSIAENIFLG--------NERAkrgvidwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQ 231
Cdd:NF040905  156 KDVKLLILDEPTAALNEEDSAAL-LDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 45-223 7.16e-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: 65.47  E-value: 7.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   45 KNELFALLGSSGCGKSTLLRMLAGLETATSGK-IFVDGEDLaslppyrrpvnmmfqsyalfphmtvesnvafglkqegtp 123
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDI--------------------------------------- 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  124 kneikervADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLE-----LVNIIE 198
Cdd:smart00382  42 --------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKS 113

                          170       180
                   ....*....|....*....|....*
gi 1219505750  199 KVDVTCVMVTHDQEEAMTMASRLAV 223
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRF 138
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
21-238 1.08e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 68.61  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCG--KSTLLRMLAGLETATSGKIF----VDGEDLASLPPYRRPV 94
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*twcANRRALRRTIG*HRPV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSyalfpHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:NF000106   94 R*GRRE-----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 175 DEPMSALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:NF000106  169 DEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
GguA NF040905
sugar ABC transporter ATP-binding protein;
151-238 1.89e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 46.32  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 151 LSGGQQQRVALARSLVKRPKLLLLDEPMSALD---KkirqktqLELVNIIEKVDVT---CVMVTHDQEEAMTMASRLAVM 224
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgaK-------YEIYTIINELAAEgkgVIVISSELPELLGMCDRIYVM 477

                          90
                  ....*....|....
gi 1219505750 225 SEGKIVqigapGEV 238
Cdd:NF040905  478 NEGRIT-----GEL 486
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-378 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 547.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQ 99
Cdd:COG3842     5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:COG3842    85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEG 259
Cdd:COG3842   165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 260 RVVEDEPDHIFVESDDLEarmyVSHGITGPLGMPVGISVRPERIHVSREKPgskHNWARGVVTDIAYMGSYSLYHVRLPS 339
Cdd:COG3842   245 TVLGDEGGGVRTGGRTLE----VPADAGLAAGGPVTVAIRPEDIRLSPEGP---ENGLPGTVEDVVFLGSHVRYRVRLGD 317

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1219505750 340 GKTVVSNLSSSHlmnDNAPAWNDDVFVSWSPASGVVLTQ 378
Cdd:COG3842   318 GQELVVRVPNRA---ALPLEPGDRVGLSWDPEDVVVLPA 353
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
23-377 0e+00

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 513.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYA 102
Cdd:PRK11607   22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK11607  102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 183 KKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGRVV 262
Cdd:PRK11607  182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLK 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 263 EDEPDHIFVESDDLEARMYVSHGITGPLGMPVGISVRPERIHVSREKPGSKHNWARGVVTDIAYMGSYSLYHVRLPSGKT 342
Cdd:PRK11607  262 ERQEDGLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVIHIAYLGDLSIYHVRLKSGQM 341

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1219505750 343 VVSNLSSSHLMNDNAPAWNDDVFVSWSPASGVVLT 377
Cdd:PRK11607  342 ISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVLT 376
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 21-371 8.33e-148

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 421.79  E-value: 8.33e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:COG3839     4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:COG3839    84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGS--TNLFE 258
Cdd:COG3839   164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 259 GRVVEDEpdhifVESDDLeaRMYVSHGITGPLGMPVGISVRPERIHVSREKPGSkhnwARGVVTDIAYMGSYSLYHVRLP 338
Cdd:COG3839   244 GTVEGGG-----VRLGGV--RLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGG----LEATVEVVEPLGSETLVHVRLG 312

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1219505750 339 sGKTVVSNLSSSHlmndnAPAWNDDVFVSWSPA 371
Cdd:COG3839   313 -GQELVARVPGDT-----RLRPGDTVRLAFDPE 339
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 51-376 2.13e-142

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: 407.26  E-value: 2.13e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  51 LLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKER 130
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 131 VADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHD 210
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 211 QEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGRVVEDEPDHiFVESDDLEARMYVSHGITGPL 290
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQ-VVLAGVEGRRCDIYTDVPVEK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 291 GMPVGISVRPERIHVSREKPGSKHNWARGVVTDIAYMGSYSLYHVRLPSGKTVvsnLSSSHLMNDN---APAWNDDVFVS 367
Cdd:TIGR01187 240 DQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKV---LVSEFFNEDDphmSPSIGDRVGLT 316


                  ....*....
gi 1219505750 368 WSPASGVVL 376
Cdd:TIGR01187 317 WHPGSEVVL 325
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 21-252 3.07e-136

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: 387.75  E-value: 3.07e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIG 252
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
21-376 3.21e-135

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 390.85  E-value: 3.21e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGR 260
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 261 VVED-EPDHIFVESDDLEARMYVSHGITGplGMPVGISVRPERIHVSREKPGSKHNWARGVVTDIAYMGSYSLYHVRLPS 339
Cdd:PRK09452  255 VIERlDEQRVRANVEGRECNIYVNFAVEP--GQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYKGMTLDSVVELEN 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1219505750 340 GKTVVsnlsSSHLMNDNAPAWNDD----VFVSWSPASGVVL 376
Cdd:PRK09452  333 GKMVM----VSEFFNEDDPDFDHSlgqkVAVTWVEGWEVVL 369
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 21-371 2.20e-134

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 387.58  E-value: 2.20e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS-LPPYRRPVNMMFQ 99
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERRVGFVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:COG1118    83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEG 259
Cdd:COG1118   163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 260 RVVEdepDHIFVESDDLEARMYVSHGitgplgmPVGISVRPERIHVSREKPGSkhNWARGVVTDIAYMGSYSLYHVRL-- 337
Cdd:COG1118   243 RVIG---GQLEADGLTLPVAEPLPDG-------PAVAGVRPHDIEVSREPEGE--NTFPATVARVSELGPEVRVELKLed 310

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1219505750 338 PSGKTVVSNLSSSHLMNDNaPAWNDDVFVSWSPA 371
Cdd:COG1118   311 GEGQPLEAEVTKEAWAELG-LAPGDPVYLRPRPA 343
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 20-350 2.39e-124

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


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 362.43  E-value: 2.39e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQ 99
Cdd:TIGR03265   4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:TIGR03265  84 SYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEG 259
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 260 RVVEDEPDHIFvesddlEARMYVSHGITGPlGMPVGISVRPERIHVSreKPGSKHNWARGVVTDIAYMGSYSLYHVRLPS 339
Cdd:TIGR03265 244 TRGGGSRARVG------GLTLACAPGLAQP-GASVRLAVRPEDIRVS--PAGNAANLLLARVEDMEFLGAFYRLRLRLEG 314

                         330
                  ....*....|...
gi 1219505750 340 --GKTVVSNLSSS 350
Cdd:TIGR03265 315 lpGQALVADVSAS 327
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 21-233 1.56e-117

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: 339.88  E-value: 1.56e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 21-233 5.37e-106

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 310.34  E-value: 5.37e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 21-253 3.72e-104

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: 306.57  E-value: 3.72e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLK----QEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:cd03296    83 YALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 177 PMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGS 253
Cdd:cd03296   163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
20-352 3.78e-104

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 310.88  E-value: 3.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQ 99
Cdd:PRK11432    6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:PRK11432   86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEG 259
Cdd:PRK11432  166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 260 RVVEDEPDhIF---VESDDLEARMYVSHGITgplgmpVGisVRPERIHVSREKPGSKhnwaRGVVTDIAYMGSYslYHVR 336
Cdd:PRK11432  246 TLSGDYVD-IYgyrLPRPAAFAFNLPDGECT------VG--VRPEAITLSEQGEESQ----RCTIKHVAYMGPQ--YEVT 310

                         330
                  ....*....|....*..
gi 1219505750 337 LP-SGKTVVSNLSSSHL 352
Cdd:PRK11432  311 VDwHGQELLLQVNATQL 327
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
21-345 1.33e-98

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 296.75  E-value: 1.33e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF-GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQ 99
Cdd:PRK11650    4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:PRK11650   84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGS--TNLF 257
Cdd:PRK11650  164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 258 EGRVvedEPDHIFVE-SDDLEARMYVSHGITGPLGMPVGIsvRPERIHVSREKPGskhnwARGVVTDIAYMGSYSLYHVR 336
Cdd:PRK11650  244 DGRV---SADGAAFElAGGIALPLGGGYRQYAGRKLTLGI--RPEHIALSSAEGG-----VPLTVDTVELLGADNLAHGR 313


                  ....*....
gi 1219505750 337 LPSGKTVVS 345
Cdd:PRK11650  314 WGGQPLVVR 322
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 20-232 9.15e-98

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 291.22  E-value: 9.15e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKF----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRpvn 95
Cdd:COG1116     7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:COG1116    84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 176 EPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSE--GKIVQI 232
Cdd:COG1116   164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 21-255 5.65e-96

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 285.93  E-value: 5.65e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTN 255
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 21-232 5.55e-95

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: 282.44  E-value: 5.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS----TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPyrrPVNM 96
Cdd:cd03293     1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 177 PMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSE--GKIVQI 232
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 22-253 7.99e-93

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 280.44  E-value: 7.99e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY--RRpvNMMF 98
Cdd:COG1125     3 EFENVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelRR--RIGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 --QSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQM--SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:COG1125    81 viQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 175 DEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGS 253
Cdd:COG1125   161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
21-353 1.48e-91

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 278.50  E-value: 1.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDsTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:NF040840    2 IRIENLSKDWKE-FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGr 260
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEG- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 261 VVEDEPDHIFVESDDLeaRMYVSHGITGplgmPVGISVRPERIHVSREKPG-SKHNWARGVVTDIAYMGsySLYHVRLPS 339
Cdd:NF040840  240 VAEKGGEGTILDTGNI--KIELPEEKKG----KVRIGIRPEDITISTEKVKtSARNEFKGKVEEIEDLG--PLVKLTLDV 311

                         330
                  ....*....|....
gi 1219505750 340 GKTVVSNLSSSHLM 353
Cdd:NF040840  312 GIILVAFITRSSFL 325
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
21-341 5.43e-91

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 278.07  E-value: 5.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:PRK11000    4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:PRK11000   84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGS--TNLFE 258
Cdd:PRK11000  164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSpkMNFLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 259 GRVVEDEPDHIFVE-SDDLEARMYVShGITGPLGMPVGISVRPERIHVSREKPGSKHnwarGVVTDIAYMGSYSLYHVRL 337
Cdd:PRK11000  244 VKVTATAIEQVQVElPNRQQVWLPVE-GRGVQVGANMSLGIRPEHLLPSDIADVTLE----GEVQVVEQLGNETQIHIQI 318


                  ....
gi 1219505750 338 PSGK 341
Cdd:PRK11000  319 PAIR 322
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 21-257 3.27e-88

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: 266.09  E-value: 3.27e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMM 97
Cdd:cd03295     1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPveLRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQM--SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 176 EPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTN 255
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240


                  ..
gi 1219505750 256 LF 257
Cdd:cd03295   241 LL 242
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 21-343 8.50e-87

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: 266.86  E-value: 8.50e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETA--TSGKIFVDGEDLASLPPYRRPVNMMF 98
Cdd:TIGR03258   6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKRGLALLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:TIGR03258  86 QNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 179 SALDKKIRQKTQLELVNIIEKV-DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLF 257
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 258 E--GRVVEDEPDHIFVESDDLEARMYV--SHGITGPLgmpvgISVRPERIHVSREKPGSkhNWARGVVTDIAYMGSYSLY 333
Cdd:TIGR03258 246 PaiALGITEAPGLVDVSCGGAVIFAFGdgRHDGRDKL-----ACIRPEHLALTPRPAGE--GRFHATIASVEWHGAALHL 318

                         330
                  ....*....|
gi 1219505750 334 HVRLPSGKTV 343
Cdd:TIGR03258 319 LCDLDAACDE 328
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
21-261 6.89e-86

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 264.25  E-value: 6.89e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLK----QEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:PRK10851   83 YALFRHMTVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 177 PMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNL 256
Cdd:PRK10851  163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242


                  ....*
gi 1219505750 257 FEGRV 261
Cdd:PRK10851  243 LQGTI 247
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 21-256 5.45e-84

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: 255.34  E-value: 5.45e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDsTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03299     1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNL 256
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 24-251 2.28e-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: 249.87  E-value: 2.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------YRRPVNMM 97
Cdd:cd03294    28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03294   108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 178 MSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:cd03294   188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
21-254 5.12e-78

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 243.45  E-value: 5.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YR 91
Cdd:COG1135     2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 172 LLLDEPMSALD-----------KKIRQKTQLelvniiekvdvTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG1135   162 LLCDEATSALDpettrsildllKDINRELGL-----------TIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230

                         250
                  ....*....|....
gi 1219505750 241 FPNSRFSAEFIGST 254
Cdd:COG1135   231 NPQSELTRRFLPTV 244
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 28-264 1.22e-77

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


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 243.61  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  28 KKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------YRRPVNMMFQSY 101
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 182 DKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGRV 261
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240


                  ...
gi 1219505750 262 VED 264
Cdd:TIGR01186 241 AER 243
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 21-244 1.51e-77

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 238.74  E-value: 1.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL----ASLPPYRRPVNM 96
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFGLKQ-EGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 176 EPMSALDKkirqktqlELVNIIEKV-------DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNS 244
Cdd:COG1126   162 EPTSALDP--------ELVGEVLDVmrdlakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 21-245 4.23e-77

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: 237.57  E-value: 4.23e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PYRRPVN 95
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyELRRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHMTVESNVAFGLKQEGT-PKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:COG1127    86 MLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 175 DEPMSALDKkirqKTQLELVNII----EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSR 245
Cdd:COG1127   166 DEPTAGLDP----ITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPW 236
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
22-252 5.89e-77

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 236.96  E-value: 5.89e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAvdNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSY 101
Cdd:COG3840     3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV-KRPkLLLLDEPMSA 180
Cdd:COG3840    81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 181 LDKKIRQKtQLELVN-IIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIG 252
Cdd:COG3840   160 LDPALRQE-MLDLVDeLCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 21-228 3.40e-76

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 233.23  E-value: 3.40e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASL----PPYRRPVNM 96
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFGlkqegtpkneikervadalalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 177 PMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGK 228
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 21-240 3.79e-75

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: 232.22  E-value: 3.79e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--ASLPPYRRPVNMM 97
Cdd:COG1122     1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQS--YALFpHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:COG1122    81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 176 EPMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG1122   160 EPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 21-242 2.86e-74

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: 239.42  E-value: 2.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF-----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PY 90
Cdd:COG1123   261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrslrEL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 RRPVNMMFQ--SYALFPHMTVESNVAFGLKQEGT-PKNEIKERVADALALVQMS-KYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:COG1123   341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 167 KRPKLLLLDEPMSALDKKIrqktQLELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:COG1123   421 LEPKLLILDEPTSALDVSV----QAQILNLLRDLqrelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
21-230 2.92e-74

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 229.93  E-value: 2.92e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS----TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YR 91
Cdd:COG1136     5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelarLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 R-PVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:COG1136    85 RrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 171 LLLLDEPMSALDkkirQKTQLELVNIIEKV----DVTCVMVTHDqEEAMTMASRLAVMSEGKIV 230
Cdd:COG1136   165 LILADEPTGNLD----SKTGEEVLELLRELnrelGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
21-237 9.46e-74

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 228.40  E-value: 9.46e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS-TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASL-----PPYRRPV 94
Cdd:COG2884     2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreiPYLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 175 DEPMSALDkkirQKTQLELVNIIE---KVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGE 237
Cdd:COG2884   162 DEPTGNLD----PETSWEIMELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
21-238 3.22e-73

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 227.64  E-value: 3.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQ 99
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAF--GLKqeGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:COG1131    81 EPALYPDLTVRENLRFfaRLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 178 MSALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG1131   159 TSGLDPEARR----ELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 21-245 3.94e-72

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: 224.69  E-value: 3.94e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY-----RRPVN 95
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHMTVESNVAFGLKQEGT-PKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 175 DEPMSALDKkirqKTQLELVNII----EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSR 245
Cdd:cd03261   161 DEPTAGLDP----IASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 21-233 4.44e-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: 221.40  E-value: 4.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIEnvvKKFGDSTAvdNVNLTIaKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS------LPPYRRPV 94
Cdd:cd03297     4 VDIE---KRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFGLKqeGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:cd03297    78 GLVFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 175 DEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03297   156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 21-229 1.34e-70

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: 220.44  E-value: 1.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGD----STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------Y 90
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 RRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:cd03255    81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 171 LLLLDEPMSALDkkirQKTQLELVNIIEKV----DVTCVMVTHDQEEAMtMASRLAVMSEGKI 229
Cdd:cd03255   161 IILADEPTGNLD----SETGKEVMELLRELnkeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 21-260 3.20e-70

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: 220.44  E-value: 3.20e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFG----DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--ASLPPYRRPV 94
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrRRRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSY--ALFPHMTVESNVAFGLKQEGTPknEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 172 LLLDEPMSALDkkirQKTQLELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFS 247
Cdd:COG1124   160 LLLDEPTSALD----VSVQAEILNLLKDLreerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235

                         250
                  ....*....|...
gi 1219505750 248 AEFIGSTNLFEGR 260
Cdd:COG1124   236 RELLAASLAFERA 248
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 38-325 5.09e-70

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: 223.44  E-value: 5.09e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS------LPPYRRPVNMMFQSYALFPHMTVES 111
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 112 NVAFGLKQegTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQL 191
Cdd:COG4148    97 NLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 192 ELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGSTNLFEGRVVEDEPDHIFV 271
Cdd:COG4148   175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGLT 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 272 ESDDLEARMYVSHgITGPLGMPVGISVRPERIHVSREKPG--SKHNWARGVVTDIA 325
Cdd:COG4148   255 RLALGGGRLWVPR-LDLPPGTRVRVRIRARDVSLALEPPEgsSILNILPGRVVEIE 309
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 21-242 1.46e-69

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 218.22  E-value: 1.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS----TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL-----ASLPPYR 91
Cdd:cd03258     2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 172 LLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 22-228 3.85e-67

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: 211.17  E-value: 3.85e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMM 97
Cdd:cd03225     1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkeLRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQsyalFP-HM----TVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLL 172
Cdd:cd03225    81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 173 LLDEPMSALDkkirQKTQLELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGK 228
Cdd:cd03225   157 LLDEPTAGLD----PAGRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 21-233 2.16e-66

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 209.67  E-value: 2.16e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PYR 91
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSY--ALFPHMTVESNVAFGLK--QEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLV 166
Cdd:cd03257    82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 21-254 9.65e-66

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 211.97  E-value: 9.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YR 91
Cdd:PRK11153    2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:PRK11153   82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 172 LLLDEPMSALDKkirQKTQ--LELV-NIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSA 248
Cdd:PRK11153  162 LLCDEATSALDP---ATTRsiLELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238


                  ....*.
gi 1219505750 249 EFIGST 254
Cdd:PRK11153  239 EFIQST 244
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 21-239 1.39e-65

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: 209.21  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS---LPPYRRPVN 95
Cdd:TIGR04520   1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSyalfPH-----MTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:TIGR04520  81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 171 LLLLDEPMSALDKKIRQktqlELVNIIEKV----DVTCVMVTHDQEEAmTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:TIGR04520 157 IIILDEATSMLDPKGRK----EVLETIRKLnkeeGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 21-229 3.38e-64

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: 203.53  E-value: 3.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL----ASLPPYRRPVNM 96
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFGLKQ-EGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 176 EPMSALDKkirqktqlELVNiiEKVDV---------TCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:cd03262   161 EPTSALDP--------ELVG--EVLDVmkdlaeegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
35-248 2.02e-63

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 203.56  E-value: 2.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASlPPYRRPVnmMFQSYALFPHMTVESNVA 114
Cdd:COG4525    22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDNVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 115 FGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELV 194
Cdd:COG4525    99 FGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 195 NIIEKVDVTCVMVTHDQEEAMTMASRLAVMS--EGKIVqigapgEVYEFP-NSRFSA 248
Cdd:COG4525   179 DVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIV------ERLELDfSRRFLA 229
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 21-238 2.75e-63

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: 202.58  E-value: 2.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMF 98
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRreLARRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFG----LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:COG1120    82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 175 DEPMSALDkkIRQktQLELVNII----EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG1120   162 DEPTSHLD--LAH--QLEVLELLrrlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 21-238 1.88e-62

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 200.28  E-value: 1.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF-GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YRRPV 94
Cdd:COG3638     3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFG-LKQEGTPKN-------EIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVLAGrLGRTSTWRSllglfppEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 167 KRPKLLLLDEPMSALDKKI-RQKTQLeLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG3638   163 QEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
21-251 2.57e-62

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 199.93  E-value: 2.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL----ASLPPYRRPVNM 96
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFG-LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK09493   82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 176 EPMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK09493  162 EPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 20-242 4.10e-61

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 199.57  E-value: 4.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKkfgdstAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PYRRPV 94
Cdd:COG4608    24 FGRTVGVVK------AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgrelrPLRRRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQ-SYA-LFPHMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:COG4608    98 QMVFQdPYAsLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPK 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 171 LLLLDEPMSALDKKIrqktQLELVNIIE----KVDVTCVMVTHDQeeAMT--MASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:COG4608   178 LIVCDEPVSALDVSI----QAQVLNLLEdlqdELGLTYLFISHDL--SVVrhISDRVAVMYLGKIVEIAPRDELYARP 249
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 22-237 4.44e-61

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 195.78  E-value: 4.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAG-LETA--TSGKIFVDGEDLASLPPYRRPVNMMF 98
Cdd:COG4136     3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFGLKqEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:COG4136    83 QDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 179 SALDKKIRQKTqLELV-NIIEKVDVTCVMVTHDQEEAmtmasrLAVmseGKIVQIGAPGE 237
Cdd:COG4136   162 SKLDAALRAQF-REFVfEQIRQRGIPALLVTHDEEDA------PAA---GRVLDLGNWQH 211
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 22-251 2.14e-60

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: 195.08  E-value: 2.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQS 100
Cdd:COG4555     3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:COG4555    83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 181 LDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE-FPNSRFSAEFI 251
Cdd:COG4555   163 LDVMARR----LLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeIGEENLEDAFV 233
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 36-245 2.24e-60

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: 194.61  E-value: 2.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVnmmFQSYALFPHMTVESNVAF 115
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVV---FQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 116 GLKQ--EGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLEL 193
Cdd:TIGR01184  78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 194 VNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVyEFPNSR 245
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV-PFPRPR 208
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 21-238 2.36e-60

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: 194.32  E-value: 2.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDLASLPP----YR 91
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVdvleLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPhMTVESNVAFGLKQEGT-PKNEIKERVADALALVQMSKYAQRKPH--QLSGGQQQRVALARSLVKR 168
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 169 PKLLLLDEPMSALDKKIRQKtqLELVnIIE-KVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAK--IEEL-IAElKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 22-240 1.37e-59

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: 192.78  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YRRPVN 95
Cdd:cd03256     2 EVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHMTVESNVAFG-LKQEGT--------PKNEiKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:cd03256    82 MIFQQFNLIERLSVLENVLSGrLGRRSTwrslfglfPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:cd03256   161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
40-237 2.10e-59

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 192.10  E-value: 2.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  40 NLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYALFPHMTVESNVAFGLKQ 119
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 120 EGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKtQLELVN-IIE 198
Cdd:PRK10771   99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE-MLTLVSqVCQ 177

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1219505750 199 KVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGE 237
Cdd:PRK10771  178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 21-242 5.02e-59

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: 199.36  E-value: 5.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF--GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL---ETATSGKIFVDGEDLASLPPYRRP-- 93
Cdd:COG1123     5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGrr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 VNMMFQS--YALFPhMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:COG1123    85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 172 LLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:COG1123   164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 34-239 2.05e-58

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: 191.13  E-value: 2.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  34 TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS-----LPPYRRPVNMMFQ--SYALFpH 106
Cdd:TIGR04521  19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDLRKKVGLVFQfpEHQLF-E 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 MTVESNVAFGLKQEGTPKNEIKERVADALALVQMS-KYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:TIGR04521  98 ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 186 RQktqlELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:TIGR04521 178 RK----EILDLFKRLhkekGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
22-229 5.36e-58

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 187.72  E-value: 5.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMFQ 99
Cdd:COG4619     2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVPQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPhMTVESNVAFGLKQEGTPKNEikERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:COG4619    82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 179 SALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:COG4619   159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 40-233 1.75e-57

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: 186.61  E-value: 1.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  40 NLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYALFPHMTVESNVAFGLKQ 119
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 120 EGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEK 199
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1219505750 200 VDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 41-233 7.22e-57

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: 185.00  E-value: 7.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  41 LTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQSYALFPHMTVESNVAFGLKQE 120
Cdd:cd03298    19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 121 GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKV 200
Cdd:cd03298    99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1219505750 201 DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03298   179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 21-242 7.29e-57

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 188.34  E-value: 7.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLE---TATSGKIFVDGEDLASLPP---- 89
Cdd:COG0444     2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEkelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  90 -YR-RPVNMMFQ-SY-ALFPHMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMS---KYAQRKPHQLSGGQQQRVAL 161
Cdd:COG0444    82 kIRgREIQMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 162 ARSLVKRPKLLLLDEPMSALDKKIrQKTQLEL-VNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG0444   162 ARALALEPKLLIADEPTTALDVTI-QAQILNLlKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240


                  ..
gi 1219505750 241 FP 242
Cdd:COG0444   241 NP 242
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 22-238 3.15e-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: 184.47  E-value: 3.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRpVNM----M 97
Cdd:COG0411     6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-ARLgiarT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVA---------------FGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALA 162
Cdd:COG0411    85 FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 163 RSLVKRPKLLLLDEPMSALDkkiRQKTQlELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG0411   165 RALATEPKLLLLDEPAAGLN---PEETE-ELAELIRRLrderGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 22-238 3.01e-55

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: 181.48  E-value: 3.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRP---VNMMF 98
Cdd:cd03219     2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFGLkQEGTPKN-----------EIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVK 167
Cdd:cd03219    82 QIPRLFPELTVLENVMVAA-QARTGSGlllararreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 168 RPKLLLLDEPMSALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETE----ELAELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 21-229 6.05e-55

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 178.36  E-value: 6.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQ 99
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVafglkqegtpkneikervadalalvqmskyaqrkphQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 180 ALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:cd03230   125 GLDPESRR----EFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 21-238 1.55e-54

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 179.90  E-value: 1.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP------PYRRPV 94
Cdd:COG1121     7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvPQRAEV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NmmfqsyALFPhMTVESNVAFGLKQE----GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:COG1121    87 D------WDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 171 LLLLDEPMSALDkkirQKTQLELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGkIVQIGAPGEV 238
Cdd:COG1121   160 LLLLDEPFAGVD----AATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEV 225
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
20-240 2.05e-54

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 180.60  E-value: 2.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--ASLPPYRRPVN 95
Cdd:PRK13635    5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETVWDVRRQVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSY-ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK13635   85 MVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 175 DEPMSALDKKIRQKTqLELVNII-EKVDVTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13635  165 DEATSMLDPRGRREV-LETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 21-233 2.84e-54

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 179.05  E-value: 2.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE--DLASLP------PYRR 92
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsdkairELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 PVNMMFQSYALFPHMTVESN-VAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 172 LLLDEPMSALDKKIRQktqlELVNIIEKVD---VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK11124  163 LLFDEPTAALDPEITA----QIVSIIRELAetgITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 24-229 3.32e-54

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: 177.99  E-value: 3.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKF-GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASL-----PPYRRPVNMM 97
Cdd:cd03292     4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKIGVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03292    84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 178 MSALDKkirqKTQLELVNIIEKVD---VTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:cd03292   164 TGNLDP----DTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
24-250 4.01e-54

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 183.70  E-value: 4.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------YRRPVNMM 97
Cdd:PRK10070   32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:PRK10070  112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 178 MSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEF 250
Cdd:PRK10070  192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 21-237 4.71e-54

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: 177.70  E-value: 4.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS--TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY-RRPVNMM 97
Cdd:cd03263     1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAF--GLKqeGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:cd03263    81 PQFDALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 176 EPMSALDKKIRQktqlELVNIIEKV--DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGE 237
Cdd:cd03263   159 EPTSGLDPASRR----AIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 23-229 6.54e-54

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 178.72  E-value: 6.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLppyRRPVNMMFQSYA 102
Cdd:PRK11247   15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLMFQDAR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFPHMTVESNVAFGLKqegtpkNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK11247   92 LLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 183 KkirqKTQLELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK11247  166 A----LTRIEMQDLIESLwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
21-233 2.52e-53

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 176.74  E-value: 2.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE--DLASLPP------YRR 92
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSekairlLRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 PVNMMFQSYALFPHMTVESN-VAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:COG4161    83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 172 LLLDEPMSALDKKIRQktqlELVNIIE---KVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:COG4161   163 LLFDEPTAALDPEITA----QVVEIIRelsQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 21-228 4.64e-53

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


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 175.13  E-value: 4.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASL-----PPYRRPV 94
Cdd:TIGR02673   2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrqlPLLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 175 DEPMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGK 228
Cdd:TIGR02673 162 DEPTGNLDPDLSERI-LDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 21-240 4.85e-53

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


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 175.95  E-value: 4.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFG-DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA-----SLPPYRRPV 94
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITklrgkKLRKLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNV---AFGLKQE-----GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVlhgRLGYKPTwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 23-212 1.41e-52

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: 173.57  E-value: 1.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------YRRPVNM 96
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfRREKLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1219505750 177 PMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQE 212
Cdd:TIGR03608 161 PTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHDPE 195
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 21-237 3.67e-52

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: 172.94  E-value: 3.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-PYRRPVNMMFQ 99
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:cd03265    81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGE 237
Cdd:cd03265   161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
cbiO PRK13637
energy-coupling factor transporter ATPase;
32-239 4.53e-52

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 174.85  E-value: 4.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  32 DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL----ASLPPYRRPVNMMFQ--SYALFP 105
Cdd:PRK13637   19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLSDIRKKVGLVFQypEYQLFE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 106 HmTVESNVAFGLKQEGTPKNEIKERVADALALVQMS--KYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDK 183
Cdd:PRK13637   99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 184 KIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13637  178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 28-324 1.64e-51

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 175.30  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  28 KKFGDsTAVDnVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS------LPPYRRPVNMMFQSY 101
Cdd:TIGR02142   7 KRLGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 ALFPHMTVESNVAFGLKQEGTPKNEIK-ERVADALALvqmSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:TIGR02142  85 RLFPHLSVRGNLRYGMKRARPSERRISfERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFsAEFIGSTNLFEGR 260
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW-LAREDQGSLIEGV 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 261 VVEDEPDHIFVESDDLEARMYVShGITGPLGMPVGISVRPERIHVSREKP--GSKHNWARGVVTDI 324
Cdd:TIGR02142 241 VAEHDQHYGLTALRLGGGHLWVP-ENLGPTGARLRLRVPARDVSLALQKPeaTSIRNILPARVVEI 305
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 22-233 5.25e-51

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: 168.38  E-value: 5.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRpvnmmfqsy 101
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 AlfphmtveSNVAFglkqegtpkneikerVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:cd03214    72 A--------RKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 182 DkkIRQktQLELVNII----EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03214   129 D--IAH--QIELLELLrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 21-251 4.61e-50

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: 168.24  E-value: 4.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDLAS----LPPYR 91
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDkkidVVELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPhMTVESNVAFGLKQEGT-PKNEIKERVADALALV--------QMSKYAQRkphqLSGGQQQRVALA 162
Cdd:TIGR00972  82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAalwdevkdRLHDSALG----LSGGQQQRLCIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 163 RSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIieKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNP 234


                  ....*....
gi 1219505750 243 NSRFSAEFI 251
Cdd:TIGR00972 235 KEKRTEDYI 243
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 36-177 5.77e-50

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: 164.74  E-value: 5.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--ASLPPYRRPVNMMFQSYALFPHMTVESNV 113
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 114 AFGLKQEGTPKNEIKERVADALALVQMSKYAQRK----PHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
23-240 5.78e-50

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 168.34  E-value: 5.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASlPPYRRPVnmMFQSYA 102
Cdd:PRK11248    4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK11248   81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 183 KKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGkivqigaPGEVYE 240
Cdd:PRK11248  161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVE 211
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 35-242 1.01e-49

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 174.87  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLEtATSGKIFVDGEDLASLP-----PYRRPVNMMFQS-YA-LFPHM 107
Cdd:COG4172   301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpFGsLSPRM 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 TVESNVAFGLK--QEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKK 184
Cdd:COG4172   380 TVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 185 IrQKTQLELV-NIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:COG4172   460 V-QAQILDLLrDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 21-240 1.39e-49

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: 177.33  E-value: 1.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNM 96
Cdd:COG2274   474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIGV 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFpHMTVESNVAFGlkQEGTPkneiKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSL 165
Cdd:COG2274   554 VLQDVFLF-SGTIRENITLG--DPDAT----DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 166 VKRPKLLLLDEPMSALDkkirQKTQLELVNIIEKV--DVTCVMVTHDqEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG2274   627 LRNPRILILDEATSALD----AETEAIILENLRRLlkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 21-240 2.39e-49

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 167.48  E-value: 2.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNM 96
Cdd:PRK13632    8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSY-ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK13632   88 IFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 176 EPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAmTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13632  168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 21-214 2.43e-49

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: 164.96  E-value: 2.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQ 99
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEikERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:COG4133    83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1219505750 180 ALDKKIRQKtqleLVNIIEKV---DVTCVMVTHDQEEA 214
Cdd:COG4133   161 ALDAAGVAL----LAELIAAHlarGGAVLLTTHQPLEL 194
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
21-229 3.73e-49

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 165.28  E-value: 3.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVK----KFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPpY------ 90
Cdd:NF038007    2 LNMQNAEKcyitKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-Ysqkiil 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 -RRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:NF038007   81 rRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 170 KLLLLDEPMSALDKKiRQKTQLELVNIIEKVDVTCVMVTHDQeEAMTMASRLAVMSEGKI 229
Cdd:NF038007  161 ALLLADEPTGNLDSK-NARAVLQQLKYINQKGTTIIMVTHSD-EASTYGNRIINMKDGKL 218
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
22-238 7.21e-49

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 165.67  E-value: 7.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY----RRPVnmM 97
Cdd:COG4559     3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRRAV--L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYAL-FPhMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV-------KRP 169
Cdd:COG4559    81 PQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 170 KLLLLDEPMSALDkkIRQktQLELVNII-----EKVDVTCVMvtHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG4559   160 RWLFLDEPTSALD--LAH--QHAVLRLArqlarRGGGVVAVL--HDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 21-231 1.66e-48

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 163.76  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS----TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------Y 90
Cdd:COG4181     9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdararlR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 RRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPknEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:COG4181    89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 171 LLLLDEPMSALDKKIRQKtqlelvnIIE-------KVDVTCVMVTHDQEEAmTMASRLAVMSEGKIVQ 231
Cdd:COG4181   167 ILFADEPTGNLDAATGEQ-------IIDllfelnrERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 22-228 4.25e-48

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: 160.10  E-value: 4.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMFq 99
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 syalfphmtvesnvafglkqegtpkneikervadalalvqmskyaqrkphQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:cd00267    80 --------------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTS 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGK 228
Cdd:cd00267   110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 22-238 2.11e-47

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 161.86  E-value: 2.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY----RRPVnmM 97
Cdd:PRK13548    4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRRAV--L 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYAL-FPhMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV------KRPK 170
Cdd:PRK13548   82 PQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 171 LLLLDEPMSALDkkIRQktQLELVNII------EKVDVTCVMvtHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK13548  161 WLLLDEPTSALD--LAH--QHHVLRLArqlaheRGLAVIVVL--HDLNLAARYADRIVLLHQGRLVADGTPAEV 228
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 21-251 2.60e-47

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 161.36  E-value: 2.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDL--ASLPPY--R 91
Cdd:COG1117    12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIydPDVDVVelR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPhMTVESNVAFGLKQEG-TPKNEIKERVADAL---AL---V--QMSKYAQRkphqLSGGQQQRVALA 162
Cdd:COG1117    92 RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVEESLrkaALwdeVkdRLKKSALG----LSGGQQQRLCIA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 163 RSLVKRPKLLLLDEPMSALD----KKIRqktqlELvnIIE-KVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGE 237
Cdd:COG1117   167 RALAVEPEVLLMDEPTSALDpistAKIE-----EL--ILElKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239

                         250
                  ....*....|....
gi 1219505750 238 VYEFPNSRFSAEFI 251
Cdd:COG1117   240 IFTNPKDKRTEDYI 253
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
21-239 3.44e-47

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 161.79  E-value: 3.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS------TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDG---EDLASLPPYR 91
Cdd:PRK13633    5 IKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSyalfPH-----MTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:PRK13633   85 NKAGMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQktqlELVNIIEKVD----VTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRR----EVVNTIKELNkkygITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
cbiO PRK13650
energy-coupling factor transporter ATPase;
36-239 9.68e-47

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 160.67  E-value: 9.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA--SLPPYRRPVNMMFQSY-ALFPHMTVESN 112
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 113 VAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRqktqLE 192
Cdd:PRK13650  103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR----LE 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 193 LVNIIEKV----DVTCVMVTHDQEEaMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13650  179 LIKTIKGIrddyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 22-238 1.17e-46

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: 158.75  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRP---VNMMF 98
Cdd:cd03224     2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFGLkqEGTPKNEIKERVADALA----LVQMSKyaqRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:cd03224    82 EGRRIFPELTVEENLLLGA--YARRRAKRKARLERVYElfprLKERRK---QLAGTLSGGEQQMLAIARALMSRPKLLLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 175 DEPMSALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:cd03224   157 DEPSEGLAPKIVE----EIFEAIRELrdeGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 23-233 5.28e-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: 156.58  E-value: 5.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAkNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQSY 101
Cdd:cd03264     3 LENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQkLRRRIGYLPQEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:cd03264    82 GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 182 DKKIRQKtqleLVNIIEKV--DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03264   162 DPEERIR----FRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 21-240 7.09e-46

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 164.93  E-value: 7.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS-TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMM 97
Cdd:COG4988   337 IELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPasWRRQIAWV 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFpHMTVESNVAFGlKQEGTPkneikERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSLV 166
Cdd:COG4988   417 PQNPYLF-AGTIRENLRLG-RPDASD-----EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALL 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 167 KRPKLLLLDEPMSALDkkirQKTQLELVNIIEKV--DVTCVMVTHDqEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG4988   490 RDAPLLLLDEPTAHLD----AETEAEILQALRRLakGRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLA 560
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 21-228 1.06e-45

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: 154.46  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNM 96
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFpHMTVESNVafglkqegtpkneikervadalalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:cd03228    81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 177 PMSALDkkirQKTQLELVNIIEKV--DVTCVMVTHDqEEAMTMASRLAVMSEGK 228
Cdd:cd03228   123 ATSALD----PETEALILEALRALakGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 21-230 1.53e-45

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: 155.45  E-value: 1.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS 100
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKErvadALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03268    81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 181 LD----KKIRQktqleLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:cd03268   157 LDpdgiKELRE-----LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 23-275 4.32e-45

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 156.81  E-value: 4.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYR-------Rpvn 95
Cdd:COG4152     4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 mmfqsyALFPHMTVESNVAF--GLKqeGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:COG4152    81 ------GLYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 174 LDEPMSALDKkirqktqlelVN-------IIEKVD--VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE-FPN 243
Cdd:COG4152   153 LDEPFSGLDP----------VNvellkdvIRELAAkgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRqFGR 222

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1219505750 244 SRFSAEFIGST----NLFEGRVVEDEPDHIFVESDD 275
Cdd:COG4152   223 NTLRLEADGDAgwlrALPGVTVVEEDGDGAELKLED 258
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 22-224 1.00e-44

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: 153.46  E-value: 1.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP------PYRRPVN 95
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 mmfqsyALFPhMTVESNVAFGLKQE----GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:cd03235    81 ------RDFP-ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 172 LLLDEPMSALDKkirqKTQLELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVM 224
Cdd:cd03235   154 LLLDEPFAGVDP----KTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLL 205
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
21-253 1.08e-44

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 154.57  E-value: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE---------------DLA 85
Cdd:COG4598     9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgelvpaDRR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  86 SLPPYRRPVNMMFQSYALFPHMTVESNVAFG-LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARS 164
Cdd:COG4598    89 QLQRIRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 165 LVKRPKLLLLDEPMSALDKkirqktqlELVNIIEKV-------DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGE 237
Cdd:COG4598   169 LAMEPEVMLFDEPTSALDP--------ELVGEVLKVmrdlaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240

                         250
                  ....*....|....*..
gi 1219505750 238 VYEFPNS-RFsAEFIGS 253
Cdd:COG4598   241 VFGNPKSeRL-RQFLSS 256
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 25-239 2.42e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 154.47  E-value: 2.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE----DLASLPPYRRPVNMMFQ 99
Cdd:PRK13639    6 DLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVGIVFQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SY--ALFPHmTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:PRK13639   86 NPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 178 MSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13639  165 TSGLDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 27-231 8.63e-44

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: 152.65  E-value: 8.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  27 VKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YRRPVNMMFQ-S 100
Cdd:TIGR02769  18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQdS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALF-PHMTVESNVAFGLKQ-EGTPKNEIKERVADALALVQM-SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:TIGR02769  98 PSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 178 MSALDKKIrqktQLELVNIIEKVD----VTCVMVTHDQEEAMTMASRLAVMSEGKIVQ 231
Cdd:TIGR02769 178 VSNLDMVL----QAVILELLRKLQqafgTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 22-230 1.60e-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: 1.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRpVNMMFQS 100
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 --YALFPHmTVESNVAFGLKQEGtpknEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:cd03226    80 vdYQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 179 SALDKKiRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:cd03226   155 SGLDYK-NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 22-238 4.83e-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: 149.60  E-value: 4.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRR--------P 93
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaragiayvP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 vnmmfQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADAL-ALVQMSKyaqRKPHQLSGGQQQRVALARSLVKRPKLL 172
Cdd:TIGR03410  82 -----QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFpVLKEMLG---RRGGDLSGGQQQQLAIARALVTRPKLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 173 LLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 21-230 1.10e-42

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 149.47  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-----AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVN 95
Cdd:COG1101     2 LELKNLSKTFNPGTvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 M--MFQSYAL--FPHMTVESNVA--------FGLKQEGTPKN--EIKERVADaLAL-------VQMSkyaqrkphQLSGG 154
Cdd:COG1101    82 IgrVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKRreLFRELLAT-LGLglenrldTKVG--------LLSGG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 155 QQQRVALARSLVKRPKLLLLDEPMSALD----KKIRQKTQlelvNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:COG1101   153 QRQALSLLMATLTKPKLLLLDEHTAALDpktaALVLELTE----KIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
25-245 2.10e-42

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 149.07  E-value: 2.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PYRRPVNMMFQ 99
Cdd:PRK10419   17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SY--ALFPHMTVESNVAFGLKQ-EGTPKNEIKERVADALALVQMS-KYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK10419   97 DSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 176 EPMSALDKKIrqktQLELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEF--PNSR 245
Cdd:PRK10419  177 EAVSNLDLVL----QAGVIRLLKKLqqqfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFssPAGR 248
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 21-230 2.19e-42

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: 145.65  E-value: 2.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPyrrpvnmmfqs 100
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 yalfphmtvesnvafglkqegtpkneikervADALAL-VQMSkyaqrkpHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:cd03216    70 -------------------------------RDARRAgIAMV-------YQLSVGERQMVEIARALARNARLLILDEPTA 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 180 ALDKKIRQKtqleLVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:cd03216   112 ALTPAEVER----LFKVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 22-238 2.27e-42

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: 147.82  E-value: 2.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRR--------P 93
Cdd:COG0410     5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgigyvP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 vnmmfQSYALFPHMTVESNVAFGLKQeGTPKNEIKERVADALA----LVQMSKyaqRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:COG0410    85 -----EGRRIFPSLTVEENLLLGAYA-RRDRAEVRADLERVYElfprLKERRR---QRAGTLSGGEQQMLAIGRALMSRP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 170 KLLLLDEPMSALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG0410   156 KLLLLDEPSLGLAPLIVE----EIFEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 21-233 3.29e-42

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: 146.66  E-value: 3.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPpyRRPVNMMFQS 100
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03269    79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 181 LDkKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03269   159 LD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 21-245 5.75e-42

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: 146.92  E-value: 5.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRP---VNMM 97
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03218    81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 178 MSALDKKIRQKTQlELVNIIEKVDVTcVMVT-HDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSR 245
Cdd:cd03218   161 FAGVDPIAVQDIQ-KIIKILKDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 21-251 2.00e-41

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 146.05  E-value: 2.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFV-DGEDLASLP---------PY 90
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIDTARSlsqqkglirQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 RRPVNMMFQSYALFPHMTVESNVAFG-LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:PRK11264   84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 170 KLLLLDEPMSALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRF 246
Cdd:PRK11264  164 EVILFDEPTSALDPELVG----EVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239


                  ....*
gi 1219505750 247 SAEFI 251
Cdd:PRK11264  240 TRQFL 244
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
21-233 3.91e-41

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 152.24  E-value: 3.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVvkKF---GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVN 95
Cdd:COG1132   340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIG 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFpHMTVESNVAFGlKQEGTpkneiKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARS 164
Cdd:COG1132   418 VVPQDTFLF-SGTIRENIRYG-RPDAT-----DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 165 LVKRPKLLLLDEPMSALD----KKIRQKtqlelvniIEKV--DVTCVMVTH------DqeeamtmASRLAVMSEGKIVQI 232
Cdd:COG1132   491 LLKDPPILILDEATSALDteteALIQEA--------LERLmkGRTTIVIAHrlstirN-------ADRILVLDDGRIVEQ 555


                  .
gi 1219505750 233 G 233
Cdd:COG1132   556 G 556
cbiO PRK13644
energy-coupling factor transporter ATPase;
21-246 7.71e-41

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 145.13  E-value: 7.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFV---DGEDLASLPPYRRPVNM 96
Cdd:PRK13644    2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgiDTGDFSKLQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQS-YALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK13644   82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 176 EPMSALDKKiRQKTQLELVNIIEKVDVTCVMVTHDQEEaMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRF 246
Cdd:PRK13644  162 EVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 21-240 8.12e-41

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: 151.46  E-value: 8.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF--GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNM 96
Cdd:COG4987   334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddLRRRIAV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFpHMTVESNVAFGlKQEGTPkneikERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSL 165
Cdd:COG4987   414 VPQRPHLF-DTTLRENLRLA-RPDATD-----EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARAL 486

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 166 VKRPKLLLLDEPMSALDkkirQKTQLELVNIIEKV--DVTCVMVTHDqEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG4987   487 LRDAPILLLDEPTEGLD----AATEQALLADLLEAlaGRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLA 558
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 21-251 1.62e-40

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 143.51  E-value: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDLASLP--PYRRP 93
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDviELRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 VNMMFQSYALFPHMTVESNVAFGLKQEGTPKN--EIKERVADALALVQMSKYAQRK----PHQLSGGQQQRVALARSLVK 167
Cdd:PRK14247   84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 168 RPKLLLLDEPMSALDKKIRQKTQ---LELvniieKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNS 244
Cdd:PRK14247  164 QPEVLLADEPTANLDPENTAKIEslfLEL-----KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238


                  ....*..
gi 1219505750 245 RFSAEFI 251
Cdd:PRK14247  239 ELTEKYV 245
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 20-238 2.07e-40

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: 143.30  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGK-IFVDGEDL--ASLPPYRRpvNM 96
Cdd:COG1119     3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRggEDVWELRK--RI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALF----PHMTVESNVA------FGLKQEGTPknEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:COG1119    81 GLVSPALQlrfpRDETVLDVVLsgffdsIGLYREPTD--EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTqLELVN-IIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG1119   159 KDPELLILDEPTAGLDLGARELL-LALLDkLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-238 3.63e-40

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 148.24  E-value: 3.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP---YRRPVNM 96
Cdd:COG1129     4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFG--LKQEGT-PKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:COG1129    84 IHQELNLVPNLSVAENIFLGrePRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 174 LDEPMSALDKKIRQKtqleLVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG1129   164 LDEPTASLTEREVER----LFRIIRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
cbiO PRK13642
energy-coupling factor transporter ATPase;
21-239 1.51e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 141.77  E-value: 1.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF---GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY--RRPVN 95
Cdd:PRK13642    5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSY-ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK13642   85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 175 DEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13642  165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 30-251 1.90e-39

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 140.75  E-value: 1.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  30 FGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDLAS--LPP--YRRPVNMMFQS 100
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdVDPieVRREVGMVFQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLKQEG--TPKNEIKERVADAL---ALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK14267   94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALkkaALWDEVKdRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 175 DEPMSALDKKIRQKTQLELVNIieKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK14267  174 DEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 22-245 4.31e-39

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 139.39  E-value: 4.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRR--------P 93
Cdd:COG1137     5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgigylP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 vnmmfQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:COG1137    85 -----QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 174 LDEPMSALD-------KKI----RQKtqlelvNIiekvdvtCVMVT-HDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEF 241
Cdd:COG1137   160 LDEPFAGVDpiavadiQKIirhlKER------GI-------GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226


                  ....
gi 1219505750 242 PNSR 245
Cdd:COG1137   227 PLVR 230
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
21-230 1.77e-38

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 137.31  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF-GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASL-----PPYRRPV 94
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK10908   82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 175 DEPMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:PRK10908  162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 35-243 2.22e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 139.00  E-value: 2.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVdGEDLAS-------LPPYRRPVNMMFQsyalFP-H 106
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagkknkkLKPLRKKVGIVFQ----FPeH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 M----TVESNVAFGLKQEGTPKNEIKERVADALALVQMS-KYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:PRK13634   97 QlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 182 DKKIRQktqlELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPN 243
Cdd:PRK13634  177 DPKGRK----EMMEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 21-235 3.04e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 138.33  E-value: 3.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY--RRPVNMM 97
Cdd:PRK13647    5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSY--ALFPhMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK13647   85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 176 EPMSALDKKiRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAP 235
Cdd:PRK13647  164 EPMAYLDPR-GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 35-240 6.39e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 137.19  E-value: 6.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIF-----VDGEDLASLppyRRPVNMMFQS-YALFPHMT 108
Cdd:PRK13648   24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKL---RKHIGIVFQNpDNQFVGSI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQk 188
Cdd:PRK13648  101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ- 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 189 tqlELVNIIEKV----DVTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13648  180 ---NLLDLVRKVksehNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 21-233 8.64e-38

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: 135.19  E-value: 8.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST----AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-PYRRPVN 95
Cdd:cd03266     2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 176 EPMSALDKKIRQkTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03266   162 EPTTGLDVMATR-ALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 31-242 1.29e-37

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 142.13  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKS----TLLRMLAGLETATSGKIFVDGEDLASLPPYR------RPVNMMFQ- 99
Cdd:COG4172    21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQe 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 -SYALFPHMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMSKYAQR---KPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:COG4172   101 pMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLLIA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 175 DEPMSALD-----------KKIRQKTQLELvniiekvdvtcVMVTHDqeeaMT----MASRLAVMSEGKIVQIGAPGEVY 239
Cdd:COG4172   181 DEPTTALDvtvqaqildllKDLQRELGMAL-----------LLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELF 245


                  ...
gi 1219505750 240 EFP 242
Cdd:COG4172   246 AAP 248
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
21-238 1.89e-37

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 135.53  E-value: 1.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPyrrpvNMMFQS 100
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFP--HMT-----VESNVAFG----LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:PRK11231   78 LALLPqhHLTpegitVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 170 KLLLLDEPMSALDkkIRQktQLELVNIIEKVDV---TCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK11231  158 PVVLLDEPTTYLD--INH--QVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
cbiO PRK13640
energy-coupling factor transporter ATPase;
21-240 2.05e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 136.47  E-value: 2.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS--TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL---ETATSGKIFVDGEDLASLPPY--RRP 93
Cdd:PRK13640    6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWdiREK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 VNMMFQSY-ALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLL 172
Cdd:PRK13640   86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 173 LLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAmTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13640  166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS 232
cbiO PRK13645
energy-coupling factor transporter ATPase;
23-239 2.35e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 136.29  E-value: 2.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDST-----AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDG-------EDLASLPPY 90
Cdd:PRK13645    9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 RRPVNMMFQ--SYALFPHmTVESNVAFGLKQEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVK 167
Cdd:PRK13645   89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAM 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 168 RPKLLLLDEPMSALDKKIRQktqlELVNIIEKVDVT----CVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13645  168 DGNTLVLDEPTGGLDPKGEE----DFINLFERLNKEykkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 35-242 4.80e-37

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 136.76  E-value: 4.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YRRPVNMMFQS--YALFPHM 107
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewraVRSDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 TVESNVAFGLK--QEGTPKNEIKERVADALALVQM-SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKK 184
Cdd:PRK15079  116 TIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 185 IrqktQLELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:PRK15079  196 I----QAQVVNLLQQLqremGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 21-240 9.08e-37

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: 139.55  E-value: 9.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF-----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFV----DGEDLASLPPYR 91
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RP-----VNMMFQSYALFPHMTVESNV--AFGLKqegTPKNEIKERVADALALVQMS-KYAQ----RKPHQLSGGQQQRV 159
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGLE---LPDELARMKAVITLKMVGFDeEKAEeildKYPDELSEGERHRV 436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 160 ALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516


                  .
gi 1219505750 240 E 240
Cdd:TIGR03269 517 E 517
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 22-230 1.04e-36

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 132.71  E-value: 1.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIE--NVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY--RRPVN 95
Cdd:cd03245     2 RIEfrNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFpHMTVESNVAFGlKQEGTpkneiKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARS 164
Cdd:cd03245    82 YVPQDVTLF-YGTLRDNITLG-APLAD-----DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 165 LVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHDQeEAMTMASRLAVMSEGKIV 230
Cdd:cd03245   155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 35-242 1.16e-36

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 135.48  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-----YRRPVNMMFQS-YA-LFPHM 107
Cdd:PRK11308   30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqklLRQKIQIVFQNpYGsLNPRK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 TVESNVAFGLKQEGT-PKNEIKERVADALALVQM-SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:PRK11308  110 KVGQILEEPLLINTSlSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 186 R-QKTQLeLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:PRK11308  190 QaQVLNL-MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
21-245 1.27e-36

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 133.74  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PYRRPVN 95
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlyTVRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHMTVESNVAFGLKQEGT-PKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK11831   88 MLFQSGALFTDMNVFDNVAYPLREHTQlPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 175 DEPMSALDKkirqKTQLELVNIIEKVD----VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSR 245
Cdd:PRK11831  168 DEPFVGQDP----ITMGVLVKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
25-324 2.38e-36

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 135.39  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAvdNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKI------FVDGEDLASLPPYRRPVNMMF 98
Cdd:PRK11144    5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPEKRRIGYVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFGLKqegtpkNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:PRK11144   83 QDARLFPHYKVRGNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 179 SALD---KKirqktqlELVNIIEK----VDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK11144  157 ASLDlprKR-------ELLPYLERlareINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKE 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 252 GSTNLFEGRVVEDEPDH--IFVESDDleARMYVShGITGPLGMPVGISVRPERIHVSREKP--GSKHNWARGVVTDI 324
Cdd:PRK11144  230 EQSSILKVTVLEHHPHYamTALALGD--QHLWVN-KLDAPLGTALRIRIQASDVSLVLQPPqqSSIRNILRAKVVEI 303
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 21-239 4.54e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 132.66  E-value: 4.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL----ASLPPYRRPVN 95
Cdd:PRK13636    6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQS--YALFPhMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:PRK13636   86 MVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 174 LDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13636  165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 21-238 8.21e-36

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 130.97  E-value: 8.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMF 98
Cdd:COG4604     2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVAFGL--KQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:COG4604    82 QENHINSRLTVRELVAFGRfpYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 177 PMSALD-KKIRQKTQLeLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG4604   162 PLNNLDmKHSVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
28-251 3.24e-35

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 129.70  E-value: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  28 KKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA---------------SLPPYRR 92
Cdd:PRK10619   13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLLRT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 PVNMMFQSYALFPHMTVESNVAFGLKQE-GTPKNEIKERVADALALVQMSKYAQRK-PHQLSGGQQQRVALARSLVKRPK 170
Cdd:PRK10619   93 RLTMVFQHFNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 171 LLLLDEPMSALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFS 247
Cdd:PRK10619  173 VLLFDEPTSALDPELVG----EVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248


                  ....
gi 1219505750 248 AEFI 251
Cdd:PRK10619  249 QQFL 252
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 21-263 4.54e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 131.13  E-value: 4.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-----AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKI----FVDGEDLASLPPY- 90
Cdd:PRK13631   22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELIt 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 -------------RRPVNMMFQ--SYALFPHmTVESNVAFGLKQEGTPKNEIKERVAdaLALVQM---SKYAQRKPHQLS 152
Cdd:PRK13631  102 npyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAK--FYLNKMgldDSYLERSPFGLS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 153 GGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQktqlELVNII---EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK13631  179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEH----EMMQLIldaKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1219505750 230 VQIGAPGEVYefpnsrFSAEFIGSTNLFEGRVVE 263
Cdd:PRK13631  255 LKTGTPYEIF------TDQHIINSTSIQVPRVIQ 282
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 21-251 5.12e-35

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 129.13  E-value: 5.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDLASlpP------ 89
Cdd:PRK14239    6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS--Prtdtvd 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  90 YRRPVNMMFQSYALFPhMTVESNVAFGLKQEGTPKNEIKERVADAlALVQMSKYAQRKPH------QLSGGQQQRVALAR 163
Cdd:PRK14239   84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKDRlhdsalGLSGGQQQRVCIAR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 164 SLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIieKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPN 243
Cdd:PRK14239  162 VLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239


                  ....*...
gi 1219505750 244 SRFSAEFI 251
Cdd:PRK14239  240 HKETEDYI 247
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 21-238 5.71e-35

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 134.38  E-value: 5.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLaslpPYRRP------- 93
Cdd:COG3845     6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV----RIRSPrdaialg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 VNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALvqMSKY-----AQRKPHQLSGGQQQRVALARSLVKR 168
Cdd:COG3845    82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIREL--SERYgldvdPDAKVEDLSVGEQQRVEILKALYRG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 169 PKLLLLDEPMSALDkkiRQKTQlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG3845   160 ARILILDEPTAVLT---PQEAD-ELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 31-243 7.32e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 129.54  E-value: 7.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--ASLPPYRRPVNMMFQSY--ALFPh 106
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKFVGLVFQNPddQIFS- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 MTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIR 186
Cdd:PRK13652   94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 187 QKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPN 243
Cdd:PRK13652  174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 37-240 1.27e-34

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: 127.66  E-value: 1.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  37 DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMFQSYALFPhMTVESNVA 114
Cdd:cd03249    20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSQEPVLFD-GTIAENIR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 115 FGLKqegtpkNEIKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSLVKRPKLLLLDEPMSALDK 183
Cdd:cd03249    99 YGKP------DATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 184 KIRQKTQLELVNIIEkvDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:cd03249   173 ESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 21-238 3.61e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 128.28  E-value: 3.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-----AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKI---FVD------------ 80
Cdd:PRK13651    3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDeknkkktkekek 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  81 -GEDLASLPPY----------RRPVNMMFQ--SYALFpHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSK-YAQR 146
Cdd:PRK13651   83 vLEKLVIQKTRfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 147 KPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD----KKIrqktqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLA 222
Cdd:PRK13651  162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEI-----LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236

                         250
                  ....*....|....*.
gi 1219505750 223 VMSEGKIVQIGAPGEV 238
Cdd:PRK13651  237 FFKDGKIIKDGDTYDI 252
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 20-238 4.19e-34

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


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 133.45  E-value: 4.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKF-GDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY--RRPVN 95
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIG 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFpHMTVESNVAFGlkqegTPKNEiKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARS 164
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG-----APYAD-DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARA 615

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 165 LVKRPKLLLLDEPMSALD----KKIRQKTQLELvniiekVDVTCVMVTHDQeEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDnrseERFKDRLKRWL------AGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 32-251 4.64e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 126.70  E-value: 4.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  32 DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL--------ASLPPYRRPVNMMFQSYAL 103
Cdd:PRK14246   22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqIDAIKLRKEVGMVFQQPNP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FPHMTVESNVAFGLKQEGTP-KNEIKERVADALALVQMSKYAQRK----PHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:PRK14246  102 FPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 179 SALDKKIRQKTQLELVNIieKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK14246  182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 21-240 6.67e-34

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: 125.42  E-value: 6.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGD--STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA--SLPPYRRPVNM 96
Cdd:cd03251     1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFpHMTVESNVAFGLKqegtpkNEIKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSL 165
Cdd:cd03251    81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 166 VKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:cd03251   154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 22-226 6.81e-34

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 125.21  E-value: 6.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMFQ 99
Cdd:PRK10247    9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHmTVESNVAFGL---KQEGTPKneikeRVADALALVQMSKYAQRKP-HQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK10247   89 TPTLFGD-TVYDNLIFPWqirNQQPDPA-----IFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLD 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 176 EPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEE------AMTMASRLAVMSE 226
Cdd:PRK10247  163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEinhadkVITLQPHAGEMQE 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-182 7.62e-34

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 132.94  E-value: 7.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSG--KIF---VDGEDLASlppyRRPVNMMF 98
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWLFgqpVDAGDIAT----RRRVGYMS 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 QSYALFPHMTVESNVA-----FGLkqegtPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:NF033858  346 QAFSLYGELTVRQNLElharlFHL-----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420


                  ....*....
gi 1219505750 174 LDEPMSALD 182
Cdd:NF033858  421 LDEPTSGVD 429
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
25-231 9.12e-34

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 125.31  E-value: 9.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGD---STAV-DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------YRRPV 94
Cdd:PRK11629   10 NLCKRYQEgsvQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK11629   90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 175 DEPMSALDKKiRQKTQLELVNIIEKVDVTC-VMVTHDQEEAMTMaSRLAVMSEGKIVQ 231
Cdd:PRK11629  170 DEPTGNLDAR-NADSIFQLLGELNRLQGTAfLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 22-229 1.31e-33

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: 122.71  E-value: 1.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTA--VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMM 97
Cdd:cd03246     2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPhmtvesnvafglkqeGTpkneikerVADALalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03246    82 PQDDELFS---------------GS--------IAENI---------------LSGGQRQRLGLARALYGNPRILVLDEP 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 178 MSALDKKiRQKTQLELVNIIEKVDVTCVMVTHdQEEAMTMASRLAVMSEGKI 229
Cdd:cd03246   124 NSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 35-238 1.48e-33

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: 124.91  E-value: 1.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMFQSYALFpHMTVESN 112
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGVVLQENVLF-NRSIRDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 113 VAfgLKQEGTPKNEIKE--RVADALALV-QMSK-YAQRKPHQ---LSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:cd03252    96 IA--LADPGMSMERVIEaaKLAGAHDFIsELPEgYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 186 RQKTQLELVNIIEkvDVTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGEV 238
Cdd:cd03252   174 EHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
cbiO PRK13649
energy-coupling factor transporter ATPase;
35-240 1.60e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 126.01  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS------LPPYRRPVNMMFQsyalFPHM- 107
Cdd:PRK13649   22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 ----TVESNVAFGLKQEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK13649   98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 183 KKIRQktqlELVNIIEKVD---VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13649  178 PKGRK----ELMTLFKKLHqsgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
21-240 3.06e-33

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 125.69  E-value: 3.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY-RRPVNMMFQ 99
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHaRQRVGVVPQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:PRK13537   88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13537  168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 39-221 7.98e-33

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 122.58  E-value: 7.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  39 VNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRP------VNMMFQSYALFPHMTVESN 112
Cdd:PRK10584   29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLNALEN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 113 VAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLE 192
Cdd:PRK10584  109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188

                         170       180
                  ....*....|....*....|....*....
gi 1219505750 193 LVNIIEKVDVTCVMVTHDQEEAMTMASRL 221
Cdd:PRK10584  189 LFSLNREHGTTLILVTHDLQLAARCDRRL 217
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 20-259 8.80e-33

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 126.49  E-value: 8.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYR--RPVNMM 97
Cdd:PRK09536    3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGLKQEGT---PKNEIKERVAD-ALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLL 173
Cdd:PRK09536   83 PQDTSLSFEFDVRQVVEMGRTPHRSrfdTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 174 LDEPMSALDKKiRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSR--FSAEFI 251
Cdd:PRK09536  163 LDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRaaFDARTA 241


                  ....*...
gi 1219505750 252 GSTNLFEG 259
Cdd:PRK09536  242 VGTDPATG 249
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 21-251 9.11e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 123.22  E-value: 9.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-----ETATSGKIFVDGEDL----ASLPPYR 91
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyerrVNLNRLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPhMTVESNVAFGLKQEG-TPKNEIKERVADALALVQMSKYAQRKPHQ----LSGGQQQRVALARSLV 166
Cdd:PRK14258   88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSE-----GKIVQIGAPGEVYEF 241
Cdd:PRK14258  167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246

                         250
                  ....*....|
gi 1219505750 242 PNSRFSAEFI 251
Cdd:PRK14258  247 PHDSRTREYV 256
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 29-238 2.37e-32

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 122.02  E-value: 2.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  29 KFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY---RRPVNMMFQSYALFP 105
Cdd:PRK11300   14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiaRMGVVRTFQHVRLFR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 106 HMTV------------ESNVAFGLKQegTP-----KNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKR 168
Cdd:PRK11300   94 EMTVienllvaqhqqlKTGLFSGLLK--TPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 169 PKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK11300  172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
21-246 2.43e-32

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 122.43  E-value: 2.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSG----------KIFVDGEDLASLPPY 90
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIRKS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 RRPVNMMFQSYALFPHMTVESNVAFGlKQEGTP---------KNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVAL 161
Cdd:PRK09984   85 RANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 162 ARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPgevYEF 241
Cdd:PRK09984  164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS---QQF 240


                  ....*
gi 1219505750 242 PNSRF 246
Cdd:PRK09984  241 DNERF 245
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 35-252 3.14e-32

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: 120.94  E-value: 3.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKST----LLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMFQS--YALFPHMT 108
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFGLKQEGTPKNEIKERVADAL---ALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:TIGR02770  81 MGNHAIETLRSLGKLSKQARALILEALeavGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 186 rQKTQLELVNIIEKVDVTCVM-VTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIG 252
Cdd:TIGR02770 161 -QARVLKLLRELRQLFGTGILlITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
30-215 5.86e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 119.26  E-value: 5.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  30 FGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNmmfqsyALFPhMTV 109
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAFGLKQE----GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:NF040873   75 RDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1219505750 186 RQKTqLELVNIIEKVDVTCVMVTHDQEEAM 215
Cdd:NF040873  155 RERI-IALLAEEHARGATVVVVTHDLELVR 183
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 21-224 8.53e-32

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: 125.86  E-value: 8.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMM 97
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHmTVESNVAFGLKqeGTPKNEIKE--RVADALALVQ-----MSKYAQRKPHQLSGGQQQRVALARSLVKRPK 170
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARP--DASDAEIREalERAGLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 171 LLLLDEPMSALDkkirQKTQLELVNIIEKV--DVTCVMVTHDqEEAMTMASRLAVM 224
Cdd:TIGR02857 479 LLLLDEPTAHLD----AETEAEVLEALRALaqGRTVLLVTHR-LALAALADRIVVL 529
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 21-281 2.52e-31

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: 124.14  E-value: 2.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLET--ATSGKI-----------FVD------- 80
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgYVErpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  81 -----GEDLASL--------PPYRRPVN----MMFQ-SYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSK 142
Cdd:TIGR03269  81 pcpvcGGTLEPEevdfwnlsDKLRRRIRkriaIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 143 YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLA 222
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 223 VMSEGKIVQIGAPGEVyefpnsrfSAEFIGSTNLFE-GRVVEDEPDHIFVEsdDLEARMY 281
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV--------VAVFMEGVSEVEkECEVEVGEPIIKVR--NVSKRYI 290
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
29-239 3.54e-31

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 119.34  E-value: 3.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  29 KFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL----ASLPPYRRPVNMMFQ--SYA 102
Cdd:PRK13638   10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLALRQQVATVFQdpEQQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFpHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK13638   90 IF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 183 KKIRQktqlELVNIIEKVDVT---CVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13638  169 PAGRT----QMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
cbiO PRK13643
energy-coupling factor transporter ATPase;
33-240 1.61e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 117.91  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  33 STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS------LPPYRRPVNMMFQsyalFPH 106
Cdd:PRK13643   19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVRKKVGVVFQ----FPE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 M-----TVESNVAFGLKQEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:PRK13643   95 SqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 181 LDKKIRQKtQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK13643  175 LDPKARIE-MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
37-230 3.27e-30

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 122.14  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  37 DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP------YRRPVNMMFQSYALFPHMTVE 110
Cdd:PRK10535   25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLTAA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 111 SNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkirQKTQ 190
Cdd:PRK10535  105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD----SHSG 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1219505750 191 LELVNIIEKVDV---TCVMVTHDQEEAmTMASRLAVMSEGKIV 230
Cdd:PRK10535  181 EEVMAILHQLRDrghTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
cbiO PRK13646
energy-coupling factor transporter ATPase;
35-239 6.17e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 116.42  E-value: 6.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS------LPPYRRPVNMMFQsyalFPHM- 107
Cdd:PRK13646   22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPESq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 ----TVESNVAFGLKQEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK13646   98 lfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 183 KKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVY 239
Cdd:PRK13646  178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 31-238 1.14e-29

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 119.85  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRR-------PvnmmfQSYAL 103
Cdd:COG4618   343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhigylP-----QDVEL 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FPHmTVESNVA-FGlkqEGTPkneikERVADALALVQMSKYAQRKP-----------HQLSGGQQQRVALARSLVKRPKL 171
Cdd:COG4618   418 FDG-TIAENIArFG---DADP-----EKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRL 488

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 172 LLLDEPMSALDKKIRQKtqleLVNIIEKV---DVTCVMVTHDQeEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG4618   489 VVLDEPNSNLDDEGEAA----LAAAIRALkarGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 21-283 1.14e-29

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 115.26  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL----ETA-TSGKIFVDGEDL--ASLPP--YR 91
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndliPGFrVEGKVTFHGKNLyaPDVDPveVR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  92 RPVNMMFQSYALFPHmTVESNVAFGLKQEGTPKN--EIKERVADALALVQMSKYAQRKPHQ-LSGGQQQRVALARSLVKR 168
Cdd:PRK14243   91 RRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdELVERSLRQAALWDEVKDKLKQSGLsLSGGQQQRLCIARAIAVQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 169 PKLLLLDEPMSALDKKIRQKTQlELVNIIeKVDVTCVMVTHDqeeaMTMASRLAVMSegkivqigapgevyEFPNSRFSA 248
Cdd:PRK14243  170 PEVILMDEPCSALDPISTLRIE-ELMHEL-KEQYTIIIVTHN----MQQAARVSDMT--------------AFFNVELTE 229

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1219505750 249 EfiGSTNlfeGRVVE-DEPDHIFVESDDLEARMYVS 283
Cdd:PRK14243  230 G--GGRY---GYLVEfDRTEKIFNSPQQQATRDYVS 260
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 21-237 1.29e-29

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: 114.25  E-value: 1.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAV-DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNMM 97
Cdd:cd03253     1 IEFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFpHMTVESNVAFGlkqegTPkNEIKERVADALALVQMSKYAQRKPHQ-----------LSGGQQQRVALARSLV 166
Cdd:cd03253    81 PQDTVLF-NDTIGYNIRYG-----RP-DATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 167 KRPKLLLLDEPMSALDkkirQKTQLELVNIIEKV--DVTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGE 237
Cdd:cd03253   154 KNPPILLLDEATSALD----THTEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 35-229 2.88e-29

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: 111.75  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMF------QSYALFPHMT 108
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFglkqegtpkneikervadalalvqmskyaqrkPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD----KK 184
Cdd:cd03215    95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgakAE 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1219505750 185 IRQKtqlelvnIIEKVD--VTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:cd03215   143 IYRL-------IRELADagKAVLLISSELDELLGLCDRILVMYEGRI 182
cbiO PRK13641
energy-coupling factor transporter ATPase;
36-250 2.97e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 114.54  E-value: 2.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA------SLPPYRRPVNMMFQsyalFPHM-- 107
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAql 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 ---TVESNVAFGLKQEGTPKNEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDK 183
Cdd:PRK13641   99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 184 KIRqKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPN------------SRFSAEF 250
Cdd:PRK13641  179 EGR-KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldepatSRFASKL 256
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
3-235 3.68e-29

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 115.31  E-value: 3.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   3 HTLPASVAAAARHDADAFVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE 82
Cdd:PRK13536   24 QGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  83 DL-ASLPPYRRPVNMMFQSYALFPHMTVESN-VAFGlKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVA 160
Cdd:PRK13536  104 PVpARARLARARIGVVPQFDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 161 LARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAP 235
Cdd:PRK13536  183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 21-241 6.62e-29

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 112.48  E-value: 6.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF----------------------GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIF 78
Cdd:COG1134     5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  79 VDGEdLASLppyrrpVNMM--FQsyalfPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQ 156
Cdd:COG1134    85 VNGR-VSAL------LELGagFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 157 QRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPG 236
Cdd:COG1134   153 ARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231


                  ....*
gi 1219505750 237 EVYEF 241
Cdd:COG1134   232 EVIAA 236
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 35-242 8.16e-29

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 117.65  E-value: 8.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-----PYRRPVNMMFQS-YA-LFPHM 107
Cdd:PRK10261  339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPRQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 TVESNVAFGLKQEGT-PKNEIKERVADALALVQM-SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:PRK10261  419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 186 RQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:PRK10261  499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 22-227 1.28e-28

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: 111.37  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKF-----GDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE----DLASLPPY 90
Cdd:COG4778     6 EVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  91 -----RRPVnMMFQSYAL--FPHMTVESNVAFGLKQEGTPKNEIKERVADALA-------LVQMSkyaqrkPHQLSGGQQ 156
Cdd:COG4778    86 eilalRRRT-IGYVSQFLrvIPRVSALDVVAEPLLERGVDREEARARARELLArlnlperLWDLP------PATFSGGEQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 157 QRVALARSLVKRPKLLLLDEPMSALDKKIRQKtqleLVNIIEKV---DVTCVMVTHDqEEAM-TMASRLAVMSEG 227
Cdd:COG4778   159 QRVNIARGFIADPPLLLLDEPTASLDAANRAV----VVELIEEAkarGTAIIGIFHD-EEVReAVADRVVDVTPF 228
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
21-238 1.77e-28

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 112.00  E-value: 1.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL---ASLPPYRRpVNMM 97
Cdd:PRK10253    8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEVARR-IGLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGlKQEGTP-----KNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLL 172
Cdd:PRK10253   87 AQNATTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 173 LLDEPMSALDKKiRQKTQLELVNIIEKVD-VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK10253  166 LLDEPTTWLDIS-HQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 21-233 2.37e-28

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: 110.31  E-value: 2.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF----------------------GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIF 78
Cdd:cd03220     1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  79 VDGedlaslppyrRPVNMMFQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQR 158
Cdd:cd03220    81 VRG----------RVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 159 VALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03220   151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 27-238 3.38e-28

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 110.70  E-value: 3.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  27 VKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLeTATSGKIFVDGEDLASLPP-----YR-------RPV 94
Cdd:COG4138     3 LNDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelarHRaylsqqqSPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMM--FQSYALF-PHMTVESNVAFGLKQegtpkneikerVADALALvqMSKYAqRKPHQLSGGQQQRVALARSLVK---- 167
Cdd:COG4138    82 FAMpvFQYLALHqPAGASSEAVEQLLAQ-----------LAEALGL--EDKLS-RPLTQLSGGEWQRVRLAAVLLQvwpt 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 168 ---RPKLLLLDEPMSALDkkIRQktQLELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG4138   148 inpEGQLLLLDEPMNSLD--VAQ--QAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 26-233 4.31e-28

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 115.33  E-value: 4.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  26 VVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLeTATSGKIFVDGEDLASLPP--YRRPVNMMFQSYAL 103
Cdd:PRK11174  356 EILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPesWRKHLSWVGQNPQL 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FpHMTVESNVAFGlKQEGTPkneikERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSLVKRPKLL 172
Cdd:PRK11174  435 P-HGTLRDNVLLG-NPDASD-----EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLL 507

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 173 LLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK11174  508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQG 565
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 20-240 9.04e-28

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: 108.85  E-value: 9.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP--PYRRPVNM 96
Cdd:cd03254     2 EIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHmTVESNVAFGlkqegtpKNEIK-ERVADALALVQMSKYAQRKP-----------HQLSGGQQQRVALARS 164
Cdd:cd03254    82 VLQDTFLFSG-TIMENIRLG-------RPNATdEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 165 LVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdqeeamtmasRLA---------VMSEGKIVQIGAP 235
Cdd:cd03254   154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----------RLStiknadkilVLDDGKIIEEGTH 221


                  ....*
gi 1219505750 236 GEVYE 240
Cdd:cd03254   222 DELLA 226
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 25-228 1.17e-27

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 113.87  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL--ETATSGKIFVDGEDLAS---LPPYRRPVNMMFQ 99
Cdd:PRK13549   10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQAsniRDTERAGIAIIHQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGlkQEGTPK-----NEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK13549   90 ELALVKELSVLENIFLG--NEITPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 175 DEPMSALdkkIRQKTQLeLVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGK 228
Cdd:PRK13549  168 DEPTASL---TESETAV-LLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDGR 220
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 23-210 3.16e-27

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 112.47  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVD-GEDLASLPpyrrpvnmmfQSY 101
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 ALFPHMTVESNVAFGLKqegtPKNEIKERVADALALV-----QMSKYA-------------------------------- 144
Cdd:COG0488    71 PLDDDLTVLDTVLDGDA----ELRALEAELEELEAKLaepdeDLERLAelqeefealggweaearaeeilsglgfpeedl 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 145 QRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkirqktqLE----LVNIIEKVDVTCVMVTHD 210
Cdd:COG0488   147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsiewLEEFLKNYPGTVLVVSHD 208
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 23-242 4.57e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 109.45  E-value: 4.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDST----AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL----ETATSGKIFVDGEDLASLPPYRR-- 92
Cdd:PRK11022    6 VDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 ----PVNMMFQS--YALFPHMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMSKYAQR---KPHQLSGGQQQRVALA 162
Cdd:PRK11022   86 lvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 163 RSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFP 242
Cdd:PRK11022  166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 31-210 7.73e-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: 111.68  E-value: 7.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP--PYRRPVNMMFQSYALFpHMT 108
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSVCAQDAHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFGlKQEGTPkneikERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:TIGR02868 425 VRENLRLA-RPDATD-----EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEP 498

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1219505750 178 MSALDKkirqKTQLELVNIIEKVD--VTCVMVTHD 210
Cdd:TIGR02868 499 TEHLDA----ETADELLEDLLAALsgRTVVLITHH 529
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
37-184 9.76e-27

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 105.27  E-value: 9.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  37 DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRpvNMMF---QSyALFPHMTVESN 112
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQ--DLLYlghQP-GIKTELTALEN 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 113 VAFGLKQEGTPKNEikeRVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKK 184
Cdd:PRK13538   95 LRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 21-235 1.48e-26

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: 112.03  E-value: 1.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   21 VRIENVVKKFGDS--TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL-ASLPPYRRPVNMM 97
Cdd:TIGR01257  929 VCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMC 1008

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   98 FQSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750  178 MSALDKKIRQKTQLELVNIieKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAP 235
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 31-251 1.95e-26

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 110.18  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKST----LLRMLAgletaTSGKIFVDGEDLASLP-----PYRRPVNMMFQ-- 99
Cdd:PRK15134  297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVFQdp 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFGLK--QEGTPKNEIKERVADALALVQMSKYA-QRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:PRK15134  372 NSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 177 PMSALDKKIrQKTQLELVNII-EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK15134  452 PTSSLDKTV-QAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 22-238 3.11e-26

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 109.35  E-value: 3.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENV-VKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY-RRPVNMMF- 98
Cdd:COG3845   259 EVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPReRRRLGVAYi 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 ----QSYALFPHMTVESNVAFGlKQEGTPKNE---IKERVADALALVQMSKYAQRKPH------QLSGGQQQRVALARSL 165
Cdd:COG3845   339 pedrLGRGLVPDMSVAENLILG-RYRRPPFSRggfLDRKAIRAFAEELIEEFDVRTPGpdtparSLSGGNQQKVILAREL 417

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 166 VKRPKLLLLDEPMSALD----KKIRQKtqlelvnIIEKVD--VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:COG3845   418 SRDPKLLIAAQPTRGLDvgaiEFIHQR-------LLELRDagAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 21-233 3.73e-26

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: 109.81  E-value: 3.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFG--DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA--SLPPYRRPVNM 96
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHmTVESNVAFGlKQEGTPKNEIKERVADALALvqmsKYAQRKP---HQ--------LSGGQQQRVALARSL 165
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAAAYAQ----DFVDKLPlglDTpigengvlLSGGQRQRLAIARAL 484

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 166 VKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERG 549
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 21-233 5.90e-26

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 102.78  E-value: 5.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS--TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRP-VNMM 97
Cdd:cd03247     1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFphmtvesnvafglkqEGTPKNEIKERvadalalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03247    81 NQRPYLF---------------DTTLRNNLGRR--------------------FSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 178 MSALDKkirqKTQLELVNIIEKV--DVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03247   126 TVGLDP----ITERQLLSLIFEVlkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 24-238 6.18e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 104.21  E-value: 6.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY---RRPVNMMFQS 100
Cdd:PRK10895    7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYLPQE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:PRK10895   87 ASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 180 ALDKkirqKTQLELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK10895  167 GVDP----ISVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 25-252 6.71e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 105.18  E-value: 6.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSG-----KIFVDGEDLAS---LPPYRRPVNM 96
Cdd:PRK14271   26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNyrdVLEFRRRVGM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPhMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMSKYAQRK----PHQLSGGQQQRVALARSLVKRPKL 171
Cdd:PRK14271  106 LFQRPNPFP-MSIMDNVLAGVRaHKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 172 LLLDEPMSALDKKIRQKTQLELVNIIEKvdVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK14271  185 LLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262


                  .
gi 1219505750 252 G 252
Cdd:PRK14271  263 A 263
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
23-230 7.99e-26

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 103.81  E-value: 7.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP---YRRPVNMMFQ 99
Cdd:PRK11614    8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREAVAIVPE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAF-GLKQEGTPKNEIKERVADALALVQmSKYAQRKpHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:PRK11614   88 GRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPRLH-ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 179 SALDKKIRQktqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:PRK11614  166 LGLAPIIIQ----QIFDTIEQLreqGMTIFLVEQNANQALKLADRGYVLENGHVV 216
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 31-184 8.74e-26

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: 102.82  E-value: 8.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQSYALFPHMTV 109
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 110 ESNVAFGLKQEGTPKNEIKervaDALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKK 184
Cdd:TIGR01189  91 LENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
27-251 1.12e-25

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 107.80  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  27 VKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLaslpPYRRPVNMM-----F--- 98
Cdd:COG1129   259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV----RIRSPRDAIragiaYvpe 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 --QSYALFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPH------QLSGGQQQRVALARSLVKRPK 170
Cdd:COG1129   335 drKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSpeqpvgNLSGGNQQKVVLAKWLATDPK 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 171 LLLLDEPMSALDkkIRQKTqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQigapgevyEFPNSRFS 247
Cdd:COG1129   415 VLILDEPTRGID--VGAKA--EIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIVG--------ELDREEAT 482


                  ....
gi 1219505750 248 AEFI 251
Cdd:COG1129   483 EEAI 486
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 23-230 1.96e-25

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: 107.22  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL--ETATSGKIFVDGEDLAS---LPPYRRPVNMM 97
Cdd:TIGR02633   4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAsniRDTERAGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFG----LKQEGTPKNEIKERVADALALVQMSKYAQRKP-HQLSGGQQQRVALARSLVKRPKLL 172
Cdd:TIGR02633  84 HQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 173 LLDEPMSALdkkIRQKTQ--LELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:TIGR02633 164 ILDEPSSSL---TEKETEilLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 28-230 3.06e-25

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: 102.41  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  28 KKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDlaslpPYRRPVNMMFQSYALFPHM 107
Cdd:cd03267    29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRKKFLRRIGVVFGQK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 108 T--------VESnvaFGLKQE--GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03267   104 TqlwwdlpvIDS---FYLLAAiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 178 MSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:cd03267   181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 21-235 3.53e-25

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: 101.80  E-value: 3.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGD--STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNM 96
Cdd:cd03244     3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhdLRSRISI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHmTVESNVA-FGLKQEgtpkneikERVADALALVQMSKYAQRKPHQL-----------SGGQQQRVALARS 164
Cdd:cd03244    83 IPQDPVLFSG-TIRSNLDpFGEYSD--------EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 165 LVKRPKLLLLDEPMSALD----KKIRQKTQLELvniiekVDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAP 235
Cdd:cd03244   154 LLRKSKILVLDEATASVDpetdALIQKTIREAF------KDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 22-233 4.83e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 102.31  E-value: 4.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE-----DLASLPPYRRpvNM 96
Cdd:PRK11701    8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER--RR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPH--------MTVES--NV-----AFGLKQEGtpknEIKERVADALALVQMSkyAQR---KPHQLSGGQQQR 158
Cdd:PRK11701   86 LLRTEWGFVHqhprdglrMQVSAggNIgerlmAVGARHYG----DIRATAGDWLERVEID--AARiddLPTTFSGGMQQR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 159 VALARSLVKRPKLLLLDEPMSALDKKIrQKTQLELV-NIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK11701  160 LQIARNLVTHPRLVFMDEPTGGLDVSV-QARLLDLLrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 31-183 4.98e-25

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 101.10  E-value: 4.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDlASLPPYRRPVNMMFQSYALFPHMTVE 110
Cdd:PRK13539   13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYLGHRNAMKPALTVA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 111 SNVAFGLKQEGTPKNEIkervADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV-KRPkLLLLDEPMSALDK 183
Cdd:PRK13539   92 ENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALDA 160
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
35-253 7.30e-25

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 102.18  E-value: 7.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLaSLPPYR---RPVNMMFQ--SYALFPHMTV 109
Cdd:PRK15112   28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSyrsQRIRMIFQdpSTSLNPRQRI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAFGLKQEGTPKNEIKE-RVADALALVQM-SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQ 187
Cdd:PRK15112  107 SQILDFPLRLNTDLEPEQREkQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 188 KTQLELVNIIEKVDVTCVMVThdQEEAMT--MASRLAVMSEGKIVQIGAPGEVYEFPNSRFSAEFIGS 253
Cdd:PRK15112  187 QLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 33-233 1.63e-24

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: 105.21  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  33 STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPY--RRPVNMMFQSYALFPHmTVE 110
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYLPQEPYIFSG-SIL 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 111 SNVAFGLKqEGTPKNEIKErvadALALVQMSKYAQRKPH-----------QLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWA----ACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDESTS 640

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKvdvTCVMVTHDQEEAmTMASRLAVMSEGKIVQIG 233
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQG 690
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 38-240 1.69e-24

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 105.19  E-value: 1.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNMMFQSYALFPHmTVESNVAF 115
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhyLHRQVALVGQEPVLFSG-SVRENIAY 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 116 GLKQegTPKNEIKERVADALALVQMSKYAQ-------RKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQK 188
Cdd:TIGR00958 578 GLTD--TPDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 189 TQlelvNIIEKVDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:TIGR00958 656 LQ----ESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLME 702
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 23-233 1.73e-24

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: 99.14  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLE--TATSGKIFVDGEDLASLPPY---RRPVNMM 97
Cdd:cd03217     3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEeraRLGIFLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPhmtvesnvafGLKqegtpkneikerVADALALVQMSkyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03217    83 FQYPPEIP----------GVK------------NADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEP 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 178 MSALDkkirqKTQLELV-NIIEK---VDVTCVMVTHDQEEAMTM-ASRLAVMSEGKIVQIG 233
Cdd:cd03217   132 DSGLD-----IDALRLVaEVINKlreEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 21-230 2.25e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 104.38  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIfvdgedlaslppyRRPVNMMFQS 100
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVKIGY 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YA-----LFPHMTVESNVafglkQEGTPKNEIKErVADALALVQMSKYAQRKP-HQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:COG0488   383 FDqhqeeLDPDKTVLDEL-----RDGAPGGTEQE-VRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLL 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 175 DEPMSALDkkIRQKTQLElvNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:COG0488   457 DEPTNHLD--IETLEALE--EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 38-233 3.92e-24

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 98.88  E-value: 3.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGL---ETATSGKIFVDGEDLaSLPPYRRPVNMMFQSYALFPHMTVESNVA 114
Cdd:cd03234    25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLTVRETLT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 115 FGLK---QEGTPKNEIKERVAD-ALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkirQKTQ 190
Cdd:cd03234   104 YTAIlrlPRKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD----SFTA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1219505750 191 LELVNIIEKVDVT--CVMVTHDQ--EEAMTMASRLAVMSEGKIVQIG 233
Cdd:cd03234   180 LNLVSTLSQLARRnrIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 36-209 4.70e-24

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 103.73  E-value: 4.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNElfALL--GSSGCGKSTLLRMLAGLETATSGKIFV-DGEDLASLP--PYrrpvnmmfqsyalFPHMTVE 110
Cdd:COG4178   379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrPY-------------LPLGTLR 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 111 SNVAFGLKQEGTPKneikERVADALALVQMSKYAQR------KPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKk 184
Cdd:COG4178   444 EALLYPATAEAFSD----AELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE- 518

                         170       180
                  ....*....|....*....|....*..
gi 1219505750 185 irqKTQLELVNII--EKVDVTCVMVTH 209
Cdd:COG4178   519 ---ENEAALYQLLreELPGTTVISVGH 542
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 21-233 5.50e-24

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 103.37  E-value: 5.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST--AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNM 96
Cdd:PRK11160  339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEaaLRQAISV 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHmTVESNVAFGLKQEGtpkneiKERVADALALVQMSKYAQRKP----------HQLSGGQQQRVALARSLV 166
Cdd:PRK11160  419 VSQRVHLFSA-TLRDNLLLAAPNAS------DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALL 491

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 167 KRPKLLLLDEPMSALDKkirqKTQLELVNIIEKV--DVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK11160  492 HDAPLLLLDEPTEGLDA----ETERQILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQG 555
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 21-232 5.92e-24

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 103.13  E-value: 5.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDST-AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE--DLASLPPYRRPVNMM 97
Cdd:PRK10522  323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvTAEQPEDYRKLFSAV 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMtvesnvafgLKQEGTPKNEikERVADALALVQMSKYAQRKPH-----QLSGGQQQRVALARSLVKRPKLL 172
Cdd:PRK10522  403 FTDFHLFDQL---------LGPEGKPANP--ALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDIL 471

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 173 LLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDqEEAMTMASRLAVMSEGKIVQI 232
Cdd:PRK10522  472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 21-253 1.08e-23

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: 98.36  E-value: 1.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPV---NMM 97
Cdd:TIGR02323   4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEaerRRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPH--------MTV-------ESNVAFGLKQEGtpknEIKERVADALALVQMSK-YAQRKPHQLSGGQQQRVAL 161
Cdd:TIGR02323  84 MRTEWGFVHqnprdglrMRVsaganigERLMAIGARHYG----NIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 162 ARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEF 241
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239

                         250
                  ....*....|..
gi 1219505750 242 PNSRFSAEFIGS 253
Cdd:TIGR02323 240 PQHPYTQLLVSS 251
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 21-228 1.55e-23

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: 96.77  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVV-----KKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGedlaslppyrrpvn 95
Cdd:cd03250     1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 mmfqSYALFP------HMTVESNVAFGLkqegtPKNEIK-ERVADALALV----QMskyaqrkPHQ-----------LSG 153
Cdd:cd03250    67 ----SIAYVSqepwiqNGTIRENILFGK-----PFDEERyEKVIKACALEpdleIL-------PDGdlteigekginLSG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 154 GQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKtqlelvnIIEKV-------DVTCVMVTHdQEEAMTMASRLAVMSE 226
Cdd:cd03250   131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH-------IFENCilglllnNKTRILVTH-QLQLLPHADQIVVLDN 202


                  ..
gi 1219505750 227 GK 228
Cdd:cd03250   203 GR 204
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
21-248 1.99e-23

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 101.96  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF-GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGED-----LASLppyRRPV 94
Cdd:PRK13657  335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtRASL---RRNI 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFpHMTVESNVAFGlKQEGTPkneikERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALAR 163
Cdd:PRK13657  412 AVVFQDAGLF-NRSIEDNIRVG-RPDATD-----EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIAR 484

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 164 SLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFpN 243
Cdd:PRK13657  485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVAR-G 560


                  ....*
gi 1219505750 244 SRFSA 248
Cdd:PRK13657  561 GRFAA 565
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 21-212 2.59e-23

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: 94.44  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDgedlaslppyrrpvnmmfqS 100
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------S 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMtvesnvafglkqegtpkneikervadalalvqmskyaqrkpHQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:cd03221    62 TVKIGYF-----------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1219505750 181 LDkkIRQKTQLElvNIIEKVDVTCVMVTHDQE 212
Cdd:cd03221   101 LD--LESIEALE--EALKEYPGTVILVSHDRY 128
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
20-238 2.70e-23

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 101.01  E-value: 2.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP---YRRPVNM 96
Cdd:PRK09700    5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHMTVESNVAFGL----KQEGTPK---NEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:PRK09700   85 IYQELSVIDELTVLENLYIGRhltkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 170 KLLLLDEPMSALDKKIRQKTQLeLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK09700  165 KVIIMDEPTSSLTNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
22-238 2.87e-23

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 97.55  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASL--PPYRRPVNMMFQ 99
Cdd:PRK10575   13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVAYLPQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFG-------LKQEGTpknEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLL 172
Cdd:PRK10575   93 QLPAAEGMTVRELVAIGrypwhgaLGRFGA---ADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 173 LLDEPMSALDkkIRQktQLELVNIIEKVD----VTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK10575  170 LLDEPTSALD--IAH--QVDVLALVHRLSqergLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 21-229 4.02e-23

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: 96.39  E-value: 4.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKF---GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVN 95
Cdd:cd03248    12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkyLHSKVS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MMFQSYALFPHmTVESNVAFGLKQegTPKNEIKERVADALALVQMSKYAQ-------RKPHQLSGGQQQRVALARSLVKR 168
Cdd:cd03248    92 LVGQEPVLFAR-SLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASgydtevgEKGSQLSGGQKQRVAIARALIRN 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 169 PKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdQEEAMTMASRLAVMSEGKI 229
Cdd:cd03248   169 PQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAH-RLSTVERADQILVLDGGRI 226
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 23-235 4.67e-23

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 96.67  E-value: 4.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLE--TATSGKIFVDGEDLASLPPY---RRPVNMM 97
Cdd:COG0396     3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDeraRAGIFLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVES--NVAFGLKQEGTPKN-EIKERVADALALVQMSK-YAQRKPHQ-LSGGQQQRVALARSLVKRPKLL 172
Cdd:COG0396    83 FQYPVEIPGVSVSNflRTALNARRGEELSArEFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 173 LLDEPMSALD----KKIRqktqlELVNIIEKVDVTCVMVTHDQE--EAMTmASRLAVMSEGKIVQIGAP 235
Cdd:COG0396   163 ILDETDSGLDidalRIVA-----EGVNKLRSPDRGILIITHYQRilDYIK-PDFVHVLVDGRIVKSGGK 225
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 31-247 6.98e-23

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 97.87  E-value: 6.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETA---TSGKIFVDGEDLASLPPYR------RPVNMMFQS- 100
Cdd:PRK09473   27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKElnklraEQISMIFQDp 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 -YALFPHMTVESNVAFGLKQ-EGTPKNEIKE---RVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:PRK09473  107 mTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 176 EPMSALDKKIrQKTQLELVNIIEK-VDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFS 247
Cdd:PRK09473  187 EPTTALDVTV-QAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYS 258
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 21-233 2.18e-22

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: 98.74  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVkkFG---DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL-----ASLppyRR 92
Cdd:COG5265   358 VRFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdvtqASL---RA 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 PVNMMFQSYALFpHMTVESNVAFGlkQEGTPKNEIkERVADAlalVQMSKYAQRKPHQ-----------LSGGQQQRVAL 161
Cdd:COG5265   433 AIGIVPQDTVLF-NDTIAYNIAYG--RPDASEEEV-EAAARA---AQIHDFIESLPDGydtrvgerglkLSGGEKQRVAI 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 162 ARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEkvDVTCVMVTHdqeeamtmasRLA---------VMSEGKIVQI 232
Cdd:COG5265   506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH----------RLStivdadeilVLEAGRIVER 573


                  .
gi 1219505750 233 G 233
Cdd:COG5265   574 G 574
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 21-238 3.47e-22

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 97.80  E-value: 3.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENV--VKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--YRRPVNM 96
Cdd:TIGR01842 317 LSVENVtiVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRetFGKHIGY 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHmTVESNVA-FGlkqegtpKNEIKERVADALALVQMSKYAQRKPH-----------QLSGGQQQRVALARS 164
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIArFG-------ENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARA 468

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 165 LVKRPKLLLLDEPMSALDkkirQKTQLELVNII---EKVDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLD----EEGEQALANAIkalKARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 34-230 4.37e-22

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 95.54  E-value: 4.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  34 TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDlaslpPYRRPVN-------MMFQSYALFPH 106
Cdd:COG4586    36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRRKEfarrigvVFGQRSQLWWD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 MTV-ESnvaFGLKQE--GTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD- 182
Cdd:COG4586   111 LPAiDS---FRLLKAiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDv 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 183 ---KKIRQKtqleLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:COG4586   188 vskEAIREF----LKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 36-230 4.56e-22

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: 92.61  E-value: 4.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL--ETATSGKIFVDGEDLaSLPPYRRPVNMMFQSYALFPHMTVESNV 113
Cdd:cd03213    25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL-DKRSFRKIIGYVPQDDILHPTLTVRETL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 114 AFGLKQEGtpkneikervadalalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkKIRQKTQLEL 193
Cdd:cd03213   104 MFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD-SSSALQVMSL 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1219505750 194 VNIIEKVDVTCVMVTHD-QEEAMTMASRLAVMSEGKIV 230
Cdd:cd03213   154 LRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 25-234 4.79e-22

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 97.43  E-value: 4.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP--------YRRPvnm 96
Cdd:PRK15439   16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakahqlgiYLVP--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 mfQSYALFPHMTVESNVAFGLkqegtPKNEI-KERVADALALVQmskyAQRKPHQLSG----GQQQRVALARSLVKRPKL 171
Cdd:PRK15439   93 --QEPLLFPNLSVKENILFGL-----PKRQAsMQKMKQLLAALG----CQLDLDSSAGslevADRQIVEILRGLMRDSRI 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 172 LLLDEPMSALdkkirqkTQLELVNIIEKV------DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGA 234
Cdd:PRK15439  162 LILDEPTASL-------TPAETERLFSRIrellaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 35-243 5.17e-22

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 93.84  E-value: 5.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDN----VNLTIAKNELFALLGSSGCGKSTLLRMLAGLeTATSGKIFVDGEDLASLPP-----YR-------RPVNMM- 97
Cdd:PRK03695    7 AVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarHRaylsqqqTPPFAMp 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 -FQSYALFphmtvesnvafglKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALA-------RSLVKRP 169
Cdd:PRK03695   86 vFQYLTLH-------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAG 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 170 KLLLLDEPMSALDkkIRQKTQLE-LVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPN 243
Cdd:PRK03695  153 QLLLLDEPMNSLD--VAQQAALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 39-183 5.28e-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: 92.56  E-value: 5.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  39 VNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP-YRRPVNMMFQSYALFPHMTVESNVAFGL 117
Cdd:cd03231    19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGHAPGIKTTLSVLENLRFWH 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 118 KQEGTpkneikERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDK 183
Cdd:cd03231    99 ADHSD------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
hmuV PRK13547
heme ABC transporter ATP-binding protein;
36-238 1.63e-21

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 92.97  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETAT--------SGKIFVDGEDLASLPPYR----RPVnMMFQSYAL 103
Cdd:PRK13547   17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRlarlRAV-LPQAAQPA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FPhMTVESNVAFG----LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVK---------RPK 170
Cdd:PRK13547   96 FA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 171 LLLLDEPMSALDKKiRQKTQLELVNIIEKV-DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK13547  175 YLLLDEPTAALDLA-HQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 34-231 2.65e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 95.16  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  34 TAVDNVNLTIAKNELFALLGSSGCGKS-TLLRMLAGLETA----TSGKIFVDGEDL--ASLPPYRR----PVNMMFQS-- 100
Cdd:PRK15134   23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhASEQTLRGvrgnKIAMIFQEpm 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHMTVESNVAFGLK-QEGTPKNEIKERVADALALVQMSKYAQRK---PHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:PRK15134  103 VSLNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADE 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 177 PMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQ 231
Cdd:PRK15134  183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 33-233 4.38e-21

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: 95.47  E-value: 4.38e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   33 STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGED-LASLPPYRRPVNMMFQSYALFPHMTVES 111
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFDAIDDLLTGRE 2031

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  112 NVAFGLKQEGTPKNEIkERVAD-ALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQ 190
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEI-EKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1219505750  191 LELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:TIGR01257 2111 NTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 36-245 1.34e-20

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 90.14  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKS----TLLRML-AGLeTATSGKIFVDGEDLASLPPYRRPVNMMFQS--YALFPHMT 108
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGV-RQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFGLKQEGTPKNEIKERVA-DALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkKIRQ 187
Cdd:PRK10418   98 MHTHARETCLALGKPADDATLTAAlEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD-VVAQ 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 188 KTQLELV-NIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSR 245
Cdd:PRK10418  177 ARILDLLeSIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 21-212 3.16e-19

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 85.40  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDS------TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLaslppyrrpv 94
Cdd:COG2401    25 ERVAIVLEAFGVElrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN---------- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 nmmfqsyalfpHMTVESNVAFGLKQEGTPKneikervaDALALVQMSKYAQ-----RKPHQLSGGQQQRVALARSLVKRP 169
Cdd:COG2401    95 -----------QFGREASLIDAIGRKGDFK--------DAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERP 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1219505750 170 KLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQE 212
Cdd:COG2401   156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 36-209 4.78e-19

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 83.36  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKI-FVDGEDLASLPpyRRPvnmmfqsYalFPhmtvesnva 114
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLP--QRP-------Y--LP--------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 115 fglkqEGTpkneikerVADALALvqmskyaqrkP--HQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkirQKTQLE 192
Cdd:cd03223    77 -----LGT--------LREQLIY----------PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129

                         170
                  ....*....|....*..
gi 1219505750 193 LVNIIEKVDVTCVMVTH 209
Cdd:cd03223   130 LYQLLKELGITVISVGH 146
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 42-228 6.37e-19

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: 85.15  E-value: 6.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  42 TIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVnmmfqsyalFPhMTVESNVAFGLKQEG 121
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD---------YE-GTVRDLLSSITKDFY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 122 TpKNEIKERVADALalvQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVD 201
Cdd:cd03237    91 T-HPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166

                         170       180
                  ....*....|....*....|....*..
gi 1219505750 202 VTCVMVTHDQEEAMTMASRLAVMsEGK 228
Cdd:cd03237   167 KTAFVVEHDIIMIDYLADRLIVF-EGE 192
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
32-240 9.12e-19

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 87.77  E-value: 9.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  32 DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLA--SLPPYRRPVNMMFQSYALFpHMTV 109
Cdd:PRK11176  355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVHLF-NDTI 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAFGLKQEGTpKNEIKERVADALALVQMSKYAQ-------RKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK11176  434 ANNIAYARTEQYS-REQIEEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 183 KKIRQKTQLELvNIIEKvDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PRK11176  513 TESERAIQAAL-DELQK-NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLA 567
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
35-242 9.20e-19

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 86.11  E-value: 9.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLE----TATSGKIFVDGEDLASLPPY------RRPVNMMFQ--SYA 102
Cdd:COG4170    22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRerrkiiGREIAMIFQepSSC 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFPHMTVESNVAfglkqEGTPKNEIK--------ERVADALALVQ----------MSKYaqrkPHQLSGGQQQRVALARS 164
Cdd:COG4170   102 LDPSAKIGDQLI-----EAIPSWTFKgkwwqrfkWRKKRAIELLHrvgikdhkdiMNSY----PHELTEGECQKVMIAMA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 165 LVKRPKLLLLDEPMSALDkkirQKTQLELVNIIEKV----DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:COG4170   173 IANQPRLLIADEPTNAME----STTQAQIFRLLARLnqlqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248


                  ..
gi 1219505750 241 FP 242
Cdd:COG4170   249 SP 250
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 35-242 9.94e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.60  E-value: 9.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKS----TLLRML--AGLETATSGKIF--------------------VDGEDLAslp 88
Cdd:PRK10261   31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrrrsrqvielseqsaaqmrhVRGADMA--- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  89 pyrrpvnMMFQS--YALFPHMTVESNVAFGLK-QEGTPKNEI---KERVADALALVQMSKYAQRKPHQLSGGQQQRVALA 162
Cdd:PRK10261  108 -------MIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 163 RSLVKRPKLLLLDEPMSALDKKIrQKTQLELVNIIEK-VDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEVYEF 241
Cdd:PRK10261  181 MALSCRPAVLIADEPTTALDVTI-QAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259


                  .
gi 1219505750 242 P 242
Cdd:PRK10261  260 P 260
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
21-233 1.70e-18

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 87.08  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAV-DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP--PYRRPVNMM 97
Cdd:PRK10790  341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHmTVESNVAFGlkqegtpKNEIKERVADALALVQMSKYAQRKP-----------HQLSGGQQQRVALARSLV 166
Cdd:PRK10790  421 QQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLV 492

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKvdVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK10790  493 QTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQG 556
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 21-210 1.78e-18

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 84.01  E-value: 1.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDgedlaslPPYRrpVNMMFQS 100
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-------GKLR--IGYVPQK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 YALFPHM--TVESnvaFGLKQEGTPKNEIkervADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:PRK09544   76 LYLDTTLplTVNR---FLRLRPGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1219505750 179 SALDkkirQKTQLELVNIIEKV----DVTCVMVTHD 210
Cdd:PRK09544  149 QGVD----VNGQVALYDLIDQLrrelDCAVLMVSHD 180
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-240 1.97e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 87.10  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASlPPYRRPV------ 94
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVcpriay 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 -------NmmfqsyaLFPHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVK 167
Cdd:NF033858   81 mpqglgkN-------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 168 RPKLLLLDEPMSALDKKIRQktQL-ELVNII--EKVDVTcVMV-THDQEEamtmASR---LAVMSEGKIVQIGAPGEVYE 240
Cdd:NF033858  154 DPDLLILDEPTTGVDPLSRR--QFwELIDRIraERPGMS-VLVaTAYMEE----AERfdwLVAMDAGRVLATGTPAELLA 226
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 21-235 3.12e-18

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: 82.07  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGD--STAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP--PYRRPVNM 96
Cdd:cd03369     7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  97 MFQSYALFPHmTVESNVafglkqegTPKNEIKER-VADALALVQMSKyaqrkphQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:cd03369    87 IPQDPTLFSG-TIRSNL--------DPFDEYSDEeIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 176 EPMSAL----DKKIrQKTQLELVNiiekvDVTCVMVTHdqeEAMTMA--SRLAVMSEGKIVQIGAP 235
Cdd:cd03369   151 EATASIdyatDALI-QKTIREEFT-----NSTILTIAH---RLRTIIdyDKILVMDAGEVKEYDHP 207
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 23-212 3.59e-18

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 86.16  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE-DLASLPPYRRpvnmmfqsy 101
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQHRA--------- 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 102 ALFPHMTVESNVAFGlKQEGTpkneIKERVADALALVQ----MSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:PRK11147  393 ELDPEKTVMDNLAEG-KQEVM----VNGRPRHVLGYLQdflfHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEP 467

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1219505750 178 MSALDKKirqktQLELV-NIIEKVDVTCVMVTHDQE 212
Cdd:PRK11147  468 TNDLDVE-----TLELLeELLDSYQGTVLLVSHDRQ 498
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 47-241 5.74e-18

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 85.48  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  47 ELFALLGSSGCGKSTLLRMLAGLETA---TSGKIFVDGEDLaSLPPYRRPVNMMFQSYALFPHMTVESNVAFG--LK-QE 120
Cdd:TIGR00955  52 ELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHLMFQahLRmPR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 121 GTPKNEIKERVADALALVQMSKYAQRK---PHQ---LSGGQQQRVALARSLVKRPKLLLLDEPMSALD-----------K 183
Cdd:TIGR00955 131 RVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmaysvvqvlK 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750 184 KIRQKTQlelvniiekvdvTCVMVTHD-QEEAMTMASRLAVMSEGKIVQIGAPGEVYEF 241
Cdd:TIGR00955 211 GLAQKGK------------TIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 296-376 9.93e-18

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: 76.89  E-value: 9.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 296 ISVRPERIHVSrekpgSKHNWARGVVTDIAYMGSYSLYHVRLPSGKTVVSNLSSSHlmnDNAPAWNDDVFVSWSPASGVV 375
Cdd:pfam08402   1 LAIRPEKIRLA-----AAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAH---ARPPAPGDRVGLGWDPEDAHV 72


                  .
gi 1219505750 376 L 376
Cdd:pfam08402  73 L 73
GguA NF040905
sugar ABC transporter ATP-binding protein;
25-231 2.17e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 83.30  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATS--GKIFVDGE-----DLASlpPYRRPVNMM 97
Cdd:NF040905    6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD--SEALGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVESNVAFGlkqegtpkNEIK-----------ERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:NF040905   84 HQELALIPYLSIAENIFLG--------NERAkrgvidwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 167 KRPKLLLLDEPMSALDKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQ 231
Cdd:NF040905  156 KDVKLLILDEPTAALNEEDSAAL-LDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 36-229 9.33e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 81.59  E-value: 9.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPP---------Y----RR---------- 92
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdglangivYisedRKrdglvlgmsv 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 PVNMMFQSYALFphmtveSNVAFGLKQEgtpknEIKERVADALALVQMSKYAQRKP-HQLSGGQQQRVALARSLVKRPKL 171
Cdd:PRK10762  348 KENMSLTALRYF------SRAGGSLKHA-----DEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKV 416

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 172 LLLDEPMSALD----KKIRQktqleLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK10762  417 LILDEPTRGVDvgakKEIYQ-----LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 25-209 1.63e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 81.61  E-value: 1.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   25 NVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLrmlagleTATSGKIFVDGEDLA--SLPPYRRPVNMMFQSYA 102
Cdd:PTZ00265  1234 NDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTV-------FKNSGKILLDGVDICdyNLKDLRNLFSIVSQEPM 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  103 LFpHMTVESNVAFGlKQEGTpkneiKERVADALALVQMSKYAQRKPHQ-----------LSGGQQQRVALARSLVKRPKL 171
Cdd:PTZ00265  1307 LF-NMSIYENIKFG-KEDAT-----REDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKI 1379

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1219505750  172 LLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTH 209
Cdd:PTZ00265  1380 LLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 38-229 2.02e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 80.48  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRR--------PVNMmfQSYALFPHMTV 109
Cdd:PRK15439  281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylPEDR--QSSGLYLDAPL 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVA------FGLKQEGTPKNEIKERVADALALvqmsKY--AQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:PRK15439  359 AWNVCalthnrRGFWIKPARENAVLERYRRALNI----KFnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1219505750 182 DKKIRQKTqLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK15439  435 DVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 30-201 2.53e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 76.53  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  30 FGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL-ASLPPYRRPVNMMFQSYALFPHMT 108
Cdd:PRK13540   11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFGLKQEGTpKNEIKERVadalALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkirqk 188
Cdd:PRK13540   91 LRENCLYDIHFSPG-AVGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD------ 159

                         170
                  ....*....|...
gi 1219505750 189 tQLELVNIIEKVD 201
Cdd:PRK13540  160 -ELSLLTIITKIQ 171
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
34-184 3.51e-16

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 77.62  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  34 TAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEdlaslpPYRRPVNMMFQSYA--------LFP 105
Cdd:PRK15056   21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQALQKNLVAYVpqseevdwSFP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 106 hMTVESNVAFG----LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:PRK15056   95 -VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173


                  ...
gi 1219505750 182 DKK 184
Cdd:PRK15056  174 DVK 176
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-231 3.98e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 79.57  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  20 FVRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL------ASLppyRRP 93
Cdd:PRK11288    4 YLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAAL---AAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 VNMMFQSYALFPHMTVESNV-------AFGLKQEGTpkneIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLV 166
Cdd:PRK11288   81 VAIIYQELHLVPEMTVAENLylgqlphKGGIVNRRL----LNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750 167 KRPKLLLLDEPMSALdkKIRQKTQL-ELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQ 231
Cdd:PRK11288  157 RNARVIAFDEPTSSL--SAREIEQLfRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 23-233 4.52e-16

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 76.99  E-value: 4.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLE--TATSGKIFVDGEDLASLPPYRRP---VNMM 97
Cdd:CHL00131   10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQSYALFPHMTVES--NVAFGLKQEGTPKNEIK-----ERVADALALVQMS-KYAQRKPHQ-LSGGQQQRVALARSLVKR 168
Cdd:CHL00131   90 FQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLD 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 169 PKLLLLDEPMSALDkkIRQ-KTQLELVNIIEKVDVTCVMVTHDQeeamtmasRLA---------VMSEGKIVQIG 233
Cdd:CHL00131  170 SELAILDETDSGLD--IDAlKIIAEGINKLMTSENSIILITHYQ--------RLLdyikpdyvhVMQNGKIIKTG 234
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 21-182 5.57e-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: 79.21  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVdGE--DLASLPPYRRpvnmmf 98
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvKLAYVDQSRD------ 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 qsyALFPHMTVESNVAFGLKQEGTPKNEIKERvadalALVqmSKYA------QRKPHQLSGGQQQRVALARSLVKRPKLL 172
Cdd:TIGR03719 396 ---ALDPNKTVWEEISGGLDIIKLGKREIPSR-----AYV--GRFNfkgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVL 465

                         170
                  ....*....|
gi 1219505750 173 LLDEPMSALD 182
Cdd:TIGR03719 466 LLDEPTNDLD 475
PLN03211 PLN03211
ABC transporter G-25; Provisional
 22-233 1.42e-15

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 78.38  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATS--GKIFVDGEDLASlpPYRRPVNMMFQ 99
Cdd:PLN03211   70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQ 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFG--LKQEGTPKNEIKERVADA------LALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKL 171
Cdd:PLN03211  148 DDILYPHLTVRETLVFCslLRLPKSLTKQEKILVAESviselgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSL 227

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 172 LLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PLN03211  228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 32-227 1.78e-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: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  32 DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIF------VDGEDLASLPPYRRPVNMMFQSYALFp 105
Cdd:cd03290    13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkneSEPSFEATRSRNRYSVAYAAQKPWLL- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 106 HMTVESNVAFGlkqegTPKNEIKER-VADALAL---VQMSKYAQR-----KPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:cd03290    92 NATVEENITFG-----SPFNKQRYKaVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDD 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 177 PMSALDKKIRQKTQLE-LVNIIEKVDVTCVMVTHdQEEAMTMASRLAVMSEG 227
Cdd:cd03290   167 PFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 21-230 1.79e-15

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 77.68  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGeDL--ASL---PPyrRPVN 95
Cdd:PRK11147    4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLivARLqqdPP--RNVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  96 MmfqsyalfphmTVESNVAFGLKQEGtpknEIKERVADALALV----------QMSKYAQRKPHQ--------------- 150
Cdd:PRK11147   81 G-----------TVYDFVAEGIEEQA----EYLKRYHDISHLVetdpseknlnELAKLQEQLDHHnlwqlenrinevlaq 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 151 -----------LSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkIRQKTQLElvNIIEKVDVTCVMVTHDQEEAMTMAS 219
Cdd:PRK11147  146 lgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--IETIEWLE--GFLKTFQGSIIFISHDRSFIRNMAT 221

                         250
                  ....*....|.
gi 1219505750 220 RLAVMSEGKIV 230
Cdd:PRK11147  222 RIVDLDRGKLV 232
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
39-230 2.92e-15

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 76.87  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  39 VNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLaslpPYRRPVNMMFQSYAL----------FPHMT 108
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI----DIRSPRDAIRAGIMLcpedrkaegiIPVHS 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNVAFGLKQEGTP-KNEIKERVADALALVQMSKYAQRKPH------QLSGGQQQRVALARSLVKRPKLLLLDEPMSAL 181
Cdd:PRK11288  348 VADNINISARRHHLRaGCLINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 182 DKKIRQktqlELVNII---EKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:PRK11288  428 DVGAKH----EIYNVIyelAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 36-229 4.64e-15

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: 76.40  E-value: 4.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-ETATSGKIFVDGEDLASlppyRRPVNMMFQSYALFPH-------- 106
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDI----RNPAQAIRAGIAMVPEdrkrhgiv 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 --MTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPH------QLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:TIGR02633 352 piLGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 179 SALDkkIRQKTQL-ELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:TIGR02633 432 RGVD--VGAKYEIyKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
32-233 5.15e-15

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 76.29  E-value: 5.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  32 DSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNMMFQSYALFPHmTV 109
Cdd:PRK10789  327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAFGlKQEGTPKnEIkERVA-------DALALVQ--MSKYAQRKPhQLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:PRK10789  406 ANNIALG-RPDATQQ-EI-EHVArlasvhdDILRLPQgyDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSA 481

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 181 LDKkiRQKTQLeLVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK10789  482 VDG--RTEHQI-LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG 531
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
50-182 5.40e-15

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 73.34  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  50 ALL--GSSGCGKSTLLRMLAGLETATSGKIFVDGEdlaslpPYRRPVNMMFQSY-----ALFPHMTVESNVAF-----GL 117
Cdd:PRK13543   39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGDRSRFMAYlghlpGLKADLSTLENLHFlcglhGR 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 118 KQEGTPKNeikervadALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PRK13543  113 RAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
21-236 1.03e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 75.62  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGD-STAVDNVnlTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDgEDLASLPPYRRPVnmmfq 99
Cdd:PRK13409  341 VEYPDLTKKLGDfSLEVEGG--EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYIKPD----- 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 syalfPHMTVESNVAFGLKQEGTP--KNEIKERvadaLALVQMskyAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:PRK13409  413 -----YDGTVEDLLRSITDDLGSSyyKSEIIKP----LQLERL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 178 MSALD--------KKIRqktqlelvNIIEKVDVTCVMVTHDqeeaMTMasrLAVMSEGKIVQIGAPG 236
Cdd:PRK13409  481 SAHLDveqrlavaKAIR--------RIAEEREATALVVDHD----IYM---IDYISDRLMVFEGEPG 532
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 26-200 2.52e-14

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: 70.74  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  26 VVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETA--TSGKIFVDGEDLAslPPYRRPVNMMFQSYAL 103
Cdd:cd03232    13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD--KNFQRSTGYVEQQDVH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FPHMTVESNVAFGLKQEGtpkneikervadalalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDEPMSALDk 183
Cdd:cd03232    91 SPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD- 140

                         170
                  ....*....|....*..
gi 1219505750 184 kirQKTQLELVNIIEKV 200
Cdd:cd03232   141 ---SQAAYNIVRFLKKL 154
PLN03073 PLN03073
ABC transporter F family; Provisional
 38-229 3.45e-14

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 74.13  E-value: 3.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIF--------------VDGEDLASlppyrRPVNMMFQSYAL 103
Cdd:PLN03073  527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSS-----NPLLYMMRCFPG 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FPHMTVESNV-AFGlkqegtpkneikerVADALALVQMskyaqrkpHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PLN03073  602 VPEQKLRAHLgSFG--------------VTGNLALQPM--------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1219505750 183 KKIRQKTQLELVNIIEKVdvtcVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PLN03073  660 LDAVEALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
23-232 5.87e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 72.89  E-value: 5.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKfgDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYRRPVNMMF---- 98
Cdd:PRK09700  268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAyite 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 --QSYALFPHMTVESNVAFG--LKQEG--------TPKNEIK--ERVADALALVQMSkyAQRKPHQLSGGQQQRVALARS 164
Cdd:PRK09700  346 srRDNGFFPNFSIAQNMAISrsLKDGGykgamglfHEVDEQRtaENQRELLALKCHS--VNQNITELSGGNQQKVLISKW 423

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 165 LVKRPKLLLLDEPMSALDkkIRQKTqlELVNIIEKV---DVTCVMVTHDQEEAMTMASRLAVMSEGKIVQI 232
Cdd:PRK09700  424 LCCCPEVIIFDEPTRGID--VGAKA--EIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 39-176 9.92e-14

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: 72.52  E-value: 9.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  39 VNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGE--DLASLPPYRrpvNMM---FQSYALFPHMtvesnv 113
Cdd:COG4615   351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQpvTADNREAYR---QLFsavFSDFHLFDRL------ 421

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219505750 114 aFGLKQEGTPkneikERVADALALVQMskyaQRKPH---------QLSGGQQQRVALARSLV-KRPkLLLLDE 176
Cdd:COG4615   422 -LGLDGEADP-----ARARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLeDRP-ILVFDE 483
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 21-182 1.45e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 71.69  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVdGE--DLASLPPYRRpvnmmf 98
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDQSRD------ 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  99 qsyALFPHMTVESNVAFGLKQEGTPKNEIKERvadalALV---------QmskyaQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:PRK11819  398 ---ALDPNKTVWEEISGGLDIIKVGNREIPSR-----AYVgrfnfkggdQ-----QKKVGVLSGGERNRLHLAKTLKQGG 464

                         170
                  ....*....|...
gi 1219505750 170 KLLLLDEPMSALD 182
Cdd:PRK11819  465 NVLLLDEPTNDLD 477
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 31-234 2.23e-13

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 71.90  E-value: 2.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEdLASLPpyrrpvnmmfqSYALFPHMTVE 110
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVP-----------QQAWIQNDSLR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  111 SNVAFGLKQEGTPKNEIKERVAdALALVQMSKYAQR-----KPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:TIGR00957  717 ENILFGKALNEKYYQQVLEACA-LLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750  186 RQktqlelvNIIEKV--------DVTCVMVTHDQeEAMTMASRLAVMSEGKIVQIGA 234
Cdd:TIGR00957  796 GK-------HIFEHVigpegvlkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGS 844
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 28-230 3.91e-13

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: 67.67  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  28 KKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL---ETATSGKIFVDGEDLAS-LPPYRRPVNMMFQSYAL 103
Cdd:cd03233    15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEfAEKYPGEIIYVSEEDVH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 104 FPHMTVESNVAFGLKQEGtpkNEIKERVadalalvqmskyaqrkphqlSGGQQQRVALARSLVKRPKLLLLDEPMSALDk 183
Cdd:cd03233    95 FPTLTVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD- 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 184 kirQKTQLELVNII-EKVDVT--CVMVTHDQ--EEAMTMASRLAVMSEGKIV 230
Cdd:cd03233   151 ---SSTALEILKCIrTMADVLktTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 38-209 5.14e-13

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 70.83  E-value: 5.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFV-DGEDLA--SLPPYRRPVNMMFQSYALFPHmTVESNVA 114
Cdd:PTZ00265   403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKdiNLKWWRSKIGVVSQDPLLFSN-SIKNNIK 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  115 FGL-------------------KQEGT-PKNEIKERVA----------DALALVQMSKYAQ------------------- 145
Cdd:PTZ00265   482 YSLyslkdlealsnyynedgndSQENKnKRNSCRAKCAgdlndmsnttDSNELIEMRKNYQtikdsevvdvskkvlihdf 561

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750  146 -------------RKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTH 209
Cdd:PTZ00265   562 vsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 51-210 5.44e-13

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 69.96  E-value: 5.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  51 LLGSSGCGKSTLLRMLAGLETATSGKIFVDgedlaslPPYRrpVNMMFQSYALFPHMTVESNVAFGL---KQEGTPKNEI 127
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIK--VGYLPQEPQLDPTKTVRENVEEGVaeiKDALDRFNEI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 128 KERVA------DALALVQ--------------------MSKYAQRKP------HQLSGGQQQRVALARSLVKRPKLLLLD 175
Cdd:TIGR03719 107 SAKYAepdadfDKLAAEQaelqeiidaadawdldsqleIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLD 186

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1219505750 176 EPMSALDKkirqKTQLELVNIIEKVDVTCVMVTHD 210
Cdd:TIGR03719 187 EPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 38-238 6.39e-13

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 70.36  E-value: 6.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNMMFQSYALFPHmTVESNV-A 114
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFSG-SLRMNLdP 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  115 FGLKQEgtpkneikERVADALALVQMSKYAQRKP----HQ-------LSGGQQQRVALARSLVKRPKLLLLDEPMSALDk 183
Cdd:TIGR00957 1383 FSQYSD--------EEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD- 1453

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750  184 kirqktqLELVNIIEKV------DVTCVMVTHDQEEAMTMaSRLAVMSEGKIVQIGAPGEV 238
Cdd:TIGR00957 1454 -------LETDNLIQSTirtqfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 45-223 7.16e-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: 65.47  E-value: 7.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   45 KNELFALLGSSGCGKSTLLRMLAGLETATSGK-IFVDGEDLaslppyrrpvnmmfqsyalfphmtvesnvafglkqegtp 123
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDI--------------------------------------- 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  124 kneikervADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTQLE-----LVNIIE 198
Cdd:smart00382  42 --------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKS 113

                          170       180
                   ....*....|....*....|....*
gi 1219505750  199 KVDVTCVMVTHDQEEAMTMASRLAV 223
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRF 138
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 23-230 1.05e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 68.99  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDL---ASLPPYRRPVNMMFQ 99
Cdd:PRK10982    1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTVESNVAFG---LKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:PRK10982   81 ELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 177 PMSALDkkirQKTQLELVNIIEKV-DVTC--VMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:PRK10982  161 PTSSLT----EKEVNHLFTIIRKLkERGCgiVYISHKMEEIFQLCDEITILRDGQWI 213
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
21-238 1.08e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 68.61  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCG--KSTLLRMLAGLETATSGKIF----VDGEDLASLPPYRRPV 94
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*twcANRRALRRTIG*HRPV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSyalfpHMTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:NF000106   94 R*GRRE-----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219505750 175 DEPMSALDKKIRQKTQLELVNIIEKvDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:NF000106  169 DEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 36-229 1.63e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 68.42  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGL-ETATSGKIFVDGEDLAslppYRRPVNMMFQSYALFPH-------- 106
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVK----IRNPQQAIAQGIAMVPEdrkrdgiv 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 107 --MTVESNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPH------QLSGGQQQRVALARSLVKRPKLLLLDEPM 178
Cdd:PRK13549  354 pvMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 179 SALDkkIRQKTQL-ELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK13549  434 RGID--VGAKYEIyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 38-252 2.47e-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: 66.80  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEdlaslppyrrpVNMMFQSYALFPHmTVESNVAFGL 117
Cdd:cd03291    55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 118 KQEgtpknEIKER-VADALALVQ-MSKYAQRKPH-------QLSGGQQQRVALARSLVKRPKLLLLDEPMSALD----KK 184
Cdd:cd03291   123 SYD-----EYRYKsVVKACQLEEdITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfteKE 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750 185 IRQKTQLELVNIIEKVDVTCVMvthdqeEAMTMASRLAVMSEGKIVQIGAPGEVyEFPNSRFSAEFIG 252
Cdd:cd03291   198 IFESCVCKLMANKTRILVTSKM------EHLKKADKILILHEGSSYFYGTFSEL-QSLRPDFSSKLMG 258
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 42-210 3.13e-12

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: 67.89  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  42 TIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDgEDLASLPPYRRPvnmmfqSYalfpHMTVESNVAFGLKqEG 121
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYISP------DY----DGTVEEFLRSANT-DD 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 122 TPKNEIKERVADALALvqmSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD--------KKIRqktqlel 193
Cdd:COG1245   430 FGSSYYKTEIIKPLGL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIR------- 499

                         170
                  ....*....|....*..
gi 1219505750 194 vNIIEKVDVTCVMVTHD 210
Cdd:COG1245   500 -RFAENRGKTAMVVDHD 515
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 21-248 3.81e-12

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: 65.70  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKfgdstAVDNVNLTIAKNELFALLGSSGCGKSTL----LRMLAGLEtatsGKIFVDGEDLASLPPY--RRPV 94
Cdd:cd03288    27 VRYENNLKP-----VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFphmtvESNVAFGLKQEGTPKNEikeRVADALALVQMSKYAQRKPHQL-----------SGGQQQRVALAR 163
Cdd:cd03288    98 SIILQDPILF-----SGSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 164 SLVKRPKLLLLDEPMSALDkkirqktqLELVNIIEKV------DVTCVMVTHDQEEAMTmASRLAVMSEGKIVQIGAPGE 237
Cdd:cd03288   170 AFVRKSSILIMDEATASID--------MATENILQKVvmtafaDRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPEN 240

                         250
                  ....*....|.
gi 1219505750 238 VYEFPNSRFSA 248
Cdd:cd03288   241 LLAQEDGVFAS 251
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
23-251 5.88e-12

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 65.98  E-value: 5.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKF----GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLET----ATSGKIFVDGEDLASLPPYRR-- 92
Cdd:PRK15093    6 IRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrk 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  93 ----PVNMMFQ--SYALFPHMTVESNVAF---GLKQEGTPKNEIKERVADALALVQ----------MSKYaqrkPHQLSG 153
Cdd:PRK15093   86 lvghNVSMIFQepQSCLDPSERVGRQLMQnipGWTYKGRWWQRFGWRKRRAIELLHrvgikdhkdaMRSF----PYELTE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 154 GQQQRVALARSLVKRPKLLLLDEPMSALDKkirqKTQLELVNIIEKVD----VTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK15093  162 GECQKVMIAIALANQPRLLIADEPTNAMEP----TTQAQIFRLLTRLNqnnnTTILLISHDLQMLSQWADKINVLYCGQT 237

                         250       260
                  ....*....|....*....|..
gi 1219505750 230 VQIGAPGEVYEFPNSRFSAEFI 251
Cdd:PRK15093  238 VETAPSKELVTTPHHPYTQALI 259
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 38-253 7.03e-12

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: 67.24  E-value: 7.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEdlASLPPyrrpvnmmfQSYALFPHmTVESNVAFGL 117
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSP---------QTSWIMPG-TIKDNIIFGL 511

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  118 KQEgtpknEIKER-VADALALVQ-MSKYAQRKPH-------QLSGGQQQRVALARSLVKRPKLLLLDEPMSALD----KK 184
Cdd:TIGR01271  512 SYD-----EYRYTsVIKACQLEEdIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvteKE 586

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  185 IRQKTQLELVniiekVDVTCVMVThDQEEAMTMASRLAVMSEGKIVQIGAPGEVY-EFPNsrFSAEFIGS 253
Cdd:TIGR01271  587 IFESCLCKLM-----SNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGL 648
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 51-210 7.62e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 66.68  E-value: 7.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  51 LLGSSGCGKSTLLRMLAGLETATSGKIFVDgedlaslPPYRrpVNMMFQSYALFPHMTVESNVAFGLkQEGTPK----NE 126
Cdd:PRK11819   38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA-------PGIK--VGYLPQEPQLDPEKTVRENVEEGV-AEVKAAldrfNE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 127 IKERVA------DALA--------------------LVQMSKYAQRKPH------QLSGGQQQRVALARSLVKRPKLLLL 174
Cdd:PRK11819  108 IYAAYAepdadfDALAaeqgelqeiidaadawdldsQLEIAMDALRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLL 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1219505750 175 DEPMSALDKkirqktqlELVNIIEK--VDV--TCVMVTHD 210
Cdd:PRK11819  188 DEPTNHLDA--------ESVAWLEQflHDYpgTVVAVTHD 219
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 38-186 7.96e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 63.74  E-value: 7.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLP-PYrrpVNMMFQSYALFPHMTVESNVAFG 116
Cdd:PRK13541   18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKLEMTVFENLKFW 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 117 LKQEGTpkneiKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIR 186
Cdd:PRK13541   95 SEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
35-238 1.27e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 64.45  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEdlaslppyrrpVNMMFQSYALFPHMTVESNVA 114
Cdd:PRK13546   39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 115 FGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTqLELV 194
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC-LDKI 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1219505750 195 NIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK13546  187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 21-229 2.14e-11

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 65.19  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIfvdgedlaslppyrrpvnmmfqs 100
Cdd:PRK10636  313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI----------------------- 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 101 yalfphmtvesNVAFGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQ----------------------LSGGQQQR 158
Cdd:PRK10636  370 -----------GLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQklrdylggfgfqgdkvteetrrFSGGEKAR 438

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 159 VALARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIiekvDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK10636  439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
PLN03232 PLN03232
ABC transporter C family member; Provisional
 21-247 2.27e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.77  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   21 VRIENVVKKF--GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNM 96
Cdd:PLN03232  1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSI 1314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   97 MFQSYALFPHmTVESNVafglkqegTPKNEIKER-VADALALVQMSKYAQRKPHQL-----------SGGQQQRVALARS 164
Cdd:PLN03232  1315 IPQSPVLFSG-TVRFNI--------DPFSEHNDAdLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARA 1385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  165 LVKRPKLLLLDEPMSALDKKIR---QKTQLElvniiEKVDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYEF 241
Cdd:PLN03232  1386 LLRRSKILVLDEATASVDVRTDsliQRTIRE-----EFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459


                   ....*.
gi 1219505750  242 PNSRFS 247
Cdd:PLN03232  1460 DTSAFF 1465
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 22-253 2.67e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 65.52  E-value: 2.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   22 RIENVVKKFGDSTAVD---NVNLTIAKNELFALLGSSGCGKSTLLRMLA----GLETATSGKIFVDGEDLASLPP-YRRP 93
Cdd:TIGR00956   60 RGFRKLKKFRDTKTFDilkPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKhYRGD 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   94 VNMMFQSYALFPHMTVESNVAFGLKQEgTPKNEI----KERVADALALVQMSKYAQRKPHQ----------LSGGQQQRV 159
Cdd:TIGR00956  140 VVYNAETDVHFPHLTVGETLDFAARCK-TPQNRPdgvsREEYAKHIADVYMATYGLSHTRNtkvgndfvrgVSGGERKRV 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  160 ALARSLVKRPKLLLLDEPMSALDkkirQKTQLELVNIIEkvdvTCVMVTHD---------QEEAMTMASRLAVMSEGKIV 230
Cdd:TIGR00956  219 SIAEASLGGAKIQCWDNATRGLD----SATALEFIRALK----TSANILDTtplvaiyqcSQDAYELFDKVIVLYEGYQI 290

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1219505750  231 QIGAPGEVYEF--------PNSRFSAEFIGS 253
Cdd:TIGR00956  291 YFGPADKAKQYfekmgfkcPDRQTTADFLTS 321
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 31-231 4.81e-11

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: 62.56  E-value: 4.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLeTATSGKIFVDGEDLASLP--PYRRPVNMMFQSYALFPHmT 108
Cdd:cd03289    15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPlqKWRKAFGVIPQKVFIFSG-T 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 109 VESNvafgLKQEGTPKNEIKERVADALALVQMskyAQRKPHQL-----------SGGQQQRVALARSLVKRPKLLLLDEP 177
Cdd:cd03289    93 FRKN----LDPYGKWSDEEIWKVAEEVGLKSV---IEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 178 MSALDKKIRQktqlelvnIIEKV------DVTCVMVTHdQEEAMTMASRLAVMSEGKIVQ 231
Cdd:cd03289   166 SAHLDPITYQ--------VIRKTlkqafaDCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
PTZ00243 PTZ00243
ABC transporter; Provisional
 38-230 1.30e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 63.26  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   38 NVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDgEDLASLPPyrrpvnmmfQSYALfpHMTVESNVAFGl 117
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQ---------QAWIM--NATVRGNILFF- 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  118 kqegTPKNEikERVADALALVQM-SKYAQ----------RKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIR 186
Cdd:PTZ00243   745 ----DEEDA--ARLADAVRVSQLeADLAQlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1219505750  187 QKtqlelvnIIEKVDV------TCVMVTHdQEEAMTMASRLAVMSEGKIV 230
Cdd:PTZ00243   819 ER-------VVEECFLgalagkTRVLATH-QVHVVPRADYVVALGDGRVE 860
PTZ00243 PTZ00243
ABC transporter; Provisional
 39-247 1.84e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 62.87  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   39 VNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNMMFQSYALFPHmTVESNVAFG 116
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNVDPF 1407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  117 LkqEGTPKN--------EIKERVA------DALALVQMSKYaqrkphqlSGGQQQRVALARSLVKR-PKLLLLDEPMS-- 179
Cdd:PTZ00243  1408 L--EASSAEvwaalelvGLRERVAsesegiDSRVLEGGSNY--------SVGQRQLMCMARALLKKgSGFILMDEATAni 1477

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219505750  180 --ALDKKIrQKTqlelvniiekvdvtcVMVTHDQEEAMTMASRL---------AVMSEGKIVQIGAPGEVYEFPNSRFS 247
Cdd:PTZ00243  1478 dpALDRQI-QAT---------------VMSAFSAYTVITIAHRLhtvaqydkiIVMDHGAVAEMGSPRELVMNRQSIFH 1540
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 21-230 2.64e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 61.83  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKifVDGEDLASLPPYRRPVNMMF-Q 99
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--VKWSENANIGYYAQDHAYDFeN 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 SYALFPHMTvesnvafglkQEGTPKNEikERVADAlALVQM---SKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDE 176
Cdd:PRK15064  398 DLTLFDWMS----------QWRQEGDD--EQAVRG-TLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 177 PMSALDKKirqktQLELVNI-IEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIV 230
Cdd:PRK15064  465 PTNHMDME-----SIESLNMaLEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 37-182 2.66e-10

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.05  E-value: 2.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   37 DNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETA---TSGKIFVDGEDLASlpPYRRPVNMMFQSYALFPHMTVESNV 113
Cdd:TIGR00956  780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS--SFQRSIGYVQQQDLHLPTSTVRESL 857

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750  114 AFG--LKQ-EGTPKNEIKERVADALALVQMSKYAQR---KPHQ-LSGGQQQRVALARSLVKRPKLLL-LDEPMSALD 182
Cdd:TIGR00956  858 RFSayLRQpKSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
PLN03232 PLN03232
ABC transporter C family member; Provisional
 38-240 5.28e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 61.15  E-value: 5.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   38 NVNLTIAKNELFALLGSSGCGKSTLLR-MLAGLETATSGKIFVDGEdLASLPPyrrpVNMMFQSyalfphmTVESNVAFG 116
Cdd:PLN03232   635 DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-VAYVPQ----VSWIFNA-------TVRENILFG 702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  117 LKQEgtpkNEIKERVADALALVQ---------MSKYAQRKPHqLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQ 187
Cdd:PLN03232   703 SDFE----SERYWRAIDVTALQHdldllpgrdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219505750  188 ktqlELVNIIEKVDV---TCVMVThDQEEAMTMASRLAVMSEGKIVQIGAPGEVYE 240
Cdd:PLN03232   778 ----QVFDSCMKDELkgkTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 21-229 7.42e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 60.41  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAG-------LETATSGKIFVDGEDLASLppyRRp 93
Cdd:PRK10938  261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysNDLTLFGRRRGSGETIWDI---KK- 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  94 vNMMFQSYALfpHMT--VESNV----------AFGLKQEGTPKNEIKerVADALALVQMSKYAQRKP-HQLSGGQQQRVA 160
Cdd:PRK10938  337 -HIGYVSSSL--HLDyrVSTSVrnvilsgffdSIGIYQAVSDRQQKL--AQQWLDILGIDKRTADAPfHSLSWGQQRLAL 411

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 161 LARSLVKRPKLLLLDEPMSALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEA-MTMASRLAVMSEGKI 229
Cdd:PRK10938  412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDApACITHRLEFVPDGDI 481
PLN03130 PLN03130
ABC transporter C family member; Provisional
 39-247 8.07e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 60.91  E-value: 8.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   39 VNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAS--LPPYRRPVNMMFQSYALFphmtvESNVAFG 116
Cdd:PLN03130  1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKVLGIIPQAPVLF-----SGTVRFN 1332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  117 LKqegtPKNEIKErvAD---ALALVQMSKYAQRKPHQL-----------SGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PLN03130  1333 LD----PFNEHND--ADlweSLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219505750  183 KK---IRQKTQLElvniiEKVDVTCVMVTHdQEEAMTMASRLAVMSEGKIVQIGAPGEVYEFPNSRFS 247
Cdd:PLN03130  1407 VRtdaLIQKTIRE-----EFKSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 22-181 1.15e-09

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 59.63  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  22 RIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLAslppYRRP-------V 94
Cdd:PRK10762    6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT----FNGPkssqeagI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  95 NMMFQSYALFPHMTVESNVAFGlKQEGTPKNEIKERV----ADA-LALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRP 169
Cdd:PRK10762   82 GIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKmyaeADKlLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160

                         170
                  ....*....|..
gi 1219505750 170 KLLLLDEPMSAL 181
Cdd:PRK10762  161 KVIIMDEPTDAL 172
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 21-223 2.79e-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: 56.04  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDstAVDNVNL-TIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEDLASLPPYrrpvnmmfq 99
Cdd:cd03222     1 QLYPDCVKRYGV--FFLLVELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 100 syalfphmtvesnvafglkqegtpkneIKervadalalvqmskyaqrkphqLSGGQQQRVALARSLVKRPKLLLLDEPMS 179
Cdd:cd03222    70 ---------------------------ID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSA 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1219505750 180 ALDKKIRQKTQLELVNIIEKVDVTCVMVTHDQEEAMTMASRLAV 223
Cdd:cd03222   101 YLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
PLN03130 PLN03130
ABC transporter C family member; Provisional
 31-187 3.97e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 58.60  E-value: 3.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   31 GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLR-MLAGLETATSGKIFVDGEdLASLPPyrrpVNMMFQSyalfphmTV 109
Cdd:PLN03130   628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-VAYVPQ----VSWIFNA-------TV 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  110 ESNVAFGLKQEGtpknEIKERVADALALVQ---------MSKYAQRKPHqLSGGQQQRVALARSLVKRPKLLLLDEPMSA 180
Cdd:PLN03130   696 RDNILFGSPFDP----ERYERAIDVTALQHdldllpggdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770


                   ....*...
gi 1219505750  181 LDKKI-RQ 187
Cdd:PLN03130   771 LDAHVgRQ 778
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 23-233 4.26e-09

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 56.72  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  23 IENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLE--TATSGKIFVDGEDLASLPPYRRP---VNMM 97
Cdd:PRK09580    4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegIFMA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  98 FQ--------SYALFPHMTVESNVAFgLKQEGTPKNEIKERVADALALVQM-SKYAQRKPHQ-LSGGQQQRVALARSLVK 167
Cdd:PRK09580   84 FQypveipgvSNQFFLQTALNAVRSY-RGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 168 RPKLLLLDEPMSALDKKIrQKTQLELVNIIEKVDVTCVMVTHDQE-EAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK09580  163 EPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 51-210 6.52e-09

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: 56.22  E-value: 6.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  51 LLGSSGCGKSTLLRMLAGLETATSGKI-----------FVDGEDL---------ASLPPYRRPvnmmfQSYALFPHmTVE 110
Cdd:cd03236    31 LVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELqnyftklleGDVKVIVKP-----QYVDLIPK-AVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 111 SNVAFGLKQegTPKNEIKERVADALALVQMskyAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkIRQK-T 189
Cdd:cd03236   105 GKVGELLKK--KDERGKLDELVDQLELRHV---LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRlN 177

                         170       180
                  ....*....|....*....|.
gi 1219505750 190 QLELVNIIEKVDVTCVMVTHD 210
Cdd:cd03236   178 AARLIRELAEDDNYVLVVEHD 198
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 23-182 1.75e-08

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: 56.46  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   23 IENVVKKF--GDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLeTATSGKIFVDGE--DLASLPPYRRPVNMMF 98
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVswNSVTLQTWRKAFGVIP 1298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750   99 QSYALF---------PHMTVESNVAFGLKQEGTPKNEIkERVADALALVQMSkyaqrKPHQLSGGQQQRVALARSLVKRP 169
Cdd:TIGR01271 1299 QKVFIFsgtfrknldPYEQWSDEEIWKVAEEVGLKSVI-EQFPDKLDFVLVD-----GGYVLSNGHKQLMCLARSILSKA 1372

                          170
                   ....*....|...
gi 1219505750  170 KLLLLDEPMSALD 182
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 40-233 1.92e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.79  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  40 NLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDgedlaslppYRRPVNMMF-QSYALFPH--------MTVE 110
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---------FSHITRLSFeQLQKLVSDewqrnntdMLSP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 111 SNVAFGLK-----QEGTPKNEIKERVAdalALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKI 185
Cdd:PRK10938   94 GEDDTGRTtaeiiQDEVKDPARCEQLA---QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1219505750 186 RQktQL-ELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIG 233
Cdd:PRK10938  171 RQ--QLaELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETG 217
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 38-210 5.42e-08

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 52.33  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  38 NVNLTIAKNELFALLGSSGCGKSTLLrmLAGLETATSGKifvdgedLASLPP--YRRPVNMMFQSYALfphmtvesnVAF 115
Cdd:cd03238    13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKAR-------LISFLPkfSRNKLIFIDQLQFL---------IDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 116 GLkqegtpkneikervaDALALvqmskyaQRKPHQLSGGQQQRVALARSLVKRPK--LLLLDEPMSALDkkirQKTQLEL 193
Cdd:cd03238    75 GL---------------GYLTL-------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH----QQDINQL 128

                         170       180
                  ....*....|....*....|
gi 1219505750 194 VNIIEKV---DVTCVMVTHD 210
Cdd:cd03238   129 LEVIKGLidlGNTVILIEHN 148
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 35-238 8.66e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 53.74  E-value: 8.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  35 AVDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKIFVDGEdlASLppyrrpvnmMFQSYALFPHMTVESNVA 114
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AAL---------IAISSGLNGQLTGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 115 FGLKQEGTPKNEIKERVADALALVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKTqLELV 194
Cdd:PRK13545  108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC-LDKM 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1219505750 195 NIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKIVQIGAPGEV 238
Cdd:PRK13545  187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 51-209 1.00e-07

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: 53.98  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  51 LLGSSGCGKSTLLRMLAGLETATSGKIFVDGE-DLASLPpyRRP--VNMMFQSYALFPhMTVESnvafgLKQEGTPKNEI 127
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVP--QRPymTLGTLRDQIIYP-DSSED-----MKRRGLSDKDL 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 128 KErvadALALVQMSKYAQRK---------PHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDKKIRQKtqleLVNIIE 198
Cdd:TIGR00954 555 EQ----ILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY----MYRLCR 626

                         170
                  ....*....|.
gi 1219505750 199 KVDVTCVMVTH 209
Cdd:TIGR00954 627 EFGITLFSVSH 637
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 151-232 2.03e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 52.81  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 151 LSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkIRQKTQL-ELVNIIEKVDVTCVMVTHDQEEAMTMASRLAVMSEGKI 229
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID--VGAKFEIyQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469


                  ...
gi 1219505750 230 VQI 232
Cdd:PRK10982  470 AGI 472
PLN03073 PLN03073
ABC transporter F family; Provisional
 21-182 5.37e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 48.32  E-value: 5.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  21 VRIENVVKKFGDSTAVDNVNLTIAKNELFALLGSSGCGKSTLLRMLA-----GLetATSGKIF-----VDGEDLASL--- 87
Cdd:PLN03073  178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqeVVGDDTTALqcv 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  88 --PPYRRPVNMMFQSYALFPHMTVESNVAFGLKQ----EGTPKNEIKERVA---------DA----------LALVQMSK 142
Cdd:PLN03073  256 lnTDIERTQLLEEEAQLVAQQRELEFETETGKGKgankDGVDKDAVSQRLEeiykrleliDAytaearaasiLAGLSFTP 335

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1219505750 143 YAQRK-PHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALD 182
Cdd:PLN03073  336 EMQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 36-212 9.78e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 47.47  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  36 VDNVNLTIAKNELFALLGSSGCGKSTLLRMLAGLETATSGKI-FVDGEDLA----SLPPYRRP-VNMMFQSYALFPHMTV 109
Cdd:PRK10636   17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAwvnqETPALPQPaLEYVIDGDREYRQLEA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAfglkqegTPKNE------------------IKERVADALALVQMSKYAQRKP-HQLSGGQQQRVALARSLVKRPK 170
Cdd:PRK10636   97 QLHDA-------NERNDghaiatihgkldaidawtIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSD 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1219505750 171 LLLLDEPMSALDkkirqktqLELVNIIEK----VDVTCVMVTHDQE 212
Cdd:PRK10636  170 LLLLDEPTNHLD--------LDAVIWLEKwlksYQGTLILISHDRD 207
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
120-210 1.76e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 46.73  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 120 EGTPKNEIKERVADALALvqmSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkIRQKtqLELVNIIEK 199
Cdd:PRK13409  185 KKVDERGKLDEVVERLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQR--LNVARLIRE 257

                          90
                  ....*....|...
gi 1219505750 200 V--DVTCVMVTHD 210
Cdd:PRK13409  258 LaeGKYVLVVEHD 270
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 24-210 1.86e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 46.42  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  24 ENVVKKFGDStavdnvnltiakNElFALLGSSGCGKSTLLRMLAGLETATSGKIFVD-GEDLASLPpyrrpvnmmfQSYA 102
Cdd:PRK15064   18 ENISVKFGGG------------NR-YGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLR----------QDQF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 103 LFPHMTVESNVAFGLKQEGTPKneiKERvaDAL-ALVQMS------------KYAQ--------RKPHQLSG-------- 153
Cdd:PRK15064   75 AFEEFTVLDTVIMGHTELWEVK---QER--DRIyALPEMSeedgmkvadlevKFAEmdgytaeaRAGELLLGvgipeeqh 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1219505750 154 ---------GQQQRVALARSLVKRPKLLLLDEPMSALD-KKIRQktqleLVNIIEKVDVTCVMVTHD 210
Cdd:PRK15064  150 yglmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDiNTIRW-----LEDVLNERNSTMIIISHD 211
GguA NF040905
sugar ABC transporter ATP-binding protein;
151-238 1.89e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 46.32  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 151 LSGGQQQRVALARSLVKRPKLLLLDEPMSALD---KkirqktqLELVNIIEKVDVT---CVMVTHDQEEAMTMASRLAVM 224
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgaK-------YEIYTIINELAAEgkgVIVISSELPELLGMCDRIYVM 477

                          90
                  ....*....|....
gi 1219505750 225 SEGKIVqigapGEV 238
Cdd:NF040905  478 NEGRIT-----GEL 486
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 50-210 3.91e-05

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: 45.55  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  50 ALLGSSGCGKSTLLRMLAGLETATSGKIfvdgedlaSLPPYRRPVNMMFQSYALFPHMT--VESNVAFGLKQE------- 120
Cdd:COG1245   103 GILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKklANGEIKVAHKPQyvdlipk 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 121 ---GTPKNEIK---ER-VADALA-LVQMSKYAQRKPHQLSGGQQQRVALARSLVKRPKLLLLDEPMSALDkkIRQKtqLE 192
Cdd:COG1245   175 vfkGTVRELLEkvdERgKLDELAeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD--IYQR--LN 250

                         170       180
                  ....*....|....*....|.
gi 1219505750 193 LVNIIE---KVDVTCVMVTHD 210
Cdd:COG1245   251 VARLIRelaEEGKYVLVVEHD 271
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 48-212 5.48e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 43.75  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  48 LFALLGSSGCGKSTLLRmlaGLETATSG-------------KIFVDGEDLASlppyrrpVNMMFQS-----YALFPHMTV 109
Cdd:cd03240    24 LTLIVGQNGAGKTTIIE---ALKYALTGelppnskggahdpKLIREGEVRAQ-------VKLAFENangkkYTITRSLAI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 110 ESNVAFgLKQEgtpkneikervadalalvQMSKYAQRKPHQLSGGQQQ------RVALARSLVKRPKLLLLDEPMSALDK 183
Cdd:cd03240    94 LENVIF-CHQG------------------ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1219505750 184 -KIRQKtqleLVNIIEKVDVTCVM----VTHDQE 212
Cdd:cd03240   155 eNIEES----LAEIIEERKSQKNFqlivITHDEE 184
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
151-212 3.16e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 3.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1219505750 151 LSGGQQQ------RVALARSLVKRPKLLLLDEPMSALDKKIRQKtqleLVNIIEK-------VdvtcVMVTHDQE 212
Cdd:PRK03918  789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRK----LVDIMERylrkipqV----IIVSHDEE 855
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 151-355 3.40e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  151 LSGGQQQRVALARSLVKRPK--LLLLDEPMSALDKKIRQKtqleLVNIIEKV---DVTCVMVTHDqEEAMTMASRlavms 225
Cdd:PRK00635   477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHK----LINVIKKLrdqGNTVLLVEHD-EQMISLADR----- 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  226 egkIVQIGaPGevyefpnsrfsAEFIGSTNLFEGRvvedePDHIFVESDDLEARmYVSHGITGPLgmPVGISVRPERIHV 305
Cdd:PRK00635   547 ---IIDIG-PG-----------AGIFGGEVLFNGS-----PREFLAKSDSLTAK-YLRQELTIPI--PEKRTNSLGTLTL 603

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1219505750  306 SRekpGSKHNwargvVTDIAymgsyslyhVRLPSGK-TVVSNLS---SSHLMND 355
Cdd:PRK00635   604 SK---ATKHN-----LKDLT---------ISLPLGRlTVVTGVSgsgKSSLIND 640
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
151-177 2.15e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 40.01  E-value: 2.15e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1219505750 151 LSGGQQQRVALARSLVKRPK---LLLLDEP 177
Cdd:COG0178   827 LSGGEAQRVKLASELSKRSTgktLYILDEP 856
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 149-212 2.42e-03

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: 38.49  E-value: 2.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219505750 149 HQLSGGQQQRVALA-----RSLVKRPkLLLLDEPMSALDKKIRQKtqleLVNIIEK--VDVTCVMV-THDQE 212
Cdd:cd03227    76 LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQA----LAEAILEhlVKGAQVIViTHLPE 142
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 151-181 3.88e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.23  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1219505750 151 LSGGQQQRVALARSLVKR---PKLLLLDEPMSAL 181
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL 863
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 126-244 4.50e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.23  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750 126 EIKERVA-------DALALvqmskyaQRKPHQLSGGQQQRVALARSL------VkrpkLLLLDEPMSALdkkiRQKTQLE 192
Cdd:TIGR00630 464 EIRERLGflidvglDYLSL-------SRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGL----HQRDNRR 528

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1219505750 193 LVNIIEKV-DV--TCVMVTHDqEEAMTMASRLAVMSE------GKIVQIGAPGEVYEFPNS 244
Cdd:TIGR00630 529 LINTLKRLrDLgnTLIVVEHD-EDTIRAADYVIDIGPgagehgGEVVASGTPEEILANPDS 588
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 151-181 6.33e-03

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 37.98  E-value: 6.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1219505750 151 LSGGQQQRVALARSLVKR---PKLLLLDEPMSAL 181
Cdd:cd03271   170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL 203
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 43-149 6.46e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 37.84  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219505750  43 IAKNELFALL-GSSGCGKSTLLRMLagletatsgkifvdgedLASLPPYRRPVnmmfqsYALFPHMTVES-----NVAFG 116
Cdd:COG3267    39 LAQGGGFVVLtGEVGTGKTTLLRRL-----------------LERLPDDVKVA------YIPNPQLSPAEllraiADELG 95

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1219505750 117 LKQEGTPKNEIKERVADALAlvqmSKYAQRKPH 149
Cdd:COG3267    96 LEPKGASKADLLRQLQEFLL----ELAAAGRRV 124
uvrA PRK00349
excinuclease ABC subunit UvrA;
151-177 7.52e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.52  E-value: 7.52e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1219505750 151 LSGGQQQRVALARSLVKRPK---LLLLDEP 177
Cdd:PRK00349  831 LSGGEAQRVKLAKELSKRSTgktLYILDEP 860
 
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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