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Conserved domains on  [gi|1327293196|gb|PMO54985|]
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ABC transporter ATP-binding protein [Vibrio splendidus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-339 1.15e-168

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 473.05  E-value: 1.15e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:COG3842     3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG3842    83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLV 240
Cdd:COG3842   163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 241 QAN------------------KAKQLFNIETEWKVAIRPESIYVKEQGRQYGEHisapktGTIRNHQLLGNVIRYQVDVD 302
Cdd:COG3842   243 PGTvlgdegggvrtggrtlevPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLP------GTVEDVVFLGSHVRYRVRLG 316

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1327293196 303 E-CELTVDLLNRSSeRLLANGSQLELLFNLNEIQPVRA 339
Cdd:COG3842   317 DgQELVVRVPNRAA-LPLEPGDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-339 1.15e-168

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 473.05  E-value: 1.15e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:COG3842     3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG3842    83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLV 240
Cdd:COG3842   163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 241 QAN------------------KAKQLFNIETEWKVAIRPESIYVKEQGRQYGEHisapktGTIRNHQLLGNVIRYQVDVD 302
Cdd:COG3842   243 PGTvlgdegggvrtggrtlevPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLP------GTVEDVVFLGSHVRYRVRLG 316

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1327293196 303 E-CELTVDLLNRSSeRLLANGSQLELLFNLNEIQPVRA 339
Cdd:COG3842   317 DgQELVVRVPNRAA-LPLEPGDRVGLSWDPEDVVVLPA 353
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-324 3.78e-131

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: 378.23  E-value: 3.78e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLV 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 241 QANKAK---------------QLFNIETEWKVAIRPESIYVKEQGRQYGEhisapKTGTIRNHQLLGNVIRYQV---DVD 302
Cdd:TIGR03265 242 PGTRGGgsrarvggltlacapGLAQPGASVRLAVRPEDIRVSPAGNAANL-----LLARVEDMEFLGAFYRLRLrleGLP 316

                         330       340
                  ....*....|....*....|..
gi 1327293196 303 ECELTVDLLNRSSERLLANGSQ 324
Cdd:TIGR03265 317 GQALVADVSASEVERLGIRAGQ 338
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 7-235 1.95e-123

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: 353.85  E-value: 1.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:cd03300     4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:cd03300    84 FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:cd03300   164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
2-324 6.15e-119

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 347.09  E-value: 6.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   2 SYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVF 81
Cdd:PRK11432    5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:PRK11432   85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQ 241
Cdd:PRK11432  165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 242 ANKAKQLFNI----------------ETEWKVAIRPESIYVKEQGrqygehiSAPKTGTIRNHQLLGNviRYQVDVDECE 305
Cdd:PRK11432  245 ATLSGDYVDIygyrlprpaafafnlpDGECTVGVRPEAITLSEQG-------EESQRCTIKHVAYMGP--QYEVTVDWHG 315

                         330
                  ....*....|....*....
gi 1327293196 306 LTVdLLNRSSERLLANGSQ 324
Cdd:PRK11432  316 QEL-LLQVNATQLQPDLGE 333
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
21-315 4.44e-88

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 268.10  E-value: 4.44e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALFPNMTVEGNIAFGL 100
Cdd:NF040840   18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 101 KMKKLASDEIKR---EVAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIR 177
Cdd:NF040840   98 KLRKVPKEEIERkvkEIMELLGISHLLHR---KPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 178 DIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQ--ANKAKQLFNIETE- 254
Cdd:NF040840  175 RWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgvAEKGGEGTILDTGn 254

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 255 ------------WKVAIRPESIYVKEQGRQygehISAPKT--GTIRNHQLLGNVIRYQVDVdeCELTVDLLNRSS 315
Cdd:NF040840  255 ikielpeekkgkVRIGIRPEDITISTEKVK----TSARNEfkGKVEEIEDLGPLVKLTLDV--GIILVAFITRSS 323
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 4.86e-51

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: 166.28  E-value: 4.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  19 FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFPNMTVEGNI 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  97 AFGLKMKKLASDEIKREVAKVIGLVDLTGKEK----FYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-221 4.25e-32

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 126.78  E-value: 4.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT-HQVPQQRGIGMVFQSY 84
Cdd:NF033858  269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMSQAF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:NF033858  349 SLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLtTIFV-THDQEEAMiMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:NF033858  429 DPVARDMFWRLLIELSREDGV-TIFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-198 9.12e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 112.33  E-value: 9.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  12 RFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGmvfqsyALFPnMT 91
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGL-----KMKKLASDEiKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:NF040873   74 VRDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327293196 167 KIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAM 198
Cdd:NF040873  153 ESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-224 7.20e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 75.55  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG---------EEITHQV--- 71
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrRAVCPRIaym 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  72 PQqrGIGMvfqsyALFPNMTVEGNIAF-----GLkmkklasDEIKREvAKVIGLVDLTGKEKFyPH----QLSGGQRQRV 142
Cdd:NF033858   82 PQ--GLGK-----NLYPTLSVFENLDFfgrlfGQ-------DAAERR-RRIDELLRATGLAPF-ADrpagKLSGGMKQKL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 143 ALARALVVKPRILLLDE------PLSaldakirkhlRQQ----IRDIQKEM-NLTTIFVTHDQEEAMIMsDRIFLMNKGE 211
Cdd:NF033858  146 GLCCALIHDPDLLILDEpttgvdPLS----------RRQfwelIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGR 214

                         250
                  ....*....|...
gi 1327293196 212 IVQAGTPEEIYTQ 224
Cdd:NF033858  215 VLATGTPAELLAR 227
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 28-211 9.65e-15

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: 70.48  E-value: 9.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   28 KGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYalfpnmtvegniafglkmkkla 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  107 sdeikrevakviglvdltgkekfypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRD-----IQK 181
Cdd:smart00382  59 -------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1327293196  182 EMNLTTIFVTHDQE-----EAMIMSDRIFLMNKGE 211
Cdd:smart00382 114 EKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-224 5.10e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 65.91  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCG--KSTLLRSLAGlnPVDGGEIWVNGEEITHQVPQQRGIGM-- 79
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G--PDAGRRPWRF*TWCANRRALRRTIG*hr 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 -----VFQSYALFPNMTVEGNIafgLKMKKLASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRI 154
Cdd:NF000106   92 pvr*gRRESFSGRENLYMIGR*---LDLSRKDARARADELLERFSLTEAAGRAA---AKYSGGMRRRLDLAASMIGRPAV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:NF000106  166 LYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
GguA NF040905
sugar ABC transporter ATP-binding protein;
7-204 9.12e-12

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 65.58  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVdG---GEIWVNGEEITHQV---PQQRGIGMV 80
Cdd:NF040905    5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH-GsyeGEILFDGEVCRFKDirdSEALGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKK-------LASDEIKREVAKViGLVDLtgkekfyPHQLSG----GQRQRVALARALV 149
Cdd:NF040905   84 HQELALIPYLSIAENIFLGNERAKrgvidwnETNRRARELLAKV-GLDES-------PDTLVTdigvGKQQLVEIAKALS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRI 204
Cdd:NF040905  156 KDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSI 209
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-213 3.09e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 48.63  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSL----AGLNPvdGGEIWVNGEEI-THQVPQ--QRGIGMVFQ---SYALF 87
Cdd:NF040905  275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsYGRNI--SGTVFKDGKEVdVSTVSDaiDAGLAYVTEdrkGYGLN 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFGlKMKKLAS----DEIK-REVA---------KVIGLVDLTGKekfyphqLSGGQRQRVALARALVVKPR 153
Cdd:NF040905  353 LIDDIKRNITLA-NLGKVSRrgviDENEeIKVAeeyrkkmniKTPSVFQKVGN-------LSGGNQQKVVLSKWLFTDPD 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 154 ILLLDEPLSALD--AK-----IRKHLRQQIRDIqkemnlttIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:NF040905  425 VLILDEPTRGIDvgAKyeiytIINELAAEGKGV--------IVISSELPELLGMCDRIYVMNEGRIT 483
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-339 1.15e-168

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 473.05  E-value: 1.15e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:COG3842     3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG3842    83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLV 240
Cdd:COG3842   163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 241 QAN------------------KAKQLFNIETEWKVAIRPESIYVKEQGRQYGEHisapktGTIRNHQLLGNVIRYQVDVD 302
Cdd:COG3842   243 PGTvlgdegggvrtggrtlevPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLP------GTVEDVVFLGSHVRYRVRLG 316

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1327293196 303 E-CELTVDLLNRSSeRLLANGSQLELLFNLNEIQPVRA 339
Cdd:COG3842   317 DgQELVVRVPNRAA-LPLEPGDRVGLSWDPEDVVVLPA 353
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-334 2.38e-143

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 409.08  E-value: 2.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:COG3839     1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG3839    81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHY--N 238
Cdd:COG3839   161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 239 LVQANKAKQLFNIE---------------TEWKVAIRPESIYVKEQGrqygehiSAPKTGTIRNHQLLGNVIRYQVDVDE 303
Cdd:COG3839   241 LLPGTVEGGGVRLGgvrlplpaalaaaagGEVTLGIRPEHLRLADEG-------DGGLEATVEVVEPLGSETLVHVRLGG 313

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1327293196 304 CELTVDLlnrSSERLLANGSQLELLFNLNEI 334
Cdd:COG3839   314 QELVARV---PGDTRLRPGDTVRLAFDPERL 341
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-324 3.78e-131

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: 378.23  E-value: 3.78e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLV 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 241 QANKAK---------------QLFNIETEWKVAIRPESIYVKEQGRQYGEhisapKTGTIRNHQLLGNVIRYQV---DVD 302
Cdd:TIGR03265 242 PGTRGGgsrarvggltlacapGLAQPGASVRLAVRPEDIRVSPAGNAANL-----LLARVEDMEFLGAFYRLRLrleGLP 316

                         330       340
                  ....*....|....*....|..
gi 1327293196 303 ECELTVDLLNRSSERLLANGSQ 324
Cdd:TIGR03265 317 GQALVADVSASEVERLGIRAGQ 338
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 1-244 8.56e-130

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 374.48  E-value: 8.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSyVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI-THQVPQQRGIGM 79
Cdd:COG1118     1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDE 159
Cdd:COG1118    80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 160 PLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNL 239
Cdd:COG1118   160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV 239


                  ....*
gi 1327293196 240 VQANK 244
Cdd:COG1118   240 LRGRV 244
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 7-235 1.95e-123

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: 353.85  E-value: 1.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:cd03300     4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:cd03300    84 FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:cd03300   164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
2-324 6.15e-119

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 347.09  E-value: 6.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   2 SYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVF 81
Cdd:PRK11432    5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:PRK11432   85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQ 241
Cdd:PRK11432  165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 242 ANKAKQLFNI----------------ETEWKVAIRPESIYVKEQGrqygehiSAPKTGTIRNHQLLGNviRYQVDVDECE 305
Cdd:PRK11432  245 ATLSGDYVDIygyrlprpaafafnlpDGECTVGVRPEAITLSEQG-------EESQRCTIKHVAYMGP--QYEVTVDWHG 315

                         330
                  ....*....|....*....
gi 1327293196 306 LTVdLLNRSSERLLANGSQ 324
Cdd:PRK11432  316 QEL-LLQVNATQLQPDLGE 333
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 7-216 8.53e-116

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: 333.72  E-value: 8.53e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:cd03259     4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:cd03259    84 FPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03259   164 KLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
7-268 8.44e-114

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 334.61  E-value: 8.44e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:PRK09452   18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYAL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:PRK09452   98 FPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNL------- 239
Cdd:PRK09452  178 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIfdatvie 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1327293196 240 ------VQANKAKQLFNIETEW--------KVAIRPESIYVKE 268
Cdd:PRK09452  258 rldeqrVRANVEGRECNIYVNFavepgqklHVLLRPEDLRVEE 300
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 1-235 1.62e-113

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: 328.91  E-value: 1.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSyVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:cd03296     1 MS-IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLAS----DEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:cd03296    80 FQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:cd03296   160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 34-302 1.00e-106

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: 315.20  E-value: 1.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  34 LLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKRE 113
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 114 VAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHD 193
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 194 QEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQA-------------------NKAKQLFNIE-- 252
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAtvierkseqvvlagvegrrCDIYTDVPVEkd 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327293196 253 TEWKVAIRPESIYVKEQGRQYGEHiSAPktGTIRNHQLLGNVIRYQVDVD 302
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANSSN-AII--GHVIDITYLGMTLEVHVRLE 287
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 8-238 1.58e-104

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 306.34  E-value: 1.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALF 87
Cdd:TIGR00968   5 NISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:TIGR00968  85 KHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 168 IRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYN 238
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-213 3.15e-104

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 306.25  E-value: 3.15e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRF----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQqrg 76
Cdd:COG1116     5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:COG1116    82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNK--GEIV 213
Cdd:COG1116   162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-235 5.87e-102

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 304.07  E-value: 5.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRF-GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGM 79
Cdd:PRK11650    1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLtgkEKFY---PHQLSGGQRQRVALARALVVKPRILL 156
Cdd:PRK11650   81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILEL---EPLLdrkPRELSGGQRQRVAMGRAIVREPAVFL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:PRK11650  158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 7-216 3.75e-100

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: 294.16  E-value: 3.75e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:cd03301     4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIK---REVAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:cd03301    84 YPHMTVYDNIAFGLKLRKVPKDEIDervREVAELLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 6-214 4.65e-99

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: 291.68  E-value: 4.65e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIThqvPQQRGIGMVF 81
Cdd:cd03293     3 VRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGYVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:cd03293    80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNK--GEIVQ 214
Cdd:cd03293   160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
7-239 1.37e-95

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 288.66  E-value: 1.37e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:PRK11607   23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYAL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:PRK11607  103 FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNL 239
Cdd:PRK11607  183 KLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 7-236 2.45e-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: 280.05  E-value: 2.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTV-FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQS 83
Cdd:COG1125     5 ENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKE--KFYPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:COG1125    85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGH 236
Cdd:COG1125   165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
8-249 6.21e-93

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 280.82  E-value: 6.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALF 87
Cdd:PRK10851    7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFGLKM----KKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:PRK10851   87 RHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQAN 243
Cdd:PRK10851  167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQGT 246


                  ....*..
gi 1327293196 244 -KAKQLF 249
Cdd:PRK10851  247 iRGGQFH 253
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
 4-243 7.72e-90

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: 273.41  E-value: 7.72e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG--GEIWVNGEEITHQVPQQRGIGMVF 81
Cdd:TIGR03258   6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKRGLALLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:TIGR03258  86 QNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKEM-NLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLV 240
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245


                  ...
gi 1327293196 241 QAN 243
Cdd:TIGR03258 246 PAI 248
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 8-239 1.07e-88

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 265.74  E-value: 1.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDnTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALF 87
Cdd:cd03299     5 NLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFGLKMKKLASDEIKREV---AKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:cd03299    84 PHMTVYKNIAYGLKKRKVDKKEIERKVleiAEMLGIDHLLNR---KPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNL 239
Cdd:cd03299   161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-235 2.56e-88

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 269.59  E-value: 2.56e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMV 80
Cdd:PRK11000    1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKR---EVAKVIGLVDLTGKEkfyPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:PRK11000   81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQrvnQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:PRK11000  158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
21-315 4.44e-88

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 268.10  E-value: 4.44e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALFPNMTVEGNIAFGL 100
Cdd:NF040840   18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 101 KMKKLASDEIKR---EVAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIR 177
Cdd:NF040840   98 KLRKVPKEEIERkvkEIMELLGISHLLHR---KPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 178 DIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQ--ANKAKQLFNIETE- 254
Cdd:NF040840  175 RWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgvAEKGGEGTILDTGn 254

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 255 ------------WKVAIRPESIYVKEQGRQygehISAPKT--GTIRNHQLLGNVIRYQVDVdeCELTVDLLNRSS 315
Cdd:NF040840  255 ikielpeekkgkVRIGIRPEDITISTEKVK----TSARNEfkGKVEEIEDLGPLVKLTLDV--GIILVAFITRSS 323
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 7-234 1.03e-87

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: 263.38  E-value: 1.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-----RGIGMVF 81
Cdd:COG1127     9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGMLF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKM-KKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG1127    89 QGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEP 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPaNEFVAGFM 234
Cdd:COG1127   169 TAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 7-235 4.75e-85

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: 256.84  E-value: 4.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQS 83
Cdd:cd03295     4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYVIQQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLtGKEKF---YPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:cd03295    84 IGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGL-DPAEFadrYPHELSGGQQQRVGVARALAADPPLLLMDEP 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:cd03295   163 FGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 4-228 9.82e-83

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 250.68  E-value: 9.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH---QVPQQRG-IGM 79
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkDINKLRRkVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIAFGL-KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:COG1126   162 EPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 4-233 4.13e-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: 247.56  E-value: 4.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT---------------VFE---------DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGE 59
Cdd:cd03294     1 IKIKGLYKIFGKNPqkafkllakgkskeeILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  60 IWVNGEEITH-------QVPQQRgIGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPH 132
Cdd:cd03294    81 VLIDGQDIAAmsrkelrELRRKK-ISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 133 QLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03294   160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239

                         250       260
                  ....*....|....*....|.
gi 1327293196 213 VQAGTPEEIYTQPANEFVAGF 233
Cdd:cd03294   240 VQVGTPEEILTNPANDYVREF 260
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 7-233 7.53e-80

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: 243.18  E-value: 7.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-----RGIGMVF 81
Cdd:cd03261     4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGMLF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMK-KLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:cd03261    84 QSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIyTQPANEFVAGF 233
Cdd:cd03261   164 TAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 6-228 1.28e-79

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 251.75  E-value: 1.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRF-----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-----R 75
Cdd:COG1123   263 VRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrR 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQ--SYALFPNMTVEGNIAFGLKMKKLAS-DEIKREVAKVIGLVDLtgKEKF---YPHQLSGGQRQRVALARALV 149
Cdd:COG1123   343 RVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSrAERRERVAELLERVGL--PPDLadrYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:COG1123   421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-229 9.69e-78

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: 238.16  E-value: 9.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFG----DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGI 77
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSY--ALFPNMTVEGNIAFGLKMKKLasDEIKREVAKVIGLVDLTGKEKF-YPHQLSGGQRQRVALARALVVKPRI 154
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEF 229
Cdd:COG1124   160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 11-317 5.13e-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: 240.52  E-value: 5.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  11 KRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ------RGIGMVFQSY 84
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQANK 244
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 245 AKQLFNIETEWKVAIRP----------------ESIYVKEQGRQYGEHISAPKTGTIRNHQL-LGNVIRYQV-DVDECEL 306
Cdd:TIGR01186 241 AERIAQRMNTGPITKTAdkgprsalqlmrdervDSLYVVDRQNKLVGVVDVESIKQARKKAQgLQDVLIDDIyTVDAGTL 320

                         330
                  ....*....|.
gi 1327293196 307 TVDLLNRSSER 317
Cdd:TIGR01186 321 LRETVRKVLKA 331
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
4-213 1.00e-75

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 232.24  E-value: 1.00e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--- 76
Cdd:COG1136     5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 ---IGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPR 153
Cdd:COG1136    85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDqEEAMIMSDRIFLMNKGEIV 213
Cdd:COG1136   165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 4-225 1.24e-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: 1.24e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMV 80
Cdd:COG1122     1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQS--YALFpNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:COG1122    81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:COG1122   160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 7-211 6.60e-75

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: 228.61  E-value: 6.60e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ----VPQQRGIGMVFQ 82
Cdd:cd03229     4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGlkmkklasdeikrevakviglvdltgkekfyphqLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03229    84 DFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTS 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGE 211
Cdd:cd03229   130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 4-212 1.97e-74

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: 228.91  E-value: 1.97e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRF--GDNTVF--EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--- 76
Cdd:cd03255     1 IELKNLSKTYggGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 ---IGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPR 153
Cdd:cd03255    81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMiMSDRIFLMNKGEI 212
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 11-216 2.97e-74

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: 228.33  E-value: 2.97e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  11 KRFGDNTVfeDIEFSIEkGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEI------WVNGEEITHQVPQQRGIGMVFQSY 84
Cdd:cd03297     8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQQRKIGLVFQQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFGLKmkKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:cd03297    85 ALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03297   163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-221 3.38e-72

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 223.79  E-value: 3.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-IGMVFQ 82
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
7-235 4.64e-72

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 223.09  E-value: 4.64e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVfeDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:COG3840     5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMK-KLASDEiKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:COG3840    83 FPHLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 166 AKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMG 235
Cdd:COG3840   162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 4-212 3.24e-71

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 220.48  E-value: 3.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ----QRGIGM 79
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIAFGL----KMKKLASDEIKREVAKVIGLVDltgKEKFYPHQLSGGQRQRVALARALVVKPRIL 155
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPikvkGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAIARALAMNPKVM 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 156 LLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03262   158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
7-228 1.13e-70

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 223.42  E-value: 1.13e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-----RGI 77
Cdd:COG1135     5 ENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRKI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:COG1135    85 GMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLC 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDqeeamiMS------DRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:COG1135   165 DEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQSE 235
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 4-213 1.80e-70

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: 218.91  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRF----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--- 76
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 --IGMVFQSY--ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKF---YPHQLSGGQRQRVALARALV 149
Cdd:cd03257    82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 7-226 9.16e-70

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: 225.94  E-value: 9.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF--GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG---GEIWVNGEEITHQVPQQRG--IGM 79
Cdd:COG1123     8 RDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGrrIGM 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQS--YALFPnMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:COG1123    88 VFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:COG1123   167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 8-242 2.20e-69

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: 220.74  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDntvFE-DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGE-----EITHQVP-QQRGIGMV 80
Cdd:COG4148     6 DFRLRRGG---FTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPpHRRRIGYV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGlkMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG4148    83 FQEARLFPHLSVRGNLLYG--RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAkirkHLRQQI----RDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGH 236
Cdd:COG4148   161 LAALDL----ARKAEIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEA 236


                  ....*.
gi 1327293196 237 YNLVQA 242
Cdd:COG4148   237 GSVLEA 242
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 6-223 1.21e-68

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 215.29  E-value: 1.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--IGMVFQS 83
Cdd:COG1120     4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVPQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFG----LKMKKLASDEIKREVAKVIGLVDLTG-KEKFYpHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:COG1120    84 PPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHlADRPV-DELSGGERQRVLIARALAQEPPLLLLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:COG1120   163 EPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
4-236 8.96e-67

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 209.95  E-value: 8.96e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGI----GM 79
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAK-VIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK09493   82 VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGH 236
Cdd:PRK09493  162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQH 238
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-216 1.48e-66

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 208.75  E-value: 1.48e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF-GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QVPQ-QRGIGMV 80
Cdd:COG2884     5 ENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYlRRRIGVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:COG2884    85 FQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 161 LSALDAKirkhLRQQIRDIQKEMNL--TTIFV-THDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:COG2884   165 TGNLDPE----TSWEIMELLEEINRrgTTVLIaTHDLELVDRMPKRVLELEDGRLVRDE 219
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 4-225 1.97e-66

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 208.97  E-value: 1.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT-----HQVPQQ 74
Cdd:cd03258     2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgkELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRI 154
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 7-224 2.27e-66

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: 209.98  E-value: 2.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVF--EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG-----EEITHQVPQQrgIGM 79
Cdd:TIGR04520   4 ENVSFSYPESEKPalKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldEENLWEIRKK--VGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSyalfP-----NMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRI 154
Cdd:TIGR04520  82 VFQN----PdnqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAmIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 7-211 7.70e-65

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 203.85  E-value: 7.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--IGMVFQ 82
Cdd:cd03225     3 KNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 syalFP-----NMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:cd03225    83 ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGE 211
Cdd:cd03225   159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 7-226 2.86e-64

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: 206.06  E-value: 2.86e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF--GDNTVF--EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP---VDGGEIWVNGEEITHQVPQQ----R 75
Cdd:COG0444     5 RNLKVYFptRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkiR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 G--IGMVFQ-SY-ALFPNMTVEGNIAFGLKMKKLAS-DEIKREVAKVIGLVDLTGKEKF---YPHQLSGGQRQRVALARA 147
Cdd:COG0444    85 GreIQMIFQdPMtSLNPVMTVGDQIAEPLRIHGGLSkAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIARA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:COG0444   165 LALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-214 8.08e-64

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 203.17  E-value: 8.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQrg 76
Cdd:COG4525     1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 iGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:COG4525    79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLM--NKGEIVQ 214
Cdd:COG4525   158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 7-221 1.26e-63

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 202.21  E-value: 1.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF-GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-----RGIGMV 80
Cdd:COG3638     6 RNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGMI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGL--------KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKP 152
Cdd:COG3638    86 FQQFNLVPRLSVLTNVLAGRlgrtstwrSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG3638   166 KLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 4-225 4.67e-63

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: 201.53  E-value: 4.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFE-----DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ---- 74
Cdd:TIGR04521   1 IKLKNVSYIYQPGTPFEkkaldDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 -RGIGMVFQ--SYALFPNmTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLtgKEKFY---PHQLSGGQRQRVALARAL 148
Cdd:TIGR04521  81 rKKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGL--DEEYLersPFELSGGQMRRVAIAGVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 149 VVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 4-221 1.39e-62

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: 198.94  E-value: 1.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPV-----DGGEIWVNGEEITHQ----VPQQ 74
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdvdvLELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGMVFQSYALFPnMTVEGNIAFGLKMKKLAS-DEIKREVAKVIGLVDLTG--KEKFYPHQLSGGQRQRVALARALVVK 151
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 7-197 1.42e-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: 1.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVD---GGEIWVNGEEITHQVPQQRGIGMVFQS 83
Cdd:COG4136     5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLKmKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:COG4136    85 DLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEA 197
Cdd:COG4136   164 LDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
6-212 6.32e-61

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 193.88  E-value: 6.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQS 83
Cdd:COG4619     3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNmTVEGNIAFGLKMKKLASDEIK-REVAKVIGL-VDLTGKEkfyPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:COG4619    83 PALWGG-TVRDNLPFPFQLRERKFDRERaLELLERLGLpPDILDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:COG4619   159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
 4-234 3.10e-60

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


Pssm-ID: 132050 [Multi-domain]  Cd Length: 252  Bit Score: 193.51  E-value: 3.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ------------- 70
Cdd:TIGR03005   1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMpgrngplvpadek 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  71 -VPQQRG-IGMVFQSYALFPNMTVEGNIAFG-LKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARA 147
Cdd:TIGR03005  81 hLRQMRNkIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPAN 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240


                  ....*..
gi 1327293196 228 EFVAGFM 234
Cdd:TIGR03005 241 ERTREFL 247
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 5-228 6.23e-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: 192.38  E-value: 6.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   5 NAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-QRGIGMVFQS 83
Cdd:COG4555     3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:COG4555    83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:COG4555   163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 4-226 1.21e-59

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 194.57  E-value: 1.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRF---------GDNTV--FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH--- 69
Cdd:COG4608     8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlsg 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  70 --QVPQQRGIGMVFQ-SYA-LFPNMTVEGNIAFGLKMKKLAS-DEIKREVAKVIGLVDLtgKEKF---YPHQLSGGQRQR 141
Cdd:COG4608    88 reLRPLRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLASkAERRERVAELLELVGL--RPEHadrYPHEFSGGQRQR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 142 VALARALVVKPRILLLDEPLSALDAKIRKhlrqQI----RDIQKEMNLTTIFVTHDQeeAMI--MSDRIFLMNKGEIVQA 215
Cdd:COG4608   166 IGIARALALNPKLIVCDEPVSALDVSIQA----QVlnllEDLQDELGLTYLFISHDL--SVVrhISDRVAVMYLGKIVEI 239

                         250
                  ....*....|.
gi 1327293196 216 GTPEEIYTQPA 226
Cdd:COG4608   240 APRDELYARPL 250
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 4-212 2.24e-58

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: 186.06  E-value: 2.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-IGMVFQ 82
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIafglkmkklasdeikrevakviglvdltgkekfyphQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-226 3.31e-58

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 187.99  E-value: 3.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ------VPQQ 74
Cdd:COG1121     4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigyVPQR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGmvfqsyALFPnMTVEGNIAFGL----KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVV 150
Cdd:COG1121    84 AEVD------WDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 151 KPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGeIVQAGTPEEIYTQPA 226
Cdd:COG1121   157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 6-216 6.49e-58

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 184.95  E-value: 6.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--IGMVFQs 83
Cdd:cd03214     2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVPQ- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 yalfpnmtvegniafglkmkklasdeikreVAKVIGLVDLtgKEKFYpHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:cd03214    81 ------------------------------ALELLGLAHL--ADRPF-NELSGGERQRVLLARALAQEPPILLLDEPTSH 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03214   128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 7-228 1.69e-57

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: 186.23  E-value: 1.69e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQRG-IGMV 80
Cdd:cd03256     4 ENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLRRqIGMI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGL-----KMKKLASDEIKREVAKVIGLVDLTG-KEKFYPH--QLSGGQRQRVALARALVVKP 152
Cdd:cd03256    84 FQQFNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALERVGlLDKAYQRadQLSGGQQQRVAIARALMQQP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:cd03256   164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 20-221 9.29e-56

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: 181.51  E-value: 9.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLN-PVDGGeIWVNGEEITHQVPQQRgigMVFQSYALFPNMTVEGNIAF 98
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAqPTSGG-VILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  99 GLK--MKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQI 176
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1327293196 177 RDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-228 4.66e-55

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 179.78  E-value: 4.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  24 FSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALFPNMTVEGNIAFGLKMK 103
Cdd:PRK10771   20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 104 -KLASDEIK--REVAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQ 180
Cdd:PRK10771  100 lKLNAAQREklHAIARQMGIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1327293196 181 KEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:PRK10771  177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 6-197 1.10e-54

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: 177.67  E-value: 1.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-IGMVFQSY 84
Cdd:COG4133     5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGHAD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFGLKMKKLASDEikREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:COG4133    85 GLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1327293196 165 DAKIRKHLRQQIRDiQKEMNLTTIFVTHDQEEA 197
Cdd:COG4133   163 DAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 6-226 1.70e-54

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: 179.08  E-value: 1.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMVFQ 82
Cdd:COG0411     7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIA---------------FGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARA 147
Cdd:COG0411    87 NPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:COG0411   167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 6-221 2.30e-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: 177.31  E-value: 2.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGD--NTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI-THQVPQQRGIGMVFQ 82
Cdd:cd03263     3 IRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYCPQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03263    83 FDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKemNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:cd03263   163 GLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 4-220 4.43e-54

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: 177.24  E-value: 4.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QVPQQR 75
Cdd:COG4181     9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 G--IGMVFQSYALFPNMTVEGNIAFGLKmkkLASDEIKREVAK-VIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKP 152
Cdd:COG4181    89 ArhVGFVFQSFQLLPTLTALENVMLPLE---LAGRRDARARARaLLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMiMSDRIFLMNKGEIVQAGTPEE 220
Cdd:COG4181   166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 7-228 7.67e-54

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 180.00  E-value: 7.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF--GDNTV--FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-----RGI 77
Cdd:PRK11153    5 KNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:PRK11153   85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:PRK11153  165 DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 4-221 1.66e-53

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: 175.25  E-value: 1.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-QRGIGMVFQ 82
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03265    81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:cd03265   161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
1-224 2.19e-53

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 177.16  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSyVNAKNLTKRFGDNTVFE-----DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-- 73
Cdd:PRK13637    1 MS-IKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKls 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  74 --QRGIGMVFQ--SYALFPNmTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDL---TGKEKfYPHQLSGGQRQRVALAR 146
Cdd:PRK13637   80 diRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyeDYKDK-SPFELSGGQKRRVAIAG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 147 ALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK13637  158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 7-224 4.54e-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: 174.79  E-value: 4.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQRG-IGMV 80
Cdd:TIGR02315   5 ENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITklrgKKLRKLRRrIGMI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGL--------KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKP 152
Cdd:TIGR02315  85 FQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQP 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 7-212 5.47e-53

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 175.25  E-value: 5.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIwVNGEEITHQVpqQRGIGMVFQSYAL 86
Cdd:PRK11247   16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEA--REDTRLMFQDARL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASdeiKREVAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:PRK11247   93 LPWKKVIDNVGLGLKGQWRDA---ALQALAAVGLADRANE---WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:PRK11247  167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 8-211 7.90e-53

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


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 173.20  E-value: 7.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QVPQ-QRGIGMVF 81
Cdd:TIGR02673   6 NVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrQLPLlRRRIGVVF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:TIGR02673  86 QDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPT 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 162 SALDAkirkHLRQQIRDIQKEMN---LTTIFVTHDQEEAMIMSDRIFLMNKGE 211
Cdd:TIGR02673 166 GNLDP----DLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDGR 214
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-236 8.90e-53

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 174.17  E-value: 8.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP--QQRG-- 76
Cdd:PRK11264    1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQKGli 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 ------IGMVFQSYALFPNMTVEGNIAFG-LKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALV 149
Cdd:PRK11264   81 rqlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE- 228
Cdd:PRK11264  161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPr 239

                         250
                  ....*....|.
gi 1327293196 229 ---FVAGFMGH 236
Cdd:PRK11264  240 trqFLEKFLLQ 250
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 6-221 1.81e-52

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: 173.01  E-value: 1.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMVFQ 82
Cdd:cd03219     3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLAS----------DEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKP 152
Cdd:cd03219    83 IPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:cd03219   163 KLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 7-221 3.85e-52

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 183.11  E-value: 3.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEItHQVPQQ---RGIGMVF 81
Cdd:COG2274   477 ENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-RQIDPAslrRQIGVVL 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFpNMTVEGNIAFGlkmKKLASDEIKREVAKVIGLVDLTGKekfYPH-----------QLSGGQRQRVALARALVV 150
Cdd:COG2274   556 QDVFLF-SGTIRENITLG---DPDATDEEIIEAARLAGLHDFIEA---LPMgydtvvgeggsNLSGGQRQRLAIARALLR 628

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 151 KPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDqEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG2274   629 NPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 7-221 4.77e-52

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: 171.46  E-value: 4.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMVFQS 83
Cdd:cd03224     4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLkmKKLASDEIKREVAKVIGLV-DLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03224    84 RRIFPELTVEENLLLGA--YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 163 ALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:cd03224   162 GLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 21-228 5.23e-52

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: 179.88  E-value: 5.23e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPvDGGEIWVNGEEITHQVPQQ-----RGIGMVFQS-YA-LFPNMTVE 93
Cdd:COG4172   304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVG 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  94 GNIAFGLK--MKKLASDEIKREVAKVIGLVDLTGKEKF-YPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRK 170
Cdd:COG4172   383 QIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQA 462

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 171 hlrqQI----RDIQKEMNLTTIFVTHDQeeAMI--MSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:COG4172   463 ----QIldllRDLQREHGLAYLFISHDL--AVVraLAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
6-234 5.87e-52

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 172.29  E-value: 5.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT--------------HQV 71
Cdd:COG4598    11 VRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpadrRQL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  72 PQQRG-IGMVFQSYALFPNMTVEGNIAFG----LKM-KKLASDEIKREVAKViGLVDltgKEKFYPHQLSGGQRQRVALA 145
Cdd:COG4598    91 QRIRTrLGMVFQSFNLWSHMTVLENVIEApvhvLGRpKAEAIERAEALLAKV-GLAD---KRDAYPAHLSGGQQQRAAIA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 146 RALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:COG4598   167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245


                  ....*....
gi 1327293196 226 ANEFVAGFM 234
Cdd:COG4598   246 KSERLRQFL 254
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 8-226 8.38e-52

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 174.92  E-value: 8.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVfeDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ------VPQQRGIGMVF 81
Cdd:TIGR02142   4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPEKRRIGYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKRE-VAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:TIGR02142  82 QEARLFPHLSVRGNLRYGMKRARPSERRISFErVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-211 2.09e-51

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: 167.42  E-value: 2.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQs 83
Cdd:cd00267     2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 yalfpnmtvegniafglkmkklasdeikrevakviglvdltgkekfyphqLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:cd00267    81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGE 211
Cdd:cd00267   111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 1-236 4.14e-51

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 169.81  E-value: 4.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSyVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI---THQVPQQ--- 74
Cdd:PRK11124    1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAire 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 --RGIGMVFQSYALFPNMTVEGN-IAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVK 151
Cdd:PRK11124   80 lrRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQkEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTpEEIYTQPANEFVA 231
Cdd:PRK11124  160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFK 237


                  ....*
gi 1327293196 232 GFMGH 236
Cdd:PRK11124  238 NYLSH 242
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
7-236 4.52e-51

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 169.81  E-value: 4.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEE------ITHQVPQQ--RGIG 78
Cdd:COG4161     6 KNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLlrQKVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQSYALFPNMTVEGN-IAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:COG4161    86 MVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQkEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTpEEIYTQPANEFVAGFMGH 236
Cdd:COG4161   166 DEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLSH 242
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 4.86e-51

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: 166.28  E-value: 4.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  19 FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFPNMTVEGNI 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  97 AFGLKMKKLASDEIKREVAKVIGLVDLTGKEK----FYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
20-248 1.03e-50

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 173.30  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH------QVPQQRGIGMVFQSYALFPNMTVE 93
Cdd:PRK10070   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQSFALMPHMTVL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  94 GNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLR 173
Cdd:PRK10070  125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 174 QQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFMGHYNLVQANKAKQL 248
Cdd:PRK10070  205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDI 279
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 21-216 1.20e-50

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: 167.67  E-value: 1.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALFPNMTVEGNIAFGL 100
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 101 KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQ 180
Cdd:cd03298    96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1327293196 181 KEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03298   176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 6-228 2.19e-50

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 168.29  E-value: 2.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP-VDG----GEIWVNGEEI----THQVPQQRG 76
Cdd:COG1117    14 VRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIydpdVDVVELRRR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYALFPnMTVEGNIAFGLKMKKLAS----DEIKREVAKVIGLVD-----LtgkekfypHQ----LSGGQRQRVA 143
Cdd:COG1117    94 VGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSkselDEIVEESLRKAALWDevkdrL--------KKsalgLSGGQQQRLC 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 144 LARALVVKPRILLLDEPLSALD----AKIrkhlRQQIRDIQKEMnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPE 219
Cdd:COG1117   165 IARALAVEPEVLLMDEPTSALDpistAKI----EELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238


                  ....*....
gi 1327293196 220 EIYTQPANE 228
Cdd:COG1117   239 QIFTNPKDK 247
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 6-224 6.47e-50

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 167.26  E-value: 6.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQS 83
Cdd:PRK13548    5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YAL-FPnMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTG-KEKFYPhQLSGGQRQRVALARALV------VKPRIL 155
Cdd:PRK13548   85 SSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 156 LLDEPLSALDakirkhLRQQI------RDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK13548  163 LLDEPTSALD------LAHQHhvlrlaRQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 7-223 7.04e-50

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 167.48  E-value: 7.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGD--NTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT-HQVPQQRG-IGMVFQ 82
Cdd:PRK13632   11 ENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKkIGIIFQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SY-ALFPNMTVEGNIAFGLKMKKLASDEIKR---EVAKVIGLVDLTGKEkfyPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13632   91 NPdNQFIGATVEDDIAFGLENKKVPPKKMKDiidDLAKKVGMEDYLDKE---PQNLSGGQKQRVAIASVLALNPEIIIFD 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAmIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:PRK13632  168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 6-224 8.36e-50

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: 174.56  E-value: 8.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDN-TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQ 82
Cdd:COG4988   339 LEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWVPQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPnMTVEGNIAFGlkmKKLASDEikrEVAKVIGLVDLTGKEKFYPH-----------QLSGGQRQRVALARALVVK 151
Cdd:COG4988   419 NPYLFA-GTIRENLRLG---RPDASDE---ELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRD 491

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTHDQEEAMIMsDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:COG4988   492 APLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
4-222 1.73e-49

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 166.73  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGM 79
Cdd:PRK13635    6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSY-ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13635   86 VFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMiMSDRIFLMNKGEIVQAGTPEEIY 222
Cdd:PRK13635  166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIF 228
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 6-216 4.88e-49

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 163.47  E-value: 4.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHqvpQQRGIGMVFQSYA 85
Cdd:cd03235     2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 L---FPnMTVEGNIAFGL----KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:cd03235    79 IdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKgEIVQAG 216
Cdd:cd03235   158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 4-211 7.40e-49

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 161.40  E-value: 7.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI----THQVPQQrgI 77
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdldLESLRKN--I 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFpNMTVEGNIafglkmkklasdeikrevakviglvdltgkekfyphqLSGGQRQRVALARALVVKPRILLL 157
Cdd:cd03228    79 AYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDqEEAMIMSDRIFLMNKGE 211
Cdd:cd03228   121 DEATSALDPETEALILEALRALAKGK--TVIVIAHR-LSTIRDADRIIVLDDGR 171
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 7-204 1.09e-48

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: 162.40  E-value: 1.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG------IGMV 80
Cdd:TIGR03608   2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrrekLGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:TIGR03608  82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMiMSDRI 204
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAK-QADRV 203
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-220 3.01e-48

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 170.73  E-value: 3.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIThQVPQQ---RGIGMVFQSYALFpNM 90
Cdd:COG1132   351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLEslrRQIGVVPQDTFLF-SG 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  91 TVEGNIAFGlkmKKLASDEIKREVAKVIGLVDLTgkEKFyPH-----------QLSGGQRQRVALARALVVKPRILLLDE 159
Cdd:COG1132   429 TIRENIRYG---RPDATDEEVEEAAKAAQAHEFI--EAL-PDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 160 PLSALDAKIRKHLRQQIRDIQKemNLTTIFVTH------DqeeamimSDRIFLMNKGEIVQAGTPEE 220
Cdd:COG1132   503 ATSALDTETEALIQEALERLMK--GRTTIVIAHrlstirN-------ADRILVLDDGRIVEQGTHEE 560
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-222 3.37e-48

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 163.36  E-value: 3.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNT---VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQV--PQQR 75
Cdd:PRK13650    2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQSY-ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRI 154
Cdd:PRK13650   82 KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEaMIMSDRIFLMNKGEIVQAGTPEEIY 222
Cdd:PRK13650  162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 7-226 5.96e-48

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: 161.30  E-value: 5.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMVFQS 83
Cdd:COG0410     7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLKMKKlASDEIKREVAKVIGLV-DLtgKEKFypHQ----LSGGQRQRVALARALVVKPRILLLD 158
Cdd:COG0410    87 RRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRL--KERR--RQragtLSGGEQQMLAIGRALMSRPKLLLLD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:COG0410   162 EPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-213 7.80e-48

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 161.79  E-value: 7.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTV-----FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-- 76
Cdd:COG1101     2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYAL--FPNMTVEGNIA--------FGLKMKKLAS--DEIKREVAKV-IGLVD-LTGKEKFyphqLSGGQRQRV 142
Cdd:COG1101    82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKrrELFRELLATLgLGLENrLDTKVGL----LSGGQRQAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 143 ALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:COG1101   158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
5-214 1.19e-47

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 161.41  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   5 NAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQrgiGMVFQSY 84
Cdd:PRK11248    3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQNE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:PRK11248   80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLM--NKGEIVQ 214
Cdd:PRK11248  160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
7-228 2.10e-47

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 160.77  E-value: 2.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT---------VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG- 76
Cdd:COG4167     8 RNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCk 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 -IGMVFQ--SYALFPNMTVeGNIafgLKMK-KLASD--EIKRE--VAKVIGLVDLTGKEK-FYPHQLSGGQRQRVALARA 147
Cdd:COG4167    88 hIRMIFQdpNTSLNPRLNI-GQI---LEEPlRLNTDltAEEREerIFATLRLVGLLPEHAnFYPHMLSSGQKQRVALARA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQeeAMI--MSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:COG4167   164 LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHL--GIVkhISDKVLVMHQGEVVEYGKTAEVFANP 241


                  ...
gi 1327293196 226 ANE 228
Cdd:COG4167   242 QHE 244
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 4-226 7.41e-47

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: 166.48  E-value: 7.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRF--GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGM 79
Cdd:COG4987   334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFpNMTVEGNIAFGlkmKKLASDEikrEVAKVIGLVDLtgkEKFY---PH-----------QLSGGQRQRVALA 145
Cdd:COG4987   414 VPQRPHLF-DTTLRENLRLA---RPDATDE---ELWAALERVGL---GDWLaalPDgldtwlgeggrRLSGGERRRLALA 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 146 RALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDQEEAMIMsDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:COG4987   484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560


                  .
gi 1327293196 226 A 226
Cdd:COG4987   561 G 561
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 7-212 1.16e-46

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: 157.18  E-value: 1.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTV-FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QVPQ-QRGIGMV 80
Cdd:cd03292     4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYlRRKIGVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:cd03292    84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKeMNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03292   164 TGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 6-226 2.07e-46

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: 157.32  E-value: 2.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMVFQ 82
Cdd:cd03218     3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03218    83 EASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 163 ALDAKIRKHLRQQIRDIqKEMNLtTIFVT-HDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:cd03218   163 GVDPIAVQDIQKIIKIL-KDRGI-GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-230 2.20e-46

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 157.50  E-value: 2.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GI 77
Cdd:COG1137     1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:COG1137    81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 158 DEPLSALD----AKIRK---HLRQqiRDIqkemnltTIFVT-HDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYtqpANEF 229
Cdd:COG1137   161 DEPFAGVDpiavADIQKiirHLKE--RGI-------GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL---NNPL 228


                  .
gi 1327293196 230 V 230
Cdd:COG1137   229 V 229
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
5-225 2.98e-46

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 157.58  E-value: 2.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   5 NAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQ 82
Cdd:COG4559     3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYAL-FPnMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTG-KEKFYPhQLSGGQRQRVALARALV-------VKPR 153
Cdd:COG4559    83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 154 ILLLDEPLSALDakirkhLRQQIR--DIQKEM---NLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:COG4559   161 WLFLDEPTSALD------LAHQHAvlRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 12-216 4.97e-46

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 155.79  E-value: 4.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  12 RFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYALFPNMT 91
Cdd:TIGR01277   7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGLK--MKKLASDEIKRE-VAKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKI 168
Cdd:TIGR01277  87 VRQNIGLGLHpgLKLNAEQQEKVVdAAQQVGIADYLDR---LPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1327293196 169 RKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 7-226 9.41e-46

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: 162.93  E-value: 9.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP----VDGGEIWVNGEEITHQVPQQ---- 74
Cdd:COG4172    10 EDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERElrri 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RG--IGMVFQ--SYALFPNMTVEGNIAFGLKMKKLASDEIKRevAKVIGLVDLTG------KEKFYPHQLSGGQRQRVAL 144
Cdd:COG4172    90 RGnrIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGLSGAAAR--ARALELLERVGipdperRLDAYPHQLSGGQRQRVMI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 145 ARALVVKPRILLLDEPLSALDAKIRKhlrqQI----RDIQKEMNLTTIFVTHDQeeAMI--MSDRIFLMNKGEIVQAGTP 218
Cdd:COG4172   168 AMALANEPDLLIADEPTTALDVTVQA----QIldllKDLQRELGMALLLITHDL--GVVrrFADRVAVMRQGEIVEQGPT 241


                  ....*...
gi 1327293196 219 EEIYTQPA 226
Cdd:COG4172   242 AELFAAPQ 249
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 20-234 1.34e-45

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 157.95  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR-----GIGMVFQS--YALFPNMTV 92
Cdd:PRK15079   38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTI 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAFGLKM--KKLASDEIKREV----AKVIGLVDLTGKekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:PRK15079  118 GEIIAEPLRTyhPKLSRQEVKDRVkammLKVGLLPNLINR---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFM 234
Cdd:PRK15079  195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALM 262
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 4-216 1.54e-45

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: 154.27  E-value: 1.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGeFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-IGMVFQ 82
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKemNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03264   160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 4-213 1.56e-45

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


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 154.79  E-value: 1.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT----VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ----- 74
Cdd:TIGR02982   2 ISIRNLNHYYGHGSlrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGMVFQSYALFPNMTVEGNIAFGLKM-KKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPR 153
Cdd:TIGR02982  82 RRIGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQeEAMIMSDRIFLMNKGEIV 213
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKLL 220
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
6-221 4.40e-45

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 160.57  E-value: 4.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP---QQRGIGMVFQ 82
Cdd:COG1129     7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAIIHQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFG-LKMKKLASD--EIKREVAKVIGLVDLtgkeKFYPHQ----LSGGQRQRVALARALVVKPRIL 155
Cdd:COG1129    87 ELNLVPNLSVAENIFLGrEPRRGGLIDwrAMRRRARELLARLGL----DIDPDTpvgdLSVAQQQLVEIARALSRDARVL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 156 LLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG1129   163 ILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 21-222 4.49e-45

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 154.91  E-value: 4.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQS-YALFPNMTVEGNIA 97
Cdd:PRK13648   27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklRKHIGIVFQNpDNQFVGSIVKYDVA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  98 FGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIR 177
Cdd:PRK13648  107 FGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1327293196 178 DIQKEMNLTTIFVTHDQEEAMiMSDRIFLMNKGEIVQAGTPEEIY 222
Cdd:PRK13648  187 KVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEIF 230
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 6-213 5.54e-45

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 151.04  E-value: 5.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP---QQRGIGMVfq 82
Cdd:cd03216     3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdaRRAGIAMV-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 syalfpnmtvegniafglkmkklasdeikrevakviglvdltgkekfypHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03216    81 -------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTA 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:cd03216   112 ALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 4-225 5.92e-45

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 154.85  E-value: 5.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ----VPQQRGIG 78
Cdd:PRK13639    2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkkslLEVRKTVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQSY--ALFPNmTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:PRK13639   82 IVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK13639  161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 4-216 2.93e-44

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: 150.89  E-value: 2.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQV-------PQQRG 76
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 igmvfqsyaLFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:cd03269    81 ---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDiQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03269   152 LDEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
cbiO PRK13640
energy-coupling factor transporter ATPase;
18-273 3.35e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 150.34  E-value: 3.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL---NPVDGGEIWVNGEEITHQV--PQQRGIGMVFQSY-ALFPNMT 91
Cdd:PRK13640   22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTvwDIREKVGIVFQNPdNQFVGAT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:PRK13640  102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 172 LRQQIRDIQKEMNLTTIFVTHDQEEAmIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFmghyNLVQANKAKQLFnI 251
Cdd:PRK13640  182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGL----DIPFVYKLKNKL-K 255

                         250       260
                  ....*....|....*....|..
gi 1327293196 252 ETEWKVairPESIYVKEQGRQY 273
Cdd:PRK13640  256 EKGISV---PQEINTEEKLVQY 274
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 7-220 1.95e-42

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 153.64  E-value: 1.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ---RGIGMVFQS 83
Cdd:COG3845     9 RGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMVHQH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGL---KMKKLASDEIKREVAKVI---GL-VDLTGKekfyPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:COG3845    89 FMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSeryGLdVDPDAK----VEDLSVGEQQRVEILKALYRGARILI 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEE 220
Cdd:COG3845   165 LDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 4-223 2.15e-42

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: 147.15  E-value: 2.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLN-PVDGGEIWVNGEeithqvpqQRG------ 76
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGE--------RRGgedvwe 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 ----IGMVfqSYALF----PNMTVEGNIAFGL------------KMKKLAsdeikREVAKVIGLVDLTGKeKFypHQLSG 136
Cdd:COG1119    76 lrkrIGLV--SPALQlrfpRDETVLDVVLSGFfdsiglyreptdEQRERA-----RELLELLGLAHLADR-PF--GTLSQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 137 GQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:COG1119   146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225


                  ....*..
gi 1327293196 217 TPEEIYT 223
Cdd:COG1119   226 PKEEVLT 232
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 7-226 3.75e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 147.86  E-value: 3.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFE-----DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQV------PQQR 75
Cdd:PRK13634    6 QKVEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkklkPLRK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQsyalFPNM-----TVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTgkEKFY---PHQLSGGQRQRVALARA 147
Cdd:PRK13634   86 KVGIVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLarsPFELSGGQMRRVAIAGV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:PRK13634  160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 4-216 4.64e-42

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: 145.59  E-value: 4.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT----VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEiTHQVPQQ--RGI 77
Cdd:cd03266     2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEarRRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:cd03266    81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDiQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03266   161 DEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
4-224 5.41e-42

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 147.16  E-value: 5.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN------TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG---EEITHQVPQQ 74
Cdd:PRK13633    5 IKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGMVFQSyalfPN-----MTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALV 149
Cdd:PRK13633   85 NKAGMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAmIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 5-221 6.91e-42

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 145.36  E-value: 6.91e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   5 NAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMVF 81
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVakviglVDLtgkekfYP--HQ--------LSGGQRQRVALARALVVK 151
Cdd:TIGR03410  82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEI------YEL------FPvlKEmlgrrggdLSGGQQQQLAIARALVTR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 7-213 8.17e-42

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: 144.67  E-value: 8.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYAL 86
Cdd:cd03268     4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGNIAFGLKMKKLASDEIKrEVAKVIGLVDlTGKEKFypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:cd03268    84 YPNLTARENLRLLARLLGIRKKRID-EVLDVVGLKD-SAKKKV--KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1327293196 167 KIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:cd03268   160 DGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 15-220 8.70e-42

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: 145.45  E-value: 8.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIThQVPQQ---RGIGMVFQSYALFpNMT 91
Cdd:cd03253    13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-EVTLDslrRAIGVVPQDTVLF-NDT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGlkmKKLASDEIKREVAKVIGLVDLTGKEKF-YPHQ-------LSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:cd03253    91 IGYNIRYG---RPDATDEEVIEAAKAAQIHDKIMRFPDgYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 164 LDAKIRKHLRQQIRDIQKemNLTTIFVTHDQEEAMiMSDRIFLMNKGEIVQAGTPEE 220
Cdd:cd03253   168 LDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEE 221
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 6-221 3.53e-41

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 145.64  E-value: 3.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQV-------PQQRGig 78
Cdd:COG4152     4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEERG-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 mvfqsyaLFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:COG4152    82 -------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDiQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG4152   155 EPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 6-213 3.66e-41

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 143.26  E-value: 3.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG----- 76
Cdd:TIGR02211   4 CENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnk 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 -IGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRIL 155
Cdd:TIGR02211  84 kLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 156 LLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMsDRIFLMNKGEIV 213
Cdd:TIGR02211 164 LADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 7-223 6.71e-41

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 143.30  E-value: 6.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSY 84
Cdd:COG4604     5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQEN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFG--------LkmkklaSDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:COG4604    85 HINSRLTVRELVAFGrfpyskgrL------TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 157 LDEPLSALDAkirKHLRQ---QIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:COG4604   159 LDEPLNNLDM---KHSVQmmkLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 4-235 6.92e-41

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 143.44  E-value: 6.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRS---LAGLNPVDG--GEIWVNGEEITHQ----VPQQ 74
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARveGEVRLFGRNIYSPdvdpIEVR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGMVFQSYALFPNMTVEGNIAFGLKMKKLAS-----DEIKREVAKVIGLVD-LTGKEKFYPHQLSGGQRQRVALARAL 148
Cdd:PRK14267   85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskkelDERVEWALKKAALWDeVKDRLNDYPSNLSGGQRQRLVIARAL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 149 VVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmnLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:PRK14267  165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242

                         250
                  ....*....|.
gi 1327293196 229 ----FVAGFMG 235
Cdd:PRK14267  243 ltekYVTGALG 253
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 2-214 9.82e-41

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 143.41  E-value: 9.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   2 SYVNAKNLTKRF---------GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP 72
Cdd:TIGR02769   1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 QQ-----RGIGMVFQ-SYALF-PNMTVEGNIAFGLK-MKKLASDEIKREVAKVIGLVDLTGKE-KFYPHQLSGGQRQRVA 143
Cdd:TIGR02769  81 KQrrafrRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRIN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 144 LARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQ 214
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 6-213 1.07e-40

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: 141.63  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEItHQVPQQRGIGMVFQS- 83
Cdd:cd03226     2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 -YALFPNmTVEGNIAFGLKMKKlASDEIKREVAKVIGLVDLtgKEKfYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03226    81 dYQLFTD-SVREELLLGLKELD-AGNEQAETVLKDLDLYAL--KER-HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:cd03226   156 GLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 4-225 2.90e-40

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 143.95  E-value: 2.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRF--------GDNTV--FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ 73
Cdd:PRK11308    6 LQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  74 Q-----RGIGMVFQS-YA-LFPNMTVEGNIAFGLKMK-KLASDEIKREVAKVIGLVDL-TGKEKFYPHQLSGGQRQRVAL 144
Cdd:PRK11308   86 AqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 145 ARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK11308  166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245


                  .
gi 1327293196 225 P 225
Cdd:PRK11308  246 P 246
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 1-225 3.72e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 142.25  E-value: 3.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRF-GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVpqQR 75
Cdd:PRK13652    1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeniREV--RK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQSY--ALFpNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPR 153
Cdd:PRK13652   79 FVGLVFQNPddQIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK13652  158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
4-225 3.62e-39

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 139.51  E-value: 3.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI-----THQVPQQRGIG 78
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQSYALFPNMTVEGNIAFGLK-MKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:PRK11831   88 MLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK11831  168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 7-212 6.48e-39

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: 135.81  E-value: 6.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--IGMVFQ 82
Cdd:cd03246     4 ENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNmTVEGNIafglkmkklasdeikrevakviglvdltgkekfyphqLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03246    84 DDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHdQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03246   126 HLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 7-224 7.88e-39

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: 144.17  E-value: 7.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF-----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVN-GEE---ITHQVPQQRG- 76
Cdd:TIGR03269 283 RNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPDGRGr 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 ----IGMVFQSYALFPNMTVEGNI--AFGLKMkklaSDEIKREVA----KVIGLVDLTGKEKF--YPHQLSGGQRQRVAL 144
Cdd:TIGR03269 363 akryIGILHQEYDLYPHRTVLDNLteAIGLEL----PDELARMKAvitlKMVGFDEEKAEEILdkYPDELSEGERHRVAL 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 145 ARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 15-242 9.36e-39

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 137.29  E-value: 9.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFpNMTV 92
Cdd:cd03249    15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLF-DGTI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAFGlkmKKLASDEIKREVAKVIGLVDLTGK--EKFYPH------QLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:cd03249    94 AENIRYG---KPDATDEEVEEAAKKANIHDFIMSlpDGYDTLvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMnlTTIFVTHdqEEAMIM-SDRIFLMNKGEIVQAGTPEEIYTQPanefvagfmGHY-NLVQA 242
Cdd:cd03249   171 DAESEKLVQEALDRAMKGR--TTIVIAH--RLSTIRnADLIAVLQNGQVVEQGTHDELMAQK---------GVYaKLVKA 237
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 20-224 4.13e-38

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: 143.85  E-value: 4.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQSYALFpNMTVEGNIA 97
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIA 560

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  98 FGlkmKKLASDEIKREVAKVIGLVDLTGKE-KFYPHQ-------LSGGQRQRVALARALVVKPRILLLDEPLSALDAKIR 169
Cdd:TIGR03375 561 LG---APYADDEEILRAAELAGVTEFVRRHpDGLDMQigergrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSE 637

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 170 KHLRQQIRDIQKEMnlTTIFVTHDQeeAMI-MSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:TIGR03375 638 ERFKDRLKRWLAGK--TLVLVTHRT--SLLdLVDRIIVMDNGRIVADGPKDQVLEA 689
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
8-226 1.21e-37

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 137.70  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVfeDIEFSIeKGEFIT-LLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG------EEITHQVPQQRGIGMV 80
Cdd:PRK11144    5 NFKQQLGDLCL--TVNLTL-PAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPEKRRIGYV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKKLAsdeikrEVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:PRK11144   82 FQDARLFPHYKVRGNLRYGMAKSMVA------QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:PRK11144  156 LASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 14-221 1.38e-37

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: 141.04  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--IGMVFQSYALFPNmT 91
Cdd:COG4618   343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-T 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAfglKMKKLASDEIKrEVAKVIGLVDL--------------TGkekfypHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:COG4618   422 IAENIA---RFGDADPEKVV-AAAKLAGVHEMilrlpdgydtrigeGG------ARLSGGQRQRIGLARALYGDPRLVVL 491

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQeEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG4618   492 DEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 20-216 1.83e-37

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: 133.48  E-value: 1.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQSYALFpNMTVEGNIA 97
Cdd:cd03245    21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLRDNIT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  98 FGlkmKKLASDEIKREVAKVIGLVDLTGKekfYPH-----------QLSGGQRQRVALARALVVKPRILLLDEPLSALD- 165
Cdd:cd03245   100 LG---APLADDERILRAAELAGVTDFVNK---HPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDm 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 166 ---AKIRKHLRQQIRDIqkemnlTTIFVTHDQeeAMI-MSDRIFLMNKGEIVQAG 216
Cdd:cd03245   174 nseERLKERLRQLLGDK------TLIIITHRP--SLLdLVDRIIVMDSGRIVADG 220
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-214 2.90e-37

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 134.43  E-value: 2.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRF---------GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT--- 68
Cdd:PRK10419    1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkln 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  69 --HQVPQQRGIGMVFQSY--ALFPNMTVEGNIAfgLKMKKLAS-DEIKRE--VAKVIGLVDLTGK--EKFyPHQLSGGQR 139
Cdd:PRK10419   81 raQRKAFRRDIQMVFQDSisAVNPRKTVREIIR--EPLRHLLSlDKAERLarASEMLRAVDLDDSvlDKR-PPQLSGGQL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 140 QRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQ 214
Cdd:PRK10419  158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 6-207 5.67e-37

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: 138.96  E-value: 5.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQ 82
Cdd:TIGR02857 324 FSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQ 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNmTVEGNIAFGlkmKKLASDEIKREVAKVIGLVDLT-----------GKEkfyPHQLSGGQRQRVALARALVVK 151
Cdd:TIGR02857 404 HPFLFAG-TIAENIRLA---RPDASDAEIREALERAGLDEFVaalpqgldtpiGEG---GAGLSGGQAQRLALARAFLRD 476

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTHDqEEAMIMSDRIFLM 207
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 1-229 4.54e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 130.80  E-value: 4.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL-----NPVDGGEIWVNGEEITHQ--VPQ 73
Cdd:PRK14247    1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMdvIEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  74 QRGIGMVFQSYALFPNMTVEGNIAFGLKMKKLASD--EIKREVAKVIGLVDLTGKEKFY----PHQLSGGQRQRVALARA 147
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPAN 227
Cdd:PRK14247  161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238


                  ..
gi 1327293196 228 EF 229
Cdd:PRK14247  239 EL 240
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 9-229 8.38e-36

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 135.99  E-value: 8.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   9 LTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKST----LLRSLAGlnpvdGGEIWVNGEEItHQ------VPQQRGIG 78
Cdd:PRK15134  292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL-HNlnrrqlLPVRHRIQ 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQ--SYALFPNMTVEGNIAFGLKM--KKLASDEIKREVAKVIGLVDLTGKEKF-YPHQLSGGQRQRVALARALVVKPR 153
Cdd:PRK15134  366 VVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPS 445

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEF 229
Cdd:PRK15134  446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 7-224 1.06e-35

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 129.27  E-value: 1.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGD--NTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI-THQVPQ-QRGIGMVFQ 82
Cdd:cd03251     4 KNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASlRRQIGLVSQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFpNMTVEGNIAFGlkmKKLASDEIKREVAKVIGLVDL-TGKEKFYPH-------QLSGGQRQRVALARALVVKPRI 154
Cdd:cd03251    84 DVFLF-NDTVAENIAYG---RPGATREEVEEAARAANAHEFiMELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTHdqEEAMIM-SDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:cd03251   160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAH--RLSTIEnADRIVVLEDGKIVERGTHEELLAQ 226
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 4-226 2.52e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 130.74  E-value: 2.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT-----VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-- 76
Cdd:PRK13631   22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELit 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 ----------------IGMVFQ--SYALFPNmTVEGNIAFG---LKMKKLASDEIKREVAKVIGLvdltgKEKFY---PH 132
Cdd:PRK13631  102 npyskkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLNKMGL-----DDSYLersPF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 133 QLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:PRK13631  176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254

                         250
                  ....*....|....
gi 1327293196 213 VQAGTPEEIYTQPA 226
Cdd:PRK13631  255 LKTGTPYEIFTDQH 268
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
4-234 4.12e-35

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 128.55  E-value: 4.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT--------------H 69
Cdd:PRK10619    6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  70 QVPQQRG-IGMVFQSYALFPNMTVEGNIAFG-LKMKKLASDEIKREVAKVIGLVDLTGKEKF-YPHQLSGGQRQRVALAR 146
Cdd:PRK10619   86 QLRLLRTrLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 147 ALVVKPRILLLDEPLSALDAKIrkhLRQQIRDIQK--EMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK10619  166 ALAMEPEVLLFDEPTSALDPEL---VGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242

                         250
                  ....*....|
gi 1327293196 225 PANEFVAGFM 234
Cdd:PRK10619  243 PQSPRLQQFL 252
cbiO PRK13642
energy-coupling factor transporter ATPase;
22-222 4.90e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 129.06  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  22 IEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ--VPQQRGIGMVFQSY-ALFPNMTVEGNIAF 98
Cdd:PRK13642   26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  99 GLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRD 178
Cdd:PRK13642  106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1327293196 179 IQKEMNLTTIFVTHDQEEAMiMSDRIFLMNKGEIVQAGTPEEIY 222
Cdd:PRK13642  186 IKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELF 228
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 7-228 1.38e-34

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 126.81  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSL---AGLNP--VDGGEIWVNGEEI----THQVPQQRGI 77
Cdd:PRK14239    9 SDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPevTITGSIVYNGHNIysprTDTVDLRKEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPnMTVEGNIAFGLKMKKLASDEIKRE-VAKVIGLVDLTGKEKFYPHQ----LSGGQRQRVALARALVVKP 152
Cdd:PRK14239   89 GMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 153 RILLLDEPLSALD----AKIRKHLrQQIRDiqkemNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:PRK14239  168 KIILLDEPTSALDpisaGKIEETL-LGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 7-224 1.43e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 127.66  E-value: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQ----VPQQRGIGMVF 81
Cdd:PRK13636    9 EELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkglMKLRESVGMVF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QS--YALFpNMTVEGNIAFGLKMKKLASDEIKREVAKVI---GLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILL 156
Cdd:PRK13636   89 QDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALkrtGIEHLKDKPT---HCLSFGQKKRVAIAGVLVMEPKVLV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK13636  165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 18-220 2.03e-34

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: 125.80  E-value: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEItHQVPQ---QRGIGMVFQSYALFPNmTVEG 94
Cdd:cd03254    18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRkslRSMIGVVLQDTFLFSG-TIME 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  95 NIAFGlkmKKLASDEIKREVAKVIGLVDLTGK-EKFYPHQ-------LSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:cd03254    96 NIRLG---RPNATDEEVIEAAKEAGAHDFIMKlPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 167 KIRKHLRQQIRDIQKemNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEE 220
Cdd:cd03254   173 ETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 16-211 2.60e-34

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: 124.89  E-value: 2.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  16 NTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGeEITHqVPQQrgigmvfqsyALFPNMTVEGN 95
Cdd:cd03250    18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAY-VSQE----------PWIQNGTIREN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  96 IAFGLKMkklasDEIK-REVAKVIGLV-DLtgkEKFyPHQ-----------LSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03250    86 ILFGKPF-----DEERyEKVIKACALEpDL---EIL-PDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 163 ALDAKIRKHLRQQIrdIQKEMNL--TTIFVTHdQEEAMIMSDRIFLMNKGE 211
Cdd:cd03250   157 AVDAHVGRHIFENC--ILGLLLNnkTRILVTH-QLQLLPHADQIVVLDNGR 204
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 18-212 3.28e-34

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: 123.70  E-value: 3.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMV---FQSYALFPNMT 91
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFglkmkklasdeikrevakviglvdltgkekfyPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:cd03215    95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1327293196 172 LRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03215   143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
13-213 3.99e-34

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 124.99  E-value: 3.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  13 FGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QVP-QQRGIGMVFQSYALF 87
Cdd:PRK10908   12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPfLRRQIGMIFQDHHLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:PRK10908   92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1327293196 168 irkhLRQQIRDIQKEMN---LTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:PRK10908  172 ----LSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 1-216 7.07e-34

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: 123.43  E-value: 7.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLT-----KRFGDN-TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL--NPVDGGEIWVNGEEITHQVP 72
Cdd:cd03213     1 GVTLSFRNLTvtvksSPSKSGkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 QQRgIGMVFQSYALFPNMTVEGNIAFGLKMKklasdeikrevakviglvdltgkekfyphQLSGGQRQRVALARALVVKP 152
Cdd:cd03213    81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNP 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 153 RILLLDEPLSALDA-------KIRKHLRQQIRdiqkemnlTTIFVTHD-QEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03213   131 SLLFLDEPTSGLDSssalqvmSLLRRLADTGR--------TIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 18-221 1.04e-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: 124.14  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQSYALFpNMTVEGN 95
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  96 IAF---GLKMKKLAsdeikrEVAKVIGLVDLT-----GKEKFYPHQ---LSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:cd03252    96 IALadpGMSMERVI------EAAKLAGAHDFIselpeGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSAL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 165 DAKIRKHLRQQIRDIQKemNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:cd03252   170 DYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 4-219 1.13e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 125.23  E-value: 1.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ-RG-IGMV 80
Cdd:PRK13647    5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSY--ALFpNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13647   85 FQDPddQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 159 EPLSALDAKIRKHLRqQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPE 219
Cdd:PRK13647  164 EPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 7-227 1.73e-33

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 130.63  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQ 82
Cdd:TIGR01846 459 ENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQ 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFpNMTVEGNIAFGlkmKKLASDEIKREVAKVIGLVD-LTGKEKFYPHQ-------LSGGQRQRVALARALVVKPRI 154
Cdd:TIGR01846 539 ENVLF-SRSIRDNIALC---NPGAPFEHVIHAAKLAGAHDfISELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRI 614

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPAN 227
Cdd:TIGR01846 615 LIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 20-234 1.87e-33

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 130.36  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI-----THQVPQQRGIGMVFQS-YA-LFPNMTV 92
Cdd:PRK10261  341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQDpYAsLDPRQTV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAFGLKMKKLAS-DEIKREVAKVIGLVDLTGKEKF-YPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRK 170
Cdd:PRK10261  421 GDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 171 HLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGFM 234
Cdd:PRK10261  501 QIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 24-221 1.95e-33

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


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 123.04  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  24 FSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEithQVPQQRGIGMVFQSYAL---FPnMTVEGNIAFG- 99
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 100 ------LKMKKLASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLR 173
Cdd:TIGR03771  77 tghigwLRRPCVADFAAVRDALRRVGLTELADRPV---GELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1327293196 174 QQIRDIQKEMNlTTIFVTHDQEEAMIMSDRIFLMNkGEIVQAGTPEEI 221
Cdd:TIGR03771 154 ELFIELAGAGT-AILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 6-235 2.08e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 124.44  E-value: 2.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLN-PVDG----GEIWVNGEEITHQ---VPQQRGI 77
Cdd:PRK14271   24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrdvLEFRRRV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPnMTVEGNIAFGLKMKKLASDEIKREVAKV----IGLVDLTgKEKFY--PHQLSGGQRQRVALARALVVK 151
Cdd:PRK14271  104 GMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQArlteVGLWDAV-KDRLSdsPFRLSGGQQQLLCLARTLAVN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKEmnLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPAN---- 227
Cdd:PRK14271  182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaeta 259


                  ....*...
gi 1327293196 228 EFVAGFMG 235
Cdd:PRK14271  260 RYVAGLSG 267
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 5-234 2.09e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 124.00  E-value: 2.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   5 NAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI--------THQVPQQRG 76
Cdd:PRK14246   12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqIDAIKLRKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYALFPNMTVEGNIAFGLKMKKLASdeiKREVAKV-------IGLVDLTGKEKFYP-HQLSGGQRQRVALARAL 148
Cdd:PRK14246   92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKE---KREIKKIveeclrkVGLWKEVYDRLNSPaSQLSGGQQQRLTIARAL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 149 VVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:PRK14246  169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246


                  ....*.
gi 1327293196 229 FVAGFM 234
Cdd:PRK14246  247 LTEKYV 252
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 7-225 2.20e-33

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 123.95  E-value: 2.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQrGIGMVFQ 82
Cdd:PRK11300    9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpgHQIARM-GVVRTFQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTV------------EGNIAFGLkMKKLASDEIKREVA-------KVIGLVDLTGKEKfypHQLSGGQRQRVA 143
Cdd:PRK11300   88 HVRLFREMTVienllvaqhqqlKTGLFSGL-LKTPAFRRAESEALdraatwlERVGLLEHANRQA---GNLAYGQQRRLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 144 LARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:PRK11300  164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243


                  ..
gi 1327293196 224 QP 225
Cdd:PRK11300  244 NP 245
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 21-216 3.24e-33

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: 122.76  E-value: 3.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG---GEIWVNGEEITHQVPQQRgIGMVFQSYALFPNMTVEGNIA 97
Cdd:cd03234    25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRETLT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  98 FG--LKMKKLASDEIKREVAKVIGLVDLT----GKEKFypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:cd03234   104 YTaiLRLPRKSSDAIRKKRVEDVLLRDLAltriGGNLV--KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1327293196 172 LRQQIRDIQKEmNLTTIFVTHD-QEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03234   182 LVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 4-227 3.52e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 123.61  E-value: 3.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG-----GEIWVNGEEITHQVPQ----Q 74
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlnrlR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 RGIGMVFQSYALFPnMTVEGNIAFGLKM----KKLASDEIKREVAKVIGLVDLTgKEKFYPH--QLSGGQRQRVALARAL 148
Cdd:PRK14258   88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDEI-KHKIHKSalDLSGGQQQRLCIARAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 149 VVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSD--RIFLMNK---GEIVQAGTPEEIYT 223
Cdd:PRK14258  166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDftAFFKGNEnriGQLVEFGLTKKIFN 245


                  ....
gi 1327293196 224 QPAN 227
Cdd:PRK14258  246 SPHD 249
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
7-233 4.05e-33

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 123.56  E-value: 4.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSY 84
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFG--------LKMKKLASDEIKREVaKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILL 156
Cdd:PRK10253   91 TTPGDITVQELVARGryphqplfTRWRKEDEEAVTKAM-QATGITHLADQSV---DTLSGGQRQRAWIAMVLAQETAIML 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAGF 233
Cdd:PRK10253  167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 7-229 5.83e-33

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 128.82  E-value: 5.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVF----EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVN--------------GEEIT 68
Cdd:PRK10261   16 ENLNIAFMQEQQKiaavRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrqvielSEQSA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  69 HQVPQQRG--IGMVFQS--YALFPNMTVEGNIAFGLKMKK-LASDEIKREVAKVIGLVDLTGKEKF---YPHQLSGGQRQ 140
Cdd:PRK10261   96 AQMRHVRGadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQ 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 141 RVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEE 220
Cdd:PRK10261  176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQ 255


                  ....*....
gi 1327293196 221 IYTQPANEF 229
Cdd:PRK10261  256 IFHAPQHPY 264
cbiO PRK13646
energy-coupling factor transporter ATPase;
4-224 6.65e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 123.35  E-value: 6.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFE-----DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQV------P 72
Cdd:PRK13646    3 IRFDNVSYTYQKGTPYEhqaihDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 QQRGIGMVFQ--SYALFPNmTVEGNIAFGLKMKKLASDEIKREVAKVigLVDLtGKEK----FYPHQLSGGQRQRVALAR 146
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRL--LMDL-GFSRdvmsQSPFQMSGGQMRKIAIVS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 147 ALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK13646  159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
7-221 8.09e-33

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 123.76  E-value: 8.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG-IGMVFQSYA 85
Cdd:PRK13537   11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQFDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PRK13537   91 LDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 166 AKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PRK13537  171 PQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
6-174 1.02e-32

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 120.68  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQqrgigmvFQSYA 85
Cdd:PRK13538    4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LF--------PNMTVEGNIAFGLKMKKLASDEikrEVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:PRK13538   77 LYlghqpgikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153

                         170       180
                  ....*....|....*....|....*
gi 1327293196 158 DEPLSALDAK--------IRKHLRQ 174
Cdd:PRK13538  154 DEPFTAIDKQgvarlealLAQHAEQ 178
cbiO PRK13641
energy-coupling factor transporter ATPase;
20-225 1.08e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 123.02  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ------RGIGMVFQ--SYALFPNmT 91
Cdd:PRK13641   24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQfpEAQLFEN-T 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGLKMKKLASDEIKREVAKVIGLV----DLTGKEkfyPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:PRK13641  103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVglseDLISKS---PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 168 IRKHLRQQIRDIQKEMNlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK13641  180 GRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 1-235 1.49e-32

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 123.68  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRF----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL---NPVDGGEIWVNGEEI----TH 69
Cdd:PRK09473   10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREIlnlpEK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  70 QVPQQRG--IGMVFQS--YALFPNMTVEGNIAFGLKM-KKLASDEIKREVAKVIGLVDLTGKEK---FYPHQLSGGQRQR 141
Cdd:PRK09473   90 ELNKLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKrmkMYPHEFSGGMRQR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 142 VALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PRK09473  170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249

                         250
                  ....*....|....
gi 1327293196 222 YTQPANEFVAGFMG 235
Cdd:PRK09473  250 FYQPSHPYSIGLLN 263
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 8-220 3.72e-32

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


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 126.61  E-value: 3.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQS 83
Cdd:TIGR03797 456 RVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGVVLQN 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNmTVEGNIAFG-----------LKMKKLASDeIKREVAKVIGLVDLTGKekfyphQLSGGQRQRVALARALVVKP 152
Cdd:TIGR03797 536 GRLMSG-SIFENIAGGapltldeaweaARMAGLAED-IRAMPMGMHTVISEGGG------TLSGGQRQRLLIARALVRKP 607

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIrdiqKEMNLTTIFVTHdqEEAMIM-SDRIFLMNKGEIVQAGTPEE 220
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAH--RLSTIRnADRIYVLDAGRVVQQGTYDE 670
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-221 4.25e-32

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 126.78  E-value: 4.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT-HQVPQQRGIGMVFQSY 84
Cdd:NF033858  269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMSQAF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:NF033858  349 SLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLtTIFV-THDQEEAMiMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:NF033858  429 DPVARDMFWRLLIELSREDGV-TIFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
cbiO PRK13644
energy-coupling factor transporter ATPase;
4-263 4.87e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 120.86  E-value: 4.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNT-VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT--HQVPQQRGI-GM 79
Cdd:PRK13644    2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLvGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQS-YALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13644   82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQkEMNLTTIFVTHDQEEaMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAgfMGHYN 238
Cdd:PRK13644  162 EVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG--LTPPS 237

                         250       260
                  ....*....|....*....|....*
gi 1327293196 239 LVQANKAKQLFNIETEWKVAIRPES 263
Cdd:PRK13644  238 LIELAENLKMHGVVIPWENTSSPSS 262
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 15-225 9.03e-32

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 125.60  E-value: 9.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQrgIGMVFQSYALFpNM 90
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhHYLHRQ--VALVGQEPVLF-SG 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  91 TVEGNIAFGLKMkklASDEIKREVAKVIGLVD-LTGKEKFY-----PH--QLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:TIGR00958 570 SVRENIAYGLTD---TPDEEIMAAAKAANAHDfIMEFPNGYdtevgEKgsQLSGGQKQRIAIARALVRKPRVLILDEATS 646

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 163 ALDAKIrKHLRQQIRdiqKEMNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:TIGR00958 647 ALDAEC-EQLLQESR---SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
8-221 9.28e-32

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 121.48  E-value: 9.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR-GIGMVFQSYAL 86
Cdd:PRK13536   46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQFDNL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNMTVEGN-IAFGlKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PRK13536  126 DLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 166 AKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PRK13536  205 PHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 1-221 1.34e-31

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 118.84  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQvPQQRG 76
Cdd:PRK10895    1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHA-RARRG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAK-------VIGLVDLTGKekfyphQLSGGQRQRVALARALV 149
Cdd:PRK10895   80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANelmeefhIEHLRDSMGQ------SLSGGERRRVEIARALA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 150 VKPRILLLDEPLSALD-------AKIRKHLRqqirdiqkEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PRK10895  154 ANPKFILLDEPFAGVDpisvidiKRIIEHLR--------DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 6-175 1.41e-31

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 117.46  E-value: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-QRGIGMVFQSY 84
Cdd:TIGR01189   3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFglkMKKLASDEiKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:TIGR01189  83 GLKPELSALENLHF---WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158

                         170
                  ....*....|....*....
gi 1327293196 165 DAK--------IRKHLRQQ 175
Cdd:TIGR01189 159 DKAgvallaglLRAHLARG 177
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 12-196 1.43e-31

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 118.28  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  12 RFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFPN 89
Cdd:PRK10247   16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  90 mTVEGNIAFGLKMKKLASDE--IKREVAKvIGLVDLTGKEKFypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:PRK10247   96 -TVYDNLIFPWQIRNQQPDPaiFLDDLER-FALPDTILTKNI--AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171

                         170       180
                  ....*....|....*....|....*....
gi 1327293196 168 IRKHLRQQIRDIQKEMNLTTIFVTHDQEE 196
Cdd:PRK10247  172 NKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 21-228 1.62e-31

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: 118.24  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVD----GGEIWVNGEEITHQVPQQRGIGMVFQS--YALFPNMTVEG 94
Cdd:TIGR02770   4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  95 NIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKF---YPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:TIGR02770  84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEEVlkkYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 172 LRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANE 228
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 11-216 1.75e-31

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


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 118.02  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  11 KRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGeeithQVPQQRGIGMVFQsyalfPNM 90
Cdd:cd03220    30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGLGGGFN-----PEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  91 TVEGNIAFGLKMKKLASDEIKREVAKVIglvDLTGKEKFY--P-HQLSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:cd03220   100 TGRENIYLNGRLLGLSRKEIDEKIDEII---EFSELGDFIdlPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1327293196 168 IRKHLRQQIRDiQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03220   177 FQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 14-193 3.01e-31

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: 123.24  E-value: 3.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEItHQVPQ---QRGIGMVFQSYALFpNM 90
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQdevRRRVSVCAQDAHLF-DT 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  91 TVEGNIAFGlkmKKLASDEIKREVAKVIGLVD------------LTGKEKFyphqLSGGQRQRVALARALVVKPRILLLD 158
Cdd:TIGR02868 424 TVRENLRLA---RPDATDEELWAALERVGLADwlralpdgldtvLGEGGAR----LSGGERQRLALARALLADAPILLLD 496

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEmnLTTIFVTHD 193
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-193 4.09e-31

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 122.48  E-value: 4.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNgeeithqvPQQRgIGMVFQSYA 85
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--------KGLR-IGYLPQEPP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPNMTVEGNIAFGLK-----MKKLA---------SDEIKR------------------EVAKVI---GLVDLTGKEKFy 130
Cdd:COG0488    72 LDDDLTVLDTVLDGDAelralEAELEeleaklaepDEDLERlaelqeefealggweaeaRAEEILsglGFPEEDLDRPV- 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 131 pHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKemnlTTIFVTHD 193
Cdd:COG0488   151 -SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHD 208
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 1-225 6.79e-31

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 119.08  E-value: 6.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGD-NTVF---EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL----NPVDGGEIWVNGEEITHQVP 72
Cdd:PRK11022    1 MALLNVDKLSVHFGDeSAPFravDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 QQR------GIGMVFQS--YALFPNMTVEGNIAFGLKMKKLASDEIKREVA----KVIGLVDLTGKEKFYPHQLSGGQRQ 140
Cdd:PRK11022   81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAidllNQVGIPDPASRLDVYPHQLSGGMSQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 141 RVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEE 220
Cdd:PRK11022  161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240


                  ....*
gi 1327293196 221 IYTQP 225
Cdd:PRK11022  241 IFRAP 245
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 12-220 7.86e-31

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: 122.62  E-value: 7.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  12 RFG---DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHqVPQQ---RGIGMVFQSYA 85
Cdd:COG5265   364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD-VTQAslrAAIGIVPQDTV 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFpNMTVEGNIAFGlkmKKLASDEIKREVAK-------VIGLVDltGKE--------KfyphqLSGGQRQRVALARALVV 150
Cdd:COG5265   443 LF-NDTIAYNIAYG---RPDASEEEVEAAARaaqihdfIESLPD--GYDtrvgerglK-----LSGGEKQRVAIARTLLK 511

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 151 KPRILLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTH------DqeeamimSDRIFLMNKGEIVQAGTPEE 220
Cdd:COG5265   512 NPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 6-210 1.08e-30

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: 115.99  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRF-----GDNT--VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEE----ITHQVPQQ 74
Cdd:COG4778     7 VENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPRE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  75 ------RGIGMVFQsyalF----PNMTvegniAFGLKMKKLASDEIKREVAKVIG---LVDLTGKEKF---YPHQLSGGQ 138
Cdd:COG4778    87 ilalrrRTIGYVSQ----FlrviPRVS-----ALDVVAEPLLERGVDREEARARArelLARLNLPERLwdlPPATFSGGE 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 139 RQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDqEEAM-IMSDRIFLMNKG 210
Cdd:COG4778   158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHD-EEVReAVADRVVDVTPF 228
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
8-217 1.34e-30

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 116.07  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNT----VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP------QQRGI 77
Cdd:PRK11629   10 NLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 GMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:PRK11629   90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSdRIFLMNKGEIVQAGT 217
Cdd:PRK11629  170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
cbiO PRK13643
energy-coupling factor transporter ATPase;
13-224 1.74e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 117.14  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  13 FGDNTVFeDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL-NPVDG----GEIWVNGEEITHQV-PQQRGIGMVFQsyal 86
Cdd:PRK13643   17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVSSTSKQKEIkPVRKKVGVVFQ---- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 FPNM-----TVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTgkEKFY---PHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13643   92 FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA--DEFWeksPFELSGGQMRRVAIAGILAMEPEVLVLD 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQkEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK13643  170 EPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 14-224 2.21e-30

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: 120.92  E-value: 2.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG--IGMVFQSYALFPNmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-T 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAfglKMKKLASDEIKREVAKVIGLVDLTGK-EKFYPHQ-------LSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:TIGR01842 408 VAENIA---RFGENADPEKIIEAAKLAGVHELILRlPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSN 484

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEmNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:TIGR01842 485 LDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 6-221 3.38e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 116.72  E-value: 3.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNT-----VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEI-WV---------------NG 64
Cdd:PRK13651    5 VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkdeknkkktkekekVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  65 EEITHQVPQ----------QRGIGMVFQ--SYALFPNmTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLtgKEKFY-- 130
Cdd:PRK13651   85 EKLVIQKTRfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL--DESYLqr 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 131 -PHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAkirkHLRQQIRDIQKEMNL---TTIFVTHDQEEAMIMSDRIFL 206
Cdd:PRK13651  162 sPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNKqgkTIILVTHDLDNVLEWTKRTIF 237

                         250
                  ....*....|....*
gi 1327293196 207 MNKGEIVQAGTPEEI 221
Cdd:PRK13651  238 FKDGKIIKDGDTYDI 252
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 6-235 3.75e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 115.65  E-value: 3.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP-VDG----GEIWVNGEEITHQ----VPQQRG 76
Cdd:PRK14243   13 TENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLYAPdvdpVEVRRR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYALFPNmTVEGNIAFGLKMK--KLASDEIKREVAKVIGLVD-LTGKEKFYPHQLSGGQRQRVALARALVVKPR 153
Cdd:PRK14243   93 IGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERSLRQAALWDeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHDQEEAMIMSDRIFLMN---------KGEIVQAGTPEEIYTQ 224
Cdd:PRK14243  172 VILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNS 249

                         250
                  ....*....|....*
gi 1327293196 225 PAN----EFVAGFMG 235
Cdd:PRK14243  250 PQQqatrDYVSGRFG 264
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 15-229 3.96e-30

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 120.20  E-value: 3.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVD-----GGEIWVNGEEITHQVPQQ----RG--IGMVFQS 83
Cdd:PRK15134   21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTlrgvRGnkIAMIFQE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 --YALFPNMTVEGNIAFGLKM-----KKLASDEIKREVAKViGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILL 156
Cdd:PRK15134  101 pmVSLNPLHTLEKQLYEVLSLhrgmrREAARGEILNCLDRV-GIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEF 229
Cdd:PRK15134  180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 11-221 5.96e-30

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 114.41  E-value: 5.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  11 KRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEeithqVPQQRGIGMVFQsyalfPNM 90
Cdd:COG1134    34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----VSALLELGAGFH-----PEL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  91 TVEGNIAFGLKMKKLASDEIKREVAKVIglvDLTGKEKF-------YphqlSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:COG1134   104 TGRENIYLNGRLLGLSRKEIDEKFDEIV---EFAELGDFidqpvktY----SSGMRARLAFAVATAVDPDILLVDEVLAV 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:COG1134   177 GDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
6-213 6.18e-30

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 118.97  E-value: 6.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRfgdnTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ---RGIGMV-- 80
Cdd:COG1129   259 VEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpe 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 -FQSYALFPNMTVEGNIA---------FGL----KMKKLASDEIKR-EVaKVIGLVDLTGkekfyphQLSGGQRQRVALA 145
Cdd:COG1129   335 dRKGEGLVLDLSIRENITlasldrlsrGGLldrrRERALAEEYIKRlRI-KTPSPEQPVG-------NLSGGNQQKVVLA 406

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 146 RALVVKPRILLLDEPLSALD--AKirkhlrqqiRDIQKEMN------LTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:COG1129   407 KWLATDPKVLILDEPTRGIDvgAK---------AEIYRLIRelaaegKAVIVISSELPELLGLSDRILVMREGRIV 473
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 6-224 7.00e-30

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 114.64  E-value: 7.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEI-WVNGEEITHQV-----PQQRGI-- 77
Cdd:PRK11701    9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLyalseAERRRLlr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 ---GMVFQSYA--LFPNMTVEGNI-----AFGLK----MKKLASDEIKR-EVAkVIGLVDLtgkekfyPHQLSGGQRQRV 142
Cdd:PRK11701   89 tewGFVHQHPRdgLRMQVSAGGNIgerlmAVGARhygdIRATAGDWLERvEID-AARIDDL-------PTTFSGGMQQRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 143 ALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAG------ 216
Cdd:PRK11701  161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGltdqvl 240


                  ....*....
gi 1327293196 217 -TPEEIYTQ 224
Cdd:PRK11701  241 dDPQHPYTQ 249
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
6-224 7.73e-30

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 114.34  E-value: 7.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGigmvfQSYA 85
Cdd:PRK11231    5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----RRLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPN-------MTVEGNIAFG----LKMKKLASDEIKREVAKVI---GLVDLTGKEKfypHQLSGGQRQRVALARALVVK 151
Cdd:PRK11231   80 LLPQhhltpegITVRELVAYGrspwLSLWGRLSAEDNARVNQAMeqtRINHLADRRL---TDLSGGQRQRAFLAMVLAQD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK11231  157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 7-234 8.22e-30

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 119.14  E-value: 8.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLN--PVDGGEI-----------WVN---------- 63
Cdd:TIGR03269   4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvgepcp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  64 --GEEITHQVPQ------------QRGIGMVFQ-SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEK 128
Cdd:TIGR03269  84 vcGGTLEPEEVDfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRIT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 129 FYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMN 208
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243

                         250       260
                  ....*....|....*....|....*.
gi 1327293196 209 KGEIVQAGTPEEIytqpanefVAGFM 234
Cdd:TIGR03269 244 NGEIKEEGTPDEV--------VAVFM 261
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-198 9.12e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 112.33  E-value: 9.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  12 RFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGmvfqsyALFPnMT 91
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGL-----KMKKLASDEiKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:NF040873   74 VRDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327293196 167 KIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAM 198
Cdd:NF040873  153 ESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
6-228 1.11e-29

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 114.50  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNT---------VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT---HQVPQ 73
Cdd:PRK15112    7 VRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdYSYRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  74 QRgIGMVFQ--SYALFPNMTVEGNIAFGLKMK-KLASDEIKREVAKVIGLVDL-TGKEKFYPHQLSGGQRQRVALARALV 149
Cdd:PRK15112   87 QR-IRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVThdQEEAMI--MSDRIFLMNKGEIVQAGTPEEIYTQPAN 227
Cdd:PRK15112  166 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLASPLH 243


                  .
gi 1327293196 228 E 228
Cdd:PRK15112  244 E 244
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 7-218 2.37e-29

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: 112.20  E-value: 2.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDN--TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQrgIGMV 80
Cdd:cd03244     6 KNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiglHDLRSR--ISII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFpnmtvEGNIAFGLKMKKLASDE----------IKREVAKVIGLVDLTGKEKfyPHQLSGGQRQRVALARALVV 150
Cdd:cd03244    84 PQDPVLF-----SGTIRSNLDPFGEYSDEelwqalervgLKEFVESLPGGLDTVVEEG--GENLSVGQRQLLCLARALLR 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 151 KPRILLLDEPLSALD----AKIRKHLRQQIRDIqkemnlTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTP 218
Cdd:cd03244   157 KSKILVLDEATASVDpetdALIQKTIREAFKDC------TVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 6-223 2.44e-29

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 117.46  E-value: 2.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP---QQRGIGMVFQ 82
Cdd:PRK15439   14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKfyphQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:PRK15439   94 EPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTA 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:PRK15439  170 SLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 9-197 5.13e-29

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 111.41  E-value: 5.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   9 LTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRG------IG 78
Cdd:PRK10584   12 LKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK10584   92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEA 197
Cdd:PRK10584  172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
12-222 5.39e-29

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 112.79  E-value: 5.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  12 RFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL-NPVDGGEIWvNGEEITHQvpqQRG-------IGMVFQS 83
Cdd:PRK13638   10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlRPQKGAVLW-QGKPLDYS---KRGllalrqqVATVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 yalfPNMTV-----EGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGkekfYPHQ----LSGGQRQRVALARALVVKPRI 154
Cdd:PRK13638   86 ----PEQQIfytdiDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH----FRHQpiqcLSHGQKKRVAIAGALVLQARY 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIfVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIY 222
Cdd:PRK13638  158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 7-221 5.64e-29

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: 117.12  E-value: 5.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFG--DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQ 82
Cdd:TIGR02203 334 RNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQ 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFpNMTVEGNIAFGlKMKKLASDEIkREVAKVIGLVDLTGKEKFYPHQ--------LSGGQRQRVALARALVVKPRI 154
Cdd:TIGR02203 414 DVVLF-NDTIANNIAYG-RTEQADRAEI-ERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALLKDAPI 490

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTH---DQEEAmimsDRIFLMNKGEIVQAGTPEEI 221
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHrlsTIEKA----DRIVVMDDGRIVERGTHNEL 554
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 6-174 7.13e-29

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 110.35  E-value: 7.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIThqvpqqrgIGMVFQS-- 83
Cdd:PRK13539    5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--------DPDVAEAch 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 Y-----ALFPNMTVEGNIAFGLKMKKlASDEIKREVAKVIGLVDLTGKeKFypHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13539   77 YlghrnAMKPALTVAENLEFWAAFLG-GEELDIAAALEAVGLAPLAHL-PF--GYLSAGQKRRVALARLLVSNRPIWILD 152

                         170       180
                  ....*....|....*....|....
gi 1327293196 159 EPLSALDAK--------IRKHLRQ 174
Cdd:PRK13539  153 EPTAALDAAavalfaelIRAHLAQ 176
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 22-225 1.60e-28

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 115.71  E-value: 1.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  22 IEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGgEIWVNGEEITHQVPQQ--RGIGMVFQSYALFPNmTVEGNIAFG 99
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPESwrKHLSWVGQNPQLPHG-TLRDNVLLG 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 100 lkmKKLASDEikrevaKVIGLVDLTGKEKFYPHQ--------------LSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PRK11174  447 ---NPDASDE------QLQQALENAWVSEFLPLLpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 166 AkirkHLRQQI-RDIQKEMN-LTTIFVTH--DQEEAMimsDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK11174  518 A----HSEQLVmQALNAASRrQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGDYAELSQAG 574
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 8-225 1.79e-28

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: 110.69  E-value: 1.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEI-WVNGEEITHQV-----PQQRGI---- 77
Cdd:TIGR02323   8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELyqlseAERRRLmrte 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 -GMVFQSYALFPNMTVE--GNI-----AFGL----KMKKLASDEIKREVAKVIGLVDLtgkekfyPHQLSGGQRQRVALA 145
Cdd:TIGR02323  88 wGFVHQNPRDGLRMRVSagANIgerlmAIGArhygNIRATAQDWLEEVEIDPTRIDDL-------PRAFSGGMQQRLQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 146 RALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 6-213 2.01e-28

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 110.11  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKR-FGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEeithqVPQQRG------IG 78
Cdd:cd03267    23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-----VPWKRRkkflrrIG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVF-QSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLL 157
Cdd:cd03267    98 VVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:cd03267   178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
cbiO PRK13649
energy-coupling factor transporter ATPase;
4-224 2.04e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 111.37  E-value: 2.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFE-----DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQV------P 72
Cdd:PRK13649    3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 QQRGIGMVFQsyalFPNM-----TVEGNIAFG---LKMKKLASDEIKREVAKVIGLV-DLTGKEkfyPHQLSGGQRQRVA 143
Cdd:PRK13649   83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGpqnFGVSQEEAEALAREKLALVGISeSLFEKN---PFELSGGQMRRVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 144 LARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:PRK13649  156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234


                  .
gi 1327293196 224 Q 224
Cdd:PRK13649  235 D 235
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-225 2.73e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 113.40  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI--THQVPQQRGIG 78
Cdd:PRK09536    1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeaLSARAASRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQSYALFPNMTVEGNIAFG----LKMKKLASDEIKREVAKVIglvDLTGKEKFYPH---QLSGGQRQRVALARALVVK 151
Cdd:PRK09536   81 SVPQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAM---ERTGVAQFADRpvtSLSGGERQRVLLARALAQA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 152 PRILLLDEPLSALDakirkhLRQQIRDIQKEMNL-----TTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK09536  158 TPVLLLDEPTASLD------INHQVRTLELVRRLvddgkTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 6-174 3.77e-28

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: 108.35  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-QRGIGMVFQSY 84
Cdd:cd03231     3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 ALFPNMTVEGNIAFglkmkkLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:cd03231    83 GIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156

                         170
                  ....*....|....
gi 1327293196 165 D----AKIRKHLRQ 174
Cdd:cd03231   157 DkagvARFAEAMAG 170
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
4-220 9.48e-28

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 108.95  E-value: 9.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL---NPVDGGEIWVNGEEITHQVPQQRGI--- 77
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrks 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  78 ----GMVFQSYALFPNMTVEGNIAFGlkmkKLASDEIKR-------EVAKVIGLVDLT--GKEKFyPHQ----LSGGQRQ 140
Cdd:PRK09984   85 rantGYIFQQFNLVNRLSVLENVLIG----ALGSTPFWRtcfswftREQKQRALQALTrvGMVHF-AHQrvstLSGGQQQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 141 RVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEE 220
Cdd:PRK09984  160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 18-224 9.78e-28

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 113.38  E-value: 9.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFpNMTVEGN 95
Cdd:PRK11160  355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRVHLF-SATLRDN 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  96 IAFGlkmKKLASDEIKREVAKVIGLVDLTGKEKfyP---------HQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:PRK11160  434 LLLA---APNASDEALIEVLQQVGLEKLLEDDK--GlnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 167 KIRKHLRQQIRDIQKemNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK11160  509 ETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 7-219 1.15e-27

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: 107.23  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGlNP---VDGGEIWVNGEEITHQVPQQR---GIGMV 80
Cdd:cd03217     4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDLPPEERarlGIFLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPnmtvegniafGLKMKKLAsdeikREVakviglvdltgKEKFyphqlSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:cd03217    83 FQYPPEIP----------GVKNADFL-----RYV-----------NEGF-----SGGEKKRNEILQLLLLEPDLAILDEP 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEA-MIMSDRIFLMNKGEIVQAGTPE 219
Cdd:cd03217   132 DSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSGDKE 190
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 3-225 2.63e-27

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 112.73  E-value: 2.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   3 YVNAKNLTkrFG----DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG---EEITHQVPQQr 75
Cdd:TIGR03796 477 YVELRNIT--FGysplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGiprEEIPREVLAN- 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQSYALFpnmtvEGNIAFGLKM--KKLASDEIKREVAKVIGLVDLTGKEKFYPHQL-------SGGQRQRVALAR 146
Cdd:TIGR03796 554 SVAMVDQDIFLF-----EGTVRDNLTLwdPTIPDADLVRACKDAAIHDVITSRPGGYDAELaegganlSGGQRQRLEIAR 628

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 147 ALVVKPRILLLDEPLSALDAKIRKHLRQQIRdiqkEMNLTTIFVTH------DqeeamimSDRIFLMNKGEIVQAGTPEE 220
Cdd:TIGR03796 629 ALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHrlstirD-------CDEIIVLERGKVVQRGTHEE 697


                  ....*
gi 1327293196 221 IYTQP 225
Cdd:TIGR03796 698 LWAVG 702
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 7-192 9.12e-27

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 110.67  E-value: 9.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTV-FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIwvngeeithQVPQqrGIGMVF---Q 82
Cdd:COG4178   366 EDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI---------ARPA--GARVLFlpqR 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYalFPNMTVEGNIAFGLKMKKLASDEIKREVAKViGLVDLTGK---EKFYPHQLSGGQRQRVALARALVVKPRILLLDE 159
Cdd:COG4178   435 PY--LPLGTLREALLYPATAEAFSDAELREALEAV-GLGHLAERldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1327293196 160 PLSALDAKIRKHLRQQIRDIQKEMnlTTIFVTH 192
Cdd:COG4178   512 ATSALDEENEAALYQLLREELPGT--TVISVGH 542
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 4-195 1.19e-26

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: 102.53  E-value: 1.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIwvngeeithQVPQQRGIGmvfqs 83
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------TWGSTVKIG----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 yalfpnmtvegniafglkmkklasdeikrevakviglvdltgkekfYPHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:cd03221    67 ----------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327293196 164 LDAKIRKHLRQQIRDIQKemnlTTIFVTHDQE 195
Cdd:cd03221   101 LDLESIEALEEALKEYPG----TVILVSHDRY 128
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 15-212 1.23e-26

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: 105.25  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT---HQVpQQRGIGMVFQSYALFPNmT 91
Cdd:cd03248    26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyeHKY-LHSKVSLVGQEPVLFAR-S 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNIAFGLKMKklaSDEIKREVAKVIGLVD-LTGKEKFYP-------HQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:cd03248   104 LQDNIAYGLQSC---SFECVKEAAQKAHAHSfISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1327293196 164 LDAKIRKHLRQQIRDIQKEmnlTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:cd03248   181 LDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 4-233 1.88e-26

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 105.20  E-value: 1.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIwvngeeithQVPQQRGIGMVFQS 83
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNM--TVEGNIAFGLKMKKlasDEIKREVAKVIG--LVDltgkekfYPHQ-LSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK09544   76 LYLDTTLplTVNRFLRLRPGTKK---EDILPALKRVQAghLID-------APMQkLSGGETQRVLLARALLNRPQLLVLD 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNkGEIVQAGTPEEIYTQPanEFVAGF 233
Cdd:PRK09544  146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217
cbiO PRK13645
energy-coupling factor transporter ATPase;
8-223 2.60e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 105.86  E-value: 2.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVFE-----DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-------QR 75
Cdd:PRK13645   11 NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkrlRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQ--SYALFPNmTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGK-EKFYPHQLSGGQRQRVALARALVVKP 152
Cdd:PRK13645   91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDG 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:PRK13645  170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
20-221 9.30e-26

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 107.74  E-value: 9.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQSYALFpNMTVEGNIA 97
Cdd:PRK13657  352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLF-NRSIEDNIR 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  98 FGlkmKKLASDEIKREVAKVIGLVD-LTGKEKFYP-------HQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIR 169
Cdd:PRK13657  431 VG---RPDATDEEMRAAAERAQAHDfIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 170 KHLRQQIRDIQKemNLTTIFVTHdqEEAMIMS-DRIFLMNKGEIVQAGTPEEI 221
Cdd:PRK13657  508 AKVKAALDELMK--GRTTFIIAH--RLSTVRNaDRILVFDNGRVVESGSFDEL 556
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-213 1.49e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 106.69  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIwvngeEITHQV-----PQQRGig 78
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGETVkigyfDQHQE-- 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 mvfqsyALFPNMTVEGNIAfglkmkKLASDEIKREVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARALVVKPRILLL 157
Cdd:COG0488   389 ------ELDPDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLL 456

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 158 DEP--------LSALdakirkhlrqqirdiqkEMNL-----TTIFVTHDQE--EAmiMSDRIFLMNKGEIV 213
Cdd:COG0488   457 DEPtnhldietLEAL-----------------EEALddfpgTVLLVSHDRYflDR--VATRILEFEDGGVR 508
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 22-227 1.86e-25

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 102.61  E-value: 1.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  22 IEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPvDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFPNMTVEGNIAFG 99
Cdd:COG4138    15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 100 LKmKKLASDEIKREVAKVIGLVDLTGKekfYP---HQLSGGQRQRVALARALV-VKPRI------LLLDEPLSALDakir 169
Cdd:COG4138    94 QP-AGASSEAVEQLLAQLAEALGLEDK---LSrplTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLD---- 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 170 khLRQQI---RDIQK--EMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTqPAN 227
Cdd:COG4138   166 --VAQQAaldRLLRElcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN 225
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 7-213 2.83e-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: 106.06  E-value: 2.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG--GEIWVNGEEITHQV---PQQRGIGMVF 81
Cdd:TIGR02633   5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirdTERAGIVIIH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFG----LKMKKLASDEIKREVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARALVVKPRILL 156
Cdd:TIGR02633  85 QELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLI 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 20-221 3.00e-25

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 103.63  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPvDGGEIWVNGEeithqVPQQ------RGIGMVF-QSYALFPNMT 91
Cdd:COG4586    39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGY-----VPFKrrkefaRRIGVVFgQRSQLWWDLP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 V-EgniAFGL--KMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKI 168
Cdd:COG4586   113 AiD---SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 169 RKHLRQQIRDIQKEMNlTTIFVT-HDqeeamiMSD------RIFLMNKGEIVQAGTPEEI 221
Cdd:COG4586   190 KEAIREFLKEYNRERG-TTILLTsHD------MDDiealcdRVIVIDHGRIIYDGSLEEL 242
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 26-233 6.65e-25

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 105.51  E-value: 6.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  26 IEKGEFITLLGPSGCGKSTLLRSLAGLNPVD---GGEIWVNGEEIThqVPQQRGI-GMVFQSYALFPNMTVEGNIAFG-- 99
Cdd:TIGR00955  48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID--AKEMRAIsAYVQQDDLFIPTLTVREHLMFQah 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 100 LKMKKLASDEIKRE-VAKVI---GLVD----LTGKEKFYpHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:TIGR00955 126 LRMPRRVTKKEKRErVDEVLqalGLRKcantRIGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 172 LRQQIRDIQkeMNLTTIFVTHDQEEAMIMS--DRIFLMNKGEIVQAGTPEEI--------YTQPANEFVAGF 233
Cdd:TIGR00955 205 VVQVLKGLA--QKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENYNPADF 274
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 7-229 9.40e-25

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 104.63  E-value: 9.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVD--GGEIWVNGEEITHQV---PQQRGIGMVF 81
Cdd:PRK13549    9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNirdTERAGIAIIH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 QSYALFPNMTVEGNIAFG---LKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:PRK13549   89 QELALVKELSVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 159 EPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGeivqagtpEEIYTQPANEF 229
Cdd:PRK13549  169 EPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG--------RHIGTRPAAGM 230
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 7-219 1.02e-24

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 100.53  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGlNP---VDGGEIWVNGEEITHQVPQQR---GIGMV 80
Cdd:COG0396     4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyeVTSGSILLDGEDILELSPDERaraGIFLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVE------GNIAFGLKMKKLASDEIKREVAKVIGL--------VDltgkEKFyphqlSGGQRQRVALAR 146
Cdd:COG0396    83 FQYPVEIPGVSVSnflrtaLNARRGEELSAREFLKLLKEKMKELGLdedfldryVN----EGF-----SGGEKKRNEILQ 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 147 ALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQE-EAMIMSDRIFLMNKGEIVQAGTPE 219
Cdd:COG0396   154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRiLDYIKPDFVHVLVDGRIVKSGGKE 226
hmuV PRK13547
heme ABC transporter ATP-binding protein;
4-226 1.31e-24

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 100.67  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG--------GEIWVNGEEITH------ 69
Cdd:PRK13547    2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAidaprl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  70 -----QVPQQRGIGMVFQSYAL-----FPNMTVEGniAFGLKMKKLASDEIKREVAKVIGLVDLTgkekfyphQLSGGQR 139
Cdd:PRK13547   82 arlraVLPQAAQPAFAFSAREIvllgrYPHARRAG--ALTHRDGEIAWQALALAGATALVGRDVT--------TLSGGEL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 140 QRVALARAL---------VVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKG 210
Cdd:PRK13547  152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADG 231

                         250
                  ....*....|....*.
gi 1327293196 211 EIVQAGTPEEIYTqPA 226
Cdd:PRK13547  232 AIVAHGAPADVLT-PA 246
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 4-218 2.63e-24

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: 98.25  E-value: 2.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN--TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHqVPQQ---RGIG 78
Cdd:cd03369     7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-IPLEdlrSSLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQSYALFpnmtvEGNIAFGLKMKKLASDEIKREVAKVIGlvdltGKEkfyphQLSGGQRQRVALARALVVKPRILLLD 158
Cdd:cd03369    86 IIPQDPTLF-----SGTIRSNLDPFDEYSDEEIYGALRVSE-----GGL-----NLSQGQRQLLCLARALLKRPRVLVLD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 159 EPLSAL----DAKIRKHLRqqirdiqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTP 218
Cdd:cd03369   151 EATASIdyatDALIQKTIR-------EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-204 2.79e-24

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 103.07  E-value: 2.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEitHQVPQQR----- 75
Cdd:PRK11288    2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTaalaa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQSYALFPNMTVEGNI-------AFGLKMKKLASDEIKREVAKvIGL-VDLTGKEKFyphqLSGGQRQRVALARA 147
Cdd:PRK11288   80 GVAIIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLEH-LGVdIDPDTPLKY----LSIGQRQMVEIAKA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRI 204
Cdd:PRK11288  155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAI 210
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 19-223 3.89e-24

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 102.82  E-value: 3.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  19 FEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR-GIGMVF-----QSYALFPNMTV 92
Cdd:PRK15439  279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPL 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAfglkmkKLASDEI------KREVAKVIGLVDLTGKEKFYPHQ----LSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:PRK15439  359 AWNVC------ALTHNRRgfwikpARENAVLERYRRALNIKFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:PRK15439  433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINV 492
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
18-213 4.22e-24

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 103.27  E-value: 4.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QVPQQR--GIGMVFQSYALFPNMT 91
Cdd:PRK10535   23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLRreHFGFIFQRYHLLSHLT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGNI---AFGLKMKKLASDEIKREVAKVIGLVDLTGkekFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAK- 167
Cdd:PRK10535  103 AAQNVevpAVYAGLERKQRLLRAQELLQRLGLEDRVE---YQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHs 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 168 ------IRKHLRQQirdiqkemNLTTIFVTHDQEEAMiMSDRIFLMNKGEIV 213
Cdd:PRK10535  180 geevmaILHQLRDR--------GHTVIIVTHDPQVAA-QAERVIEIRDGEIV 222
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 4-216 1.37e-23

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 95.46  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN--TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEI-THQVPQQRGIGMV 80
Cdd:cd03247     1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsDLEKALSSLISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFpNMTVEGNIafglkmkklasdeikrevakviglvdltGKekfyphQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:cd03247    81 NQRPYLF-DTTLRNNL----------------------------GR------RFSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEMnlTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAG 216
Cdd:cd03247   126 TVGLDPITERQLLSLIFEVLKDK--TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 15-192 3.24e-23

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: 94.14  E-value: 3.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIwvngeeithQVPQQRGIGMVFQ-SYalFPNMTVe 93
Cdd:cd03223    13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFLPQrPY--LPLGTL- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  94 gniafglkmkklasdeikREVakVIglvdltgkekfYP--HQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:cd03223    81 ------------------REQ--LI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129

                         170       180
                  ....*....|....*....|.
gi 1327293196 172 LRQQIrdiqKEMNLTTIFVTH 192
Cdd:cd03223   130 LYQLL----KELGITVISVGH 146
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
3-221 5.17e-23

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 99.47  E-value: 5.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   3 YVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEE---ITHQVPQQRGIGM 79
Cdd:PRK09700    5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIAFG-LKMKKLASDEI-----KREVAKVIGL-VDLTGKEKFYPHQLSGGQRQRVALARALVVKP 152
Cdd:PRK09700   85 IYQELSVIDELTVLENLYIGrHLTKKVCGVNIidwreMRVRAAMMLLrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 153 RILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PRK09700  165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
15-225 1.17e-22

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 98.63  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH-QVPQQRG-IGMVFQSYALFPNmTV 92
Cdd:PRK10789  327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSrLAVVSQTPFLFSD-TV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAFGlkmKKLASDEIKREVAKVIGL-VDLTGKEKFYPHQ-------LSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:PRK10789  406 ANNIALG---RPDATQQEIEHVARLASVhDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAV 482

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 165 DAKIRKHLRQQIRDIQKEmnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK10789  483 DGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 20-212 6.41e-22

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 96.23  E-value: 6.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQrGI--GMVFQSY-----ALFPNMTV 92
Cdd:PRK10762  269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLanGIVYISEdrkrdGLVLGMSV 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIA------FGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PRK10762  348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1327293196 166 AKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:PRK10762  428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
14-224 7.19e-22

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 96.33  E-value: 7.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG---EEITHQVPQQrGIGMVFQ-----SYA 85
Cdd:PRK10790  352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRQ-GVAMVQQdpvvlADT 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPNMTV-----EGNIAFGLKMKKLAsdEIKREVAKviGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:PRK10790  431 FLANVTLgrdisEEQVWQALETVQLA--ELARSLPD--GLYTPLGEQG---NNLSVGQKQLLALARVLVQTPQILILDEA 503

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 161 LSALDAKIRKHLRQQIRDIQKEmnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK10790  504 TANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 13-221 1.03e-21

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: 95.96  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  13 FGDNtVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQrgIGMVFQSYALFP 88
Cdd:TIGR01193 485 YGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrHTLRQF--INYLPQEPYIFS 561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  89 NMTVEgNIAFGLKmKKLASDEIKR-----EVAKVIGLVDLTGKEKFYPH--QLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:TIGR01193 562 GSILE-NLLLGAK-ENVSQDEIWAaceiaEIKDDIENMPLGYQTELSEEgsSISGGQKQRIALARALLTDSKVLILDEST 639

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 162 SALDAKIRKhlrqqiRDIQKEMNL---TTIFVTHDQEEAMiMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:TIGR01193 640 SNLDTITEK------KIVNNLLNLqdkTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDEL 695
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
15-224 1.15e-21

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 95.86  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT-HQVPQQRG-IGMVFQSYALFpNMTV 92
Cdd:PRK11176  355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdYTLASLRNqVALVSQNVHLF-NDTI 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAFGLKmKKLASDEIKReVAKVIGLVDLTGKekfYPH-----------QLSGGQRQRVALARALVVKPRILLLDEPL 161
Cdd:PRK11176  434 ANNIAYART-EQYSREQIEE-AARMAYAMDFINK---MDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEAT 508

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 162 SALDAKIRKHLRQQIRDIQKemNLTTIFVTHDQ---EEAmimsDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK11176  509 SALDTESERAIQAALDELQK--NRTSLVIAHRLstiEKA----DEILVVEDGEIVERGTHAELLAQ 568
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
7-213 2.15e-21

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 91.09  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH-QVPQ--QRGIGMVFQS 83
Cdd:PRK11614    9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKimREAVAIVPEG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFGLKMKKlaSDEIKREVAKVIGLVD-LTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:PRK11614   89 RRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 163 ALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:PRK11614  167 GLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 1-213 4.67e-21

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: 89.24  E-value: 4.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDN----TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG---GEIWVNGEE--ITHQV 71
Cdd:cd03233     1 ASTLSWRNISFTTGKGrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPykEFAEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  72 PQqRGIGMVFQSYALFPNMTVEGNIAFGLKMKklaSDEIKREVakviglvdltgkekfyphqlSGGQRQRVALARALVVK 151
Cdd:cd03233    81 YP-GEIIYVSEEDVHFPTLTVRETLDFALRCK---GNEFVRGI--------------------SGGERKRVSIAEALVSR 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIF-VTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:cd03233   137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
PLN03211 PLN03211
ABC transporter G-25; Provisional
 10-166 4.99e-21

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 94.18  E-value: 4.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  10 TKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDG--GEIWVNGEEITHQVpqQRGIGMVFQSYALF 87
Cdd:PLN03211   75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQI--LKRTGFVTQDDILY 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFG--LKMKKLASDEIKREVAK-VIGLVDLTGKEKF-----YPHQLSGGQRQRVALARALVVKPRILLLDE 159
Cdd:PLN03211  153 PHLTVRETLVFCslLRLPKSLTKQEKILVAEsVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILDE 232


                  ....*..
gi 1327293196 160 PLSALDA 166
Cdd:PLN03211  233 PTSGLDA 239
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 4-218 9.10e-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: 93.54  E-value: 9.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196    4 VNAKNLTKRF---GDNTVfEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR-GIGM 79
Cdd:TIGR01257  929 VCVKNLVKIFepsGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqSLGM 1007

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   80 VFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDE 159
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196  160 PLSALDAKIRKHLRQQIrdIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTP 218
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 17-221 1.06e-20

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 92.78  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  17 TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQR---GIGMV---FQSYALFPNM 90
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLVPDM 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  91 TVEGNIAFGLKMKK-------LASDEIKREVAKVIglvdltgkEKF---YPH------QLSGGQRQRVALARALVVKPRI 154
Cdd:COG3845   352 SVAENLILGRYRRPpfsrggfLDRKAIRAFAEELI--------EEFdvrTPGpdtparSLSGGNQQKVILARELSRDPKL 423

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDiQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV-----QAGTPEEI 221
Cdd:COG3845   424 LIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVgevpaAEATREEI 494
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 21-210 2.04e-20

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: 88.16  E-value: 2.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYA----LFPNMTVEGN 95
Cdd:cd03290    19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAaqkpWLLNATVEEN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  96 IAFGlkmkklaSDEIKREVAKVIGLVDLTGKEKFYPH-----------QLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:cd03290    99 ITFG-------SPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1327293196 165 DAKIRKHLRQQ-IRDIQKEMNLTTIFVTHdQEEAMIMSDRIFLMNKG 210
Cdd:cd03290   172 DIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 14-221 2.44e-20

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: 92.32  E-value: 2.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEeiTHQVPQQrgigmvfqsyALFPNMTVE 93
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ----------AWIQNDSLR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   94 GNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQ----LSGGQRQRVALARALVVKPRILLLDEPLSALDAKIR 169
Cdd:TIGR00957  717 ENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1327293196  170 KHLRQQIRDIQKEM-NLTTIFVTHDQeEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:TIGR00957  797 KHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 4-165 2.63e-20

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: 91.54  E-value: 2.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVnGEEIThqvpqqrgIGMVFQS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQS 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 Y-ALFPNMTVEGNIAFGLKMKKLASDEIKREVakVIGLVDLTG--KEKFYpHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGsdQQKKV-GQLSGGERNRVHLAKTLKSGGNVLLLDEP 470


                  ....*
gi 1327293196 161 LSALD 165
Cdd:TIGR03719 471 TNDLD 475
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
7-235 3.18e-20

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 88.69  E-value: 3.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT---------------HQV 71
Cdd:PRK10575   15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswsskafarkvaylpQQL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  72 PQQRGigmvfqsyalfpnMTVEGNIAFGL-----KMKKLASDEiKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALAR 146
Cdd:PRK10575   95 PAAEG-------------MTVRELVAIGRypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 147 ALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPA 226
Cdd:PRK10575  161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240

                         250
                  ....*....|
gi 1327293196 227 NEFVAGF-MG 235
Cdd:PRK10575  241 LEQIYGIpMG 250
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 24-225 8.46e-20

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 86.91  E-value: 8.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  24 FSIEKGEFITLLGPSGCGKSTLLRSLAGLNPvDGGEIWVNGEEI----THQVPQQRG---------IGM-VFQSYALF-P 88
Cdd:PRK03695   17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawsAAELARHRAylsqqqtppFAMpVFQYLTLHqP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  89 NMTVEGNIAFGLkmkklasdeikREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARA-LVVKPRI------LLLDEPL 161
Cdd:PRK03695   96 DKTRTEAVASAL-----------NEVAEALGLDDKLGRSV---NQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 162 SALDAKIRKHLRQQIRDIQkEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:PRK03695  162 NSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 7-212 1.12e-19

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 89.65  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTvFE--DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ--QRGIGMVFQ 82
Cdd:PRK10522  326 RNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFT 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMtvegniafgLKMKKLASDEIKreVAKVIGLVDLTGKEKFYPH-----QLSGGQRQRVALARALVVKPRILLL 157
Cdd:PRK10522  405 DFHLFDQL---------LGPEGKPANPAL--VEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLL 473

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 158 DEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDqEEAMIMSDRIFLMNKGEI 212
Cdd:PRK10522  474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 25-231 3.09e-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: 85.54  E-value: 3.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  25 SIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQvPQQrgIGMVFQsyalfpnMTVEgNIAFGLKMKK 104
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-PQY--IKADYE-------GTVR-DLLSSITKDF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 105 LASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMN 184
Cdd:cd03237    90 YTHPYFKTEIAKPLQIEQILDREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1327293196 185 LTTIFVTHDQEEAMIMSDR--IFLMNKGEIVQAGTPEEIyTQPANEFVA 231
Cdd:cd03237   167 KTAFVVEHDIIMIDYLADRliVFEGEPSVNGVANPPQSL-RSGMNRFLK 214
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 20-245 3.45e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 85.52  E-value: 3.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP----VDGGEIWVNGEEITHQVPQQRGIGMVFQS--YALFP--NMT 91
Cdd:PRK10418   20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPlhTMH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  92 VEGnIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKH 171
Cdd:PRK10418  100 THA-RETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 172 LRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAgfmghyNLVQANKA 245
Cdd:PRK10418  179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTR------SLVSAHLA 246
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
6-221 4.14e-19

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 87.92  E-value: 4.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRfgDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ---QRGIGMVFQ 82
Cdd:PRK09700  268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAYITE 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SY---ALFPNMTVEGNIAFG--LKMKKLASdeikrevakVIGLVDLTGKEKFYPHQ-----------------LSGGQRQ 140
Cdd:PRK09700  346 SRrdnGFFPNFSIAQNMAISrsLKDGGYKG---------AMGLFHEVDEQRTAENQrellalkchsvnqniteLSGGNQQ 416

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 141 RVALARALVVKPRILLLDEPLSALD----AKIRKHLRQqirdiQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQ-- 214
Cdd:PRK09700  417 KVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQ-----LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQil 491

                         250
                  ....*....|.
gi 1327293196 215 ----AGTPEEI 221
Cdd:PRK09700  492 tnrdDMSEEEI 502
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 7-208 4.94e-19

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: 87.68  E-value: 4.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDN-TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVnGEEIThqvpqqrgIGMVFQSYA 85
Cdd:TIGR03719   8 NRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIK--------VGYLPQEPQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPNMTVEGNIAFGLKMKKLASDEIK-----------------REVAKVIGLVDLTGKekfypHQ--------------- 133
Cdd:TIGR03719  79 LDPTKTVRENVEEGVAEIKDALDRFNeisakyaepdadfdklaAEQAELQEIIDAADA-----WDldsqleiamdalrcp 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 134 --------LSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKemnlTTIFVTHdqeeamimsDRIF 205
Cdd:TIGR03719 154 pwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTH---------DRYF 220


                  ...
gi 1327293196 206 LMN 208
Cdd:TIGR03719 221 LDN 223
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
6-175 7.05e-19

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 83.74  E-value: 7.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEeitHQVPQQRGIGMVFQSY- 84
Cdd:PRK13543   14 AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 -ALFPNMTVEGNIAFglkMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSA 163
Cdd:PRK13543   91 pGLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167

                         170       180
                  ....*....|....*....|
gi 1327293196 164 LDAK--------IRKHLRQQ 175
Cdd:PRK13543  168 LDLEgitlvnrmISAHLRGG 187
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 4-165 2.64e-18

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 85.56  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVnGE--EITHqVPQQRGigmvf 81
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAY-VDQSRD----- 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 qsyALFPNMTVEGNIAFGLKMKKLAsdeiKREVA----------------KVIGlvdltgkekfyphQLSGGQRQRVALA 145
Cdd:PRK11819  398 ---ALDPNKTVWEEISGGLDIIKVG----NREIPsrayvgrfnfkggdqqKKVG-------------VLSGGERNRLHLA 457

                         170       180
                  ....*....|....*....|
gi 1327293196 146 RALVVKPRILLLDEPLSALD 165
Cdd:PRK11819  458 KTLKQGGNVLLLDEPTNDLD 477
PLN03130 PLN03130
ABC transporter C family member; Provisional
 14-221 4.55e-18

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 85.56  E-value: 4.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWVNGEeiTHQVPQqrgIGMVFqsyalfpNMTV 92
Cdd:PLN03130   628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--VAYVPQ---VSWIF-------NATV 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   93 EGNIAFGLKM------KKLASDEIKREVAKVIGlVDLT--GKEKFyphQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:PLN03130   696 RDNILFGSPFdperyeRAIDVTALQHDLDLLPG-GDLTeiGERGV---NISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  165 DAkirkHLRQQIRD--IQKEM-NLTTIFVThDQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PLN03130   772 DA----HVGRQVFDkcIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 7-214 8.54e-18

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: 81.82  E-value: 8.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRF--GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDgGEIWVNGEEITHQVPQQ--RGIGMVFQ 82
Cdd:cd03289     6 KDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKwrKAFGVIPQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFpnmtvEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTgkEKFyPHQ-----------LSGGQRQRVALARALVVK 151
Cdd:cd03289    85 KVFIF-----SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVI--EQF-PGQldfvlvdggcvLSHGHKQLMCLARSVLSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 152 PRILLLDEPLSALD----AKIRKHLRQQIRDiqkemnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQ 214
Cdd:cd03289   157 AKILLLDEPSAHLDpityQVIRKTLKQAFAD-------CTVILSEHRIEAMLECQRFLVIEENKVRQ 216
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-232 1.32e-17

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 84.06  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWvnGEEITHQVPQQRGIgMvfqsyalfpNMTVEGNIAF-- 98
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQQAWI-M---------NATVRGNILFfd 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   99 ---------GLKMKKLASDeikreVAKVIGLVDLTGKEKFYphQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIR 169
Cdd:PTZ00243   746 eedaarladAVRVSQLEAD-----LAQLGGGLETEIGEKGV--NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196  170 KHlrqqirdIQKEMNL------TTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFVAG 232
Cdd:PTZ00243   819 ER-------VVEECFLgalagkTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAA 879
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 1-213 2.58e-17

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 82.69  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQrgigmv 80
Cdd:PRK11147    1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQD------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 fqsyalfPNMTVEGN----IAFGLK------------MKKLASDEIKREVAK----------------------VIGLVD 122
Cdd:PRK11147   75 -------PPRNVEGTvydfVAEGIEeqaeylkryhdiSHLVETDPSEKNLNElaklqeqldhhnlwqlenrineVLAQLG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 123 LTGKEKFypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKemnlTTIFVTHDQEEAMIMSD 202
Cdd:PRK11147  148 LDPDAAL--SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMAT 221

                         250
                  ....*....|.
gi 1327293196 203 RIFLMNKGEIV 213
Cdd:PRK11147  222 RIVDLDRGKLV 232
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
3-223 3.01e-17

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 80.31  E-value: 3.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   3 YVNAKNLTKRFGdNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEiTHQVPQQRGIGMVFQ 82
Cdd:PRK15056    8 VVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYVPQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYAL---FPnMTVEGNIAFG----LKMKKLASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRIL 155
Cdd:PRK15056   86 SEEVdwsFP-VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 156 LLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIfLMNKGEIVQAGTPEEIYT 223
Cdd:PRK15056  165 LLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFT 230
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 3-210 5.26e-17

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: 78.05  E-value: 5.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   3 YVNAKNLTKRFGDNtvfedIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP--VDGGEIWVNGEEITHQVpqQRGIGMV 80
Cdd:cd03232    12 TVPVKGGKRQLLNN-----ISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNF--QRSTGYV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGlkmkklasdeikrevAKVIGlvdltgkekfyphqLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:cd03232    85 EQQDVHSPNLTVREALRFS---------------ALLRG--------------LSVEQRKRLTIGVELAAKPSILFLDEP 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 161 LSALDA----KIRKHLRQQIRDIQkemnltTIFVTHDQEEAMIMS--DRIFLMNKG 210
Cdd:cd03232   136 TSGLDSqaayNIVRFLKKLADSGQ------AILCTIHQPSASIFEkfDRLLLLKRG 185
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
25-225 5.41e-17

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 80.33  E-value: 5.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  25 SIEKGEFITLLGPSGCGKSTLLRSLAGLNP----VDGGEIWVNGEEITHQVPQQR------GIGMVFQ--SYALFPNMTV 92
Cdd:COG4170    29 TLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPSAKI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIAFGL----------KMKKLASDEIKREVAKViGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:COG4170   109 GDQLIEAIpswtfkgkwwQRFKWRKKRAIELLHRV-GIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTN 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 163 ALDAKIrkhlRQQIRDIQKEMN----LTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQP 225
Cdd:COG4170   188 AMESTT----QAQIFRLLARLNqlqgTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 6-212 7.15e-17

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 81.13  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNT---VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPvdG---GEIWVNGEEITHQVPQQ---RG 76
Cdd:PRK13549  262 VRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKIRNPQQaiaQG 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQS---YALFPNMTVEGNI--------AFGLKMKKLAS-DEIKREVAKViglvdltgKEK-FYPHQ----LSGGQR 139
Cdd:PRK13549  340 IAMVPEDrkrDGIVPVMGVGKNItlaaldrfTGGSRIDDAAElKTILESIQRL--------KVKtASPELaiarLSGGNQ 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 140 QRVALARALVVKPRILLLDEPLSALD--AKIrkhlrqqirDIQKEMN------LTTIFVTHDQEEAMIMSDRIFLMNKGE 211
Cdd:PRK13549  412 QKAVLAKCLLLNPKILILDEPTRGIDvgAKY---------EIYKLINqlvqqgVAIIVISSELPEVLGLSDRVLVMHEGK 482


                  .
gi 1327293196 212 I 212
Cdd:PRK13549  483 L 483
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 7-219 8.91e-17

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 78.53  E-value: 8.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGlNP---VDGGEIWVNGEEITHQVPQQR---GIGMV 80
Cdd:CHL00131   11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESILDLEPEERahlGIFLA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEG--NIAFGLKMKKLASDEIKR-EVAKVIG----LVDLtgKEKFYPHQL----SGGQRQRVALARALV 149
Cdd:CHL00131   90 FQYPIEIPGVSNADflRLAYNSKRKFQGLPELDPlEFLEIINeklkLVGM--DPSFLSRNVnegfSGGEKKRNEILQMAL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 150 VKPRILLLDEPLSALDAKIrkhLRQQIRDIQKEMNLTT--IFVTHDQE-EAMIMSDRIFLMNKGEIVQAGTPE 219
Cdd:CHL00131  168 LDSELAILDETDSGLDIDA---LKIIAEGINKLMTSENsiILITHYQRlLDYIKPDYVHVMQNGKIIKTGDAE 237
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 7-214 1.20e-16

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: 81.11  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196    7 KNLTKRF--GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDgGEIWVNG---EEITHQvPQQRGIGMVF 81
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQ-TWRKAFGVIP 1298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   82 QSYALFpnmtvEGNIAFGLKMKKLASDEIKREVAKVIGLVDLT----GKEKFY----PHQLSGGQRQRVALARALVVKPR 153
Cdd:TIGR01271 1299 QKVFIF-----SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIeqfpDKLDFVlvdgGYVLSNGHKQLMCLARSILSKAK 1373

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196  154 ILLLDEPLSALDAKIRKHLRQQIRdiQKEMNLTTIFVTHdQEEAMIMSDRiFLMNKGEIVQ 214
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEH-RVEALLECQQ-FLVIEGSSVK 1430
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 56-221 1.24e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 81.23  E-value: 1.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   56 DGGEIWVNGEEIT-HQVPQQRGI-GMVFQSYALFpNMTVEGNIAFGlkmKKLASDEIKREVAKVIGLVDLTGK--EKF-- 129
Cdd:PTZ00265  1275 NSGKILLDGVDICdYNLKDLRNLfSIVSQEPMLF-NMSIYENIKFG---KEDATREDVKRACKFAAIDEFIESlpNKYdt 1350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  130 ----YPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHdQEEAMIMSDRIF 205
Cdd:PTZ00265  1351 nvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIV 1429

                          170       180
                   ....*....|....*....|.
gi 1327293196  206 LMNK----GEIVQA-GTPEEI 221
Cdd:PTZ00265  1430 VFNNpdrtGSFVQAhGTHEEL 1450
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 4-174 2.86e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 76.14  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH-QVPQQRGIGMVFQ 82
Cdd:PRK13540    2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAFGLKMKKLAsdeikREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:PRK13540   82 RSGINPYLTLRENCLYDIHFSPGA-----VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156

                         170       180
                  ....*....|....*....|
gi 1327293196 163 ALD--------AKIRKHLRQ 174
Cdd:PRK13540  157 ALDelslltiiTKIQEHRAK 176
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 7-208 3.17e-16

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 79.39  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDN-TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVnGEEIThqvpqqrgIGMVFQSYA 85
Cdd:PRK11819   10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-APGIK--------VGYLPQEPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPNMTVEGNI--AFGLKMKKLA---------------SDEIKREVAKVIGLVDltgkekfypHQ--------------- 133
Cdd:PRK11819   81 LDPEKTVRENVeeGVAEVKAALDrfneiyaayaepdadFDALAAEQGELQEIID---------AAdawdldsqleiamda 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 134 ------------LSGGQRQRVALARALVVKPRILLLDEPLSALDAK----IRKHLRqqirdiqkEMNLTTIFVTHdqeea 197
Cdd:PRK11819  152 lrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQFLH--------DYPGTVVAVTH----- 218

                         250
                  ....*....|.
gi 1327293196 198 mimsDRIFLMN 208
Cdd:PRK11819  219 ----DRYFLDN 225
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 6-212 4.71e-16

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: 78.71  E-value: 4.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNT---VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVD-GGEIWVNGEEITHQVPQQ---RGIG 78
Cdd:TIGR02633 260 ARNLTCWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIA 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  79 MVFQS---YALFPNMTVEGNI------AFGLKMKKLASDEIKrEVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARAL 148
Cdd:TIGR02633 340 MVPEDrkrHGIVPILGVGKNItlsvlkSFCFKMRIDAAAELQ-IIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKML 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 149 VVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 17-215 5.36e-16

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 75.77  E-value: 5.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  17 TVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGL---NPVDG-GEIWVNgeeithQVPQQRGIgmvfqsyalfpnmtV 92
Cdd:COG2401    44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkgTPVAGcVDVPDN------QFGREASL--------------I 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EgniAFGLKMKKLASDEIKREVakviGLVDLTgkekFY---PHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIR 169
Cdd:COG2401   104 D---AIGRKGDFKDAVELLNAV----GLSDAV----LWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1327293196 170 KHLRQQIRDIQKEMNLTTIFVTHDQE-EAMIMSDRIFLMNKGEIVQA 215
Cdd:COG2401   173 KRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIFVGYGGVPEE 219
PLN03232 PLN03232
ABC transporter C family member; Provisional
 15-222 1.26e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 78.09  E-value: 1.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWVNGEeiTHQVPQqrgIGMVFqsyalfpNMTVE 93
Cdd:PLN03232   629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--VAYVPQ---VSWIF-------NATVR 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   94 GNIAFGlkmkklaSDEIKREVAKVIGLVDLTGKEKFYPHQ-----------LSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:PLN03232   697 ENILFG-------SDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196  163 ALDAkirkHLRQQIRD--IQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIY 222
Cdd:PLN03232   770 ALDA----HVAHQVFDscMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
PLN03232 PLN03232
ABC transporter C family member; Provisional
 9-229 1.42e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 78.09  E-value: 1.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196    9 LTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH--QVPQQRGIGMVFQSYAL 86
Cdd:PLN03232  1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVL 1321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   87 FpnmtvEGNIAFGLK----------MKKLASDEIKREVAKVIGLVD---LTGKEKFyphqlSGGQRQRVALARALVVKPR 153
Cdd:PLN03232  1322 F-----SGTVRFNIDpfsehndadlWEALERAHIKDVIDRNPFGLDaevSEGGENF-----SVGQRQLLSLARALLRRSK 1391

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196  154 ILLLDEPLSALDAKIRKHLRQQIRDiqkEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEF 229
Cdd:PLN03232  1392 ILVLDEATASVDVRTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-220 2.01e-15

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 76.85  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEI-WVNGEEITHqVPQqrgigmvfQ 82
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGY-YAQ--------D 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPN-MTVE--------------------GNIAFGlkmkklaSDEIKREVaKViglvdltgkekfyphqLSGGQRQR 141
Cdd:PRK15064  391 HAYDFENdLTLFdwmsqwrqegddeqavrgtlGRLLFS-------QDDIKKSV-KV----------------LSGGEKGR 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 142 VALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKemnlTTIFVTHDQEEAMIMSDRIFLMNKGEIVQ-AGTPEE 220
Cdd:PRK15064  447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG----TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 7-213 4.21e-15

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 75.92  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ---RGIGMVFQS 83
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 YALFPNMTVEGNIAFG-LKMKKLASDEIK--REVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEP 160
Cdd:PRK10982   82 LNLVLQRSVMDNMWLGrYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 161 LSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:PRK10982  162 TSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
8-218 5.95e-15

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 75.62  E-value: 5.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDntvfedieFSIE-------KGEFITLLGPSGCGKSTLLRSLAG-LNPvDGGEIWVNgEEITHQvPQQRGIGm 79
Cdd:PRK13409  345 DLTKKLGD--------FSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGvLKP-DEGEVDPE-LKISYK-PQYIKPD- 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 vfqsyalfPNMTVE---GNIAfglkmKKLASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILL 156
Cdd:PRK13409  413 --------YDGTVEdllRSIT-----DDLGSSYYKSEIIKPLQLERLLDKNV---KDLSGGELQRVAIAACLSRDADLYL 476

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 157 LDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQeeAMI--MSDRIflmnkgeIVQAGTP 218
Cdd:PRK13409  477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI--YMIdyISDRL-------MVFEGEP 531
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 12-224 6.50e-15

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: 76.14  E-value: 6.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   12 RFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT----HQVPQQrgIGMVFQSYALF 87
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiglHDLRFK--ITIIPQDPVLF 1372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   88 pnmtvEGNIAFGLKMKKLASDEikrEVAKVIGLVDLTGKEKFYP----HQ-------LSGGQRQRVALARALVVKPRILL 156
Cdd:TIGR00957 1373 -----SGSLRMNLDPFSQYSDE---EVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILV 1444

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327293196  157 LDEPLSALDAK----IRKHLRQQIRDIqkemnlTTIFVTHDQEEAMIMSdRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:TIGR00957 1445 LDEATAAVDLEtdnlIQSTIRTQFEDC------TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 15-228 6.74e-15

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 75.84  E-value: 6.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   15 DNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGeeiTHQVPQ------QRGIGMVFQSYALFP 88
Cdd:PTZ00265   397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDinlkwwRSKIGVVSQDPLLFS 473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   89 NmTVEGNIAFGL----------------------------------------KMKKLASDEI-----KREVAKVIGLVDL 123
Cdd:PTZ00265   474 N-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNELiemrkNYQTIKDSEVVDV 552

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  124 TGK-----------EKF------YPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLT 186
Cdd:PTZ00265   553 SKKvlihdfvsalpDKYetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1327293196  187 TIFVTHdQEEAMIMSDRIFLMN---KGEIVQAGTPEEIYTQPANE 228
Cdd:PTZ00265   633 TIIIAH-RLSTIRYANTIFVLSnreRGSTVDVDIIGEDPTKDNKE 676
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-224 7.20e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 75.55  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNG---------EEITHQV--- 71
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrRAVCPRIaym 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  72 PQqrGIGMvfqsyALFPNMTVEGNIAF-----GLkmkklasDEIKREvAKVIGLVDLTGKEKFyPH----QLSGGQRQRV 142
Cdd:NF033858   82 PQ--GLGK-----NLYPTLSVFENLDFfgrlfGQ-------DAAERR-RRIDELLRATGLAPF-ADrpagKLSGGMKQKL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 143 ALARALVVKPRILLLDE------PLSaldakirkhlRQQ----IRDIQKEM-NLTTIFVTHDQEEAMIMsDRIFLMNKGE 211
Cdd:NF033858  146 GLCCALIHDPDLLILDEpttgvdPLS----------RRQfwelIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGR 214

                         250
                  ....*....|...
gi 1327293196 212 IVQAGTPEEIYTQ 224
Cdd:NF033858  215 VLATGTPAELLAR 227
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 18-275 8.88e-15

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 75.72  E-value: 8.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGgeiwvngeEITHQvpqqRGIGMVFQSYALFPNmTVEGNI 96
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEG--------KIKHS----GRISFSPQTSWIMPG-TIKDNI 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   97 AFGLkmkklASDEIK-REVAKVIGLVD----LTGKEKFYPHQ----LSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:TIGR01271  508 IFGL-----SYDEYRyTSVIKACQLEEdialFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  168 IRKHLRQqiRDIQKEM-NLTTIFVTHDQEEaMIMSDRIFLMNKGEIVQAGTPEEIYT-QPanEFVAGFMG--HYNLVQAN 243
Cdd:TIGR01271  583 TEKEIFE--SCLCKLMsNKTRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSELQAkRP--DFSSLLLGleAFDNFSAE 657

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1327293196  244 KAKQL-------FNIETEWKVAIRPESIY--VKEQGRQYGE 275
Cdd:TIGR01271  658 RRNSIltetlrrVSIDGDSTVFSGPETIKqsFKQPPPEFAE 698
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 28-211 9.65e-15

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: 70.48  E-value: 9.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   28 KGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWVNGEEITHQVPQQRGIGMVFQSYalfpnmtvegniafglkmkkla 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  107 sdeikrevakviglvdltgkekfypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRD-----IQK 181
Cdd:smart00382  59 -------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1327293196  182 EMNLTTIFVTHDQE-----EAMIMSDRIFLMNKGE 211
Cdd:smart00382 114 EKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 29-216 1.36e-14

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 74.76  E-value: 1.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   29 GEFITLLGPSGCGKSTLLRSLAG---LNPVDGGEIWVNGEEIthQVPQQRGIGMVFQSYALFPNMTVEGNIAFGLKM--- 102
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPL--DSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  103 KKLASDEIKREVAKVIGLVDLTGkekfYPHQLSG--------GQRQRVALARALVVKPRILL-LDEPLSALDAKIRKHLR 173
Cdd:TIGR00956  867 KSVSKSEKMEYVEEVIKLLEMES----YADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1327293196  174 QQIRDIQKemNLTTIFVTHDQEEAMIMS--DRIFLMNKG-EIVQAG 216
Cdd:TIGR00956  943 KLMRKLAD--HGQAILCTIHQPSAILFEefDRLLLLQKGgQTVYFG 986
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 29-164 3.64e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 73.11  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  29 GEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVP---QQRGIGMVFQSYALFPNMTVEGNIAFGL----K 101
Cdd:PRK10762   30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIPQLTIAENIFLGRefvnR 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 102 MKKLASDEIKREVAKVIGLVDLtgkeKFYPHQLSG----GQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:PRK10762  110 FGRIDWKKMYAEADKLLARLNL----RFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 16-244 5.91e-14

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 71.04  E-value: 5.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  16 NTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGgeiwvngeEITHQvpqqRGIGMVFQSYALFPNmTVEG 94
Cdd:cd03291    50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEG--------KIKHS----GRISFSSQFSWIMPG-TIKE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  95 NIAFGLkmkklASDEIK-REVAKVIGLVDLTGKekfYPHQ-----------LSGGQRQRVALARALVVKPRILLLDEPLS 162
Cdd:cd03291   117 NIIFGV-----SYDEYRyKSVVKACQLEEDITK---FPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 163 ALDAKIRKHLRQQIrdIQKEM-NLTTIFVTHDQEEaMIMSDRIFLMNKGEIVQAGTPEEIYTQPAnEFVAGFMG--HYNL 239
Cdd:cd03291   189 YLDVFTEKEIFESC--VCKLMaNKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRP-DFSSKLMGydTFDQ 264


                  ....*
gi 1327293196 240 VQANK 244
Cdd:cd03291   265 FSAER 269
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-225 6.29e-14

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 71.37  E-value: 6.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRF----GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNP----VDGGEIWVNGEEITHQVP 72
Cdd:PRK15093    1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 QQR------GIGMVFQS---------------YALFPNMTVEGNIAFGLKMKKLASDEIKREVakviGLVDLTGKEKFYP 131
Cdd:PRK15093   81 RERrklvghNVSMIFQEpqscldpservgrqlMQNIPGWTYKGRWWQRFGWRKRRAIELLHRV----GIKDHKDAMRSFP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 132 HQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGE 211
Cdd:PRK15093  157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236

                         250
                  ....*....|....
gi 1327293196 212 IVQAGTPEEIYTQP 225
Cdd:PRK15093  237 TVETAPSKELVTTP 250
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 7-197 1.22e-13

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 71.58  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPV--------------DGGEIWvngeEIthqvp 72
Cdd:PRK10938  264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgysndltlfgrrrgSGETIW----DI----- 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  73 qQRGIGMVFQSYAL--FPNMTVEGNIAFGL------------KMKKLASDEIKRevakvIGLVDLTGKEKFypHQLSGGQ 138
Cdd:PRK10938  335 -KKHIGYVSSSLHLdyRVSTSVRNVILSGFfdsigiyqavsdRQQKLAQQWLDI-----LGIDKRTADAPF--HSLSWGQ 406

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 139 rQRVAL-ARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIFVTHDQEEA 197
Cdd:PRK10938  407 -QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 18-192 1.30e-13

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 71.70  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQRGIGM-VFQSYALFPnMTVEgni 96
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSSE--- 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  97 afGLKMKKLaSDEIKREVAKVIGLVDLTGKE------KFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSAldakIRK 170
Cdd:TIGR00954 543 --DMKRRGL-SDKDLEQILDNVQLTHILEREggwsavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA----VSV 615

                         170       180
                  ....*....|....*....|..
gi 1327293196 171 HLRQQIRDIQKEMNLTTIFVTH 192
Cdd:TIGR00954 616 DVEGYMYRLCREFGITLFSVSH 637
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 26-230 2.18e-13

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: 71.20  E-value: 2.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   26 IEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ-QRGIGMVFQSYALFPNMTVEGNIAFGLKMKK 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDvHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  105 LASDEIKREVAKVIGLVDLTGKEKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmN 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2120

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1327293196  185 LTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEFV 230
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYI 2166
PLN03130 PLN03130
ABC transporter C family member; Provisional
 18-221 3.44e-13

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 70.54  E-value: 3.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH--QVPQQRGIGMVFQSYALFpnmtvEGN 95
Cdd:PLN03130  1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKVLGIIPQAPVLF-----SGT 1328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   96 IAFGLK--------------MKKLASDEIKR-------EVAKviglvdltGKEKFyphqlSGGQRQRVALARALVVKPRI 154
Cdd:PLN03130  1329 VRFNLDpfnehndadlweslERAHLKDVIRRnslgldaEVSE--------AGENF-----SVGQRQLLSLARALLRRSKI 1395

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196  155 LLLDEPLSAL----DAKIRKHLRQQIRdiqkemNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PLN03130  1396 LVLDEATAAVdvrtDALIQKTIREEFK------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 6-195 4.07e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.98  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPvDGGEIWVNGE-EITHqvpqqrgigmvFQS 83
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQA-DSGRIHCGTKlEVAY-----------FDQ 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  84 Y--ALFPNMTVEGNIAFGlkmkklasdeiKREVA------KVIG-LVDLTgkekFYPHQ-------LSGGQRQRVALARa 147
Cdd:PRK11147  390 HraELDPEKTVMDNLAEG-----------KQEVMvngrprHVLGyLQDFL----FHPKRamtpvkaLSGGERNRLLLAR- 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1327293196 148 LVVKPRILL-LDEPLSALDAKIRKHLRQQIRDIQKemnlTTIFVTHDQE 195
Cdd:PRK11147  454 LFLKPSNLLiLDEPTNDLDVETLELLEELLDSYQG----TVLLVSHDRQ 498
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-213 1.03e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 68.78  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  20 EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQrGI--GMVF-----QSYALFPNMTV 92
Cdd:PRK11288  270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIraGIMLcpedrKAEGIIPVHSV 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  93 EGNIA---------FGL-----KMKKLASDEIKREVAKVIGlvdltgkekfyPHQ----LSGGQRQRVALARALVVKPRI 154
Cdd:PRK11288  349 ADNINisarrhhlrAGClinnrWEAENADRFIRSLNIKTPS-----------REQlimnLSGGNQQKAILGRWLSEDMKV 417

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:PRK11288  418 ILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 22-213 1.12e-12

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: 68.67  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  22 IEFSIEKGE--FITllGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEIT-HQVPQQRG-IGMVFQSYALFPNMtvegnia 97
Cdd:COG4615   351 IDLTIRRGElvFIV--GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRQlFSAVFSDFHLFDRL------- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  98 fgLKMKKLASDEikrEVAKVIGLVDLTGK-----EKFYPHQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHL 172
Cdd:COG4615   422 --LGLDGEADPA---RARELLERLELDHKvsvedGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVF 496

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1327293196 173 RQQIrdIQ--KEMNLTTIFVTHDqEEAMIMSDRIFLMNKGEIV 213
Cdd:COG4615   497 YTEL--LPelKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 8-218 1.83e-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: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDntvFE-DIEF-SIEKGEFITLLGPSGCGKSTLLRSLAG-LNPvDGGEIwVNGEEITHQvPQQRGIGMvfqsy 84
Cdd:COG1245   346 DLTKSYGG---FSlEVEGgEIREGEVLGIVGPNGIGKTTFAKILAGvLKP-DEGEV-DEDLKISYK-PQYISPDY----- 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  85 alfpNMTVEGNIAFGLKmKKLASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:COG1245   415 ----DGTVEEFLRSANT-DDFGSSYYKTEIIKPLGLEKLLDKNV---KDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMNLTTIFVTHDQeeAMI--MSDRIflmnkgeIVQAGTP 218
Cdd:COG1245   487 DVEQRLAVAKAIRRFAENRGKTAMVVDHDI--YLIdyISDRL-------MVFEGEP 533
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 6-264 5.06e-12

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 65.08  E-value: 5.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   6 AKNLTKRFGDNTvFEDIEFSIEK-GEFITLLGPSGCGKSTLLRSLAG-----LNPVDGGEIW------VNGEEITHQVPQ 73
Cdd:cd03236     3 EDEPVHRYGPNS-FKLHRLPVPReGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPPDWdeildeFRGSELQNYFTK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  74 QRGIGMVF----QSYALFPNmTVEGNIafGLKMKKLASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALV 149
Cdd:cd03236    82 LLEGDVKVivkpQYVDLIPK-AVKGKV--GELLKKKDERGKLDELVDQLELRHVLDRNI---DQLSGGELQRVAIAAALA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDQEEAMIMSDRIFLMnkgeivqAGTPEE--IYTQPA- 226
Cdd:cd03236   156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL-------YGEPGAygVVTLPKs 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1327293196 227 -----NEFVAGFmghynlvqankakqlfnIETEwKVAIRPESI 264
Cdd:cd03236   228 vregiNEFLDGY-----------------LPTE-NMRFREESI 252
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-224 5.10e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 65.91  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCG--KSTLLRSLAGlnPVDGGEIWVNGEEITHQVPQQRGIGM-- 79
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G--PDAGRRPWRF*TWCANRRALRRTIG*hr 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 -----VFQSYALFPNMTVEGNIafgLKMKKLASDEIKREVAKVIGLVDLTGKEKfypHQLSGGQRQRVALARALVVKPRI 154
Cdd:NF000106   92 pvr*gRRESFSGRENLYMIGR*---LDLSRKDARARADELLERFSLTEAAGRAA---AKYSGGMRRRLDLAASMIGRPAV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 155 LLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:NF000106  166 LYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 8-216 6.48e-12

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 66.67  E-value: 6.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196    8 NLTKRFGDNTVFE---DIEFSIEKGEFITLLGPSGCGKSTLLRSLA----GLNPVDGGEIWVNG---EEIthqVPQQRGi 77
Cdd:TIGR00956   63 RKLKKFRDTKTFDilkPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEI---KKHYRG- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   78 GMVFQSYA--LFPNMTVEGNIAFGLKMK------KLASDEIKRE-----VAKVIGLvDLTGKEKF---YPHQLSGGQRQR 141
Cdd:TIGR00956  139 DVVYNAETdvHFPHLTVGETLDFAARCKtpqnrpDGVSREEYAKhiadvYMATYGL-SHTRNTKVgndFVRGVSGGERKR 217

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196  142 VALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDQ--EEAMIMSDRIFLMNKGEIVQAG 216
Cdd:TIGR00956  218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILD-TTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFG 293
GguA NF040905
sugar ABC transporter ATP-binding protein;
7-204 9.12e-12

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 65.58  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVdG---GEIWVNGEEITHQV---PQQRGIGMV 80
Cdd:NF040905    5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH-GsyeGEILFDGEVCRFKDirdSEALGIVII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQSYALFPNMTVEGNIAFGLKMKK-------LASDEIKREVAKViGLVDLtgkekfyPHQLSG----GQRQRVALARALV 149
Cdd:NF040905   84 HQELALIPYLSIAENIFLGNERAKrgvidwnETNRRARELLAKV-GLDES-------PDTLVTdigvGKQQLVEIAKALS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 150 VKPRILLLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRI 204
Cdd:NF040905  156 KDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSI 209
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 7-221 1.04e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 65.52  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRfgDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQ---QRGIGMVFQ- 82
Cdd:PRK10982  254 RNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeaiNHGFALVTEe 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 --SYALFPNMTVEGN--IA----FGLKMKKLASDEIKREVAKVIGLVDL-TGKEKFYPHQLSGGQRQRVALARALVVKPR 153
Cdd:PRK10982  332 rrSTGIYAYLDIGFNslISnirnYKNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPE 411

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGE---IVQAG--TPEEI 221
Cdd:PRK10982  412 ILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKttTQNEI 483
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 4-236 7.06e-11

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: 61.85  E-value: 7.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDN--TVFEDIEFSIEKGEFITLLGPSGCGKSTLlrSLAGLNPVD--GGEIWVNGEEIThQVPQQ---RG 76
Cdd:cd03288    20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDIS-KLPLHtlrSR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSYALFpnmtvEGNIAFGLKMKKLASD----------EIKREVAKVIGLVDLT---GKEKFyphqlSGGQRQRVA 143
Cdd:cd03288    97 LSIILQDPILF-----SGSIRFNLDPECKCTDdrlwealeiaQLKNMVKSLPGGLDAVvteGGENF-----SVGQRQLFC 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 144 LARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEMNLTTIfvTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYT 223
Cdd:cd03288   167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI--AH-RVSTILDADLVLVLSRGILVECDTPENLLA 243

                         250
                  ....*....|...
gi 1327293196 224 QPANEFVAGFMGH 236
Cdd:cd03288   244 QEDGVFASLVRTD 256
PLN03073 PLN03073
ABC transporter F family; Provisional
 14-212 9.32e-11

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 62.96  E-value: 9.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  14 GDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGgeiwvngeeithqvpqqrgigMVFQS----YALFP 88
Cdd:PLN03073  520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSG---------------------TVFRSakvrMAVFS 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  89 NMTVEG---NIAFGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARALVVKPRILLLDEPLSAL 164
Cdd:PLN03073  579 QHHVDGldlSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1327293196 165 DAKIRKHLRQQIRDIQKEMnlttIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:PLN03073  659 DLDAVEALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 13-212 1.53e-10

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 62.11  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  13 FGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVdGGEIWVN-----GEEITHQVPQQRGIGMVFQsyal 86
Cdd:PRK10636  322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPV-SGEIGLAkgiklGYFAQHQLEFLRADESPLQ---- 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 fpnmtvegniafglKMKKLASDEIKREVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PRK10636  397 --------------HLARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1327293196 166 AKIRKHLRQQIRDIQKEMnlttIFVTHDQEEAMIMSDRIFLMNKGEI 212
Cdd:PRK10636  463 LDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
4-229 1.89e-10

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 60.60  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRF------------------GDNTVF--EDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVN 63
Cdd:PRK13546    5 VNIKNVTKEYriyrtnkermkdalipkhKNKTFFalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  64 GEeithqvpqqrgIGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLtGKEKFYP-HQLSGGQRQRV 142
Cdd:PRK13546   85 GE-----------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPvKKYSSGMRAKL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 143 ALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIqKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEI- 221
Cdd:PRK13546  153 GFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVl 231

                         250
                  ....*....|
gi 1327293196 222 --YTQPANEF 229
Cdd:PRK13546  232 pkYEAFLNDF 241
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 9-233 1.92e-10

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 59.12  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   9 LTKRFGDntVFEDIEFS-IEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWvngeeithqvpqqrgigmvfqsyal 86
Cdd:cd03222     6 CVKRYGV--FFLLVELGvVKEGEVIGIVGPNGTGKTTAVKILAGqLIPNGDNDEW------------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  87 fPNMTVegniafGLKMKKLasdeikrevakviglvdltgkekfyphQLSGGQRQRVALARALVVKPRILLLDEPLSALDA 166
Cdd:cd03222    59 -DGITP------VYKPQYI---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327293196 167 KIRKHLRQQIRDIQKEMNLTTIFVTHDQEEAMIMSDRIflmnkgeIVQAGTPEE--IYTQPA------NEFVAGF 233
Cdd:cd03222   105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI-------HVFEGEPGVygIASQPKgtregiNRFLRGY 172
PTZ00243 PTZ00243
ABC transporter; Provisional
 18-229 1.82e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 59.02  E-value: 1.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITHQVPQQ--RGIGMVFQSYALFpNMTVEGN 95
Cdd:PTZ00243  1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLF-DGTVRQN 1403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   96 IAFGLKmkklASDEikrEVAKVIGLVDLTGK-----EKFYPHQLSG------GQRQRVALARALVVKPR-ILLLDEPLS- 162
Cdd:PTZ00243  1404 VDPFLE----ASSA---EVWAALELVGLRERvasesEGIDSRVLEGgsnysvGQRQLMCMARALLKKGSgFILMDEATAn 1476

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  163 ---ALDAKIRKHLRQQIRdiqkemNLTTIFVTHdQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQPANEF 229
Cdd:PTZ00243  1477 idpALDRQIQATVMSAFS------AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 7-216 2.20e-09

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 57.11  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLN--PVDGGEIWVNGEEITHQVPQQR---GIGMVF 81
Cdd:PRK09580    5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  82 Q--------SYALFPNMTV-----------------EGNIAFGLKMKKLASDEIKREVAkvIGlvdltgkekfyphqLSG 136
Cdd:PRK09580   85 QypveipgvSNQFFLQTALnavrsyrgqepldrfdfQDLMEEKIALLKMPEDLLTRSVN--VG--------------FSG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 137 GQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQE-EAMIMSDRIFLMNKGEIVQA 215
Cdd:PRK09580  149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKS 227


                  .
gi 1327293196 216 G 216
Cdd:PRK09580  228 G 228
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 1-224 3.08e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 58.10  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   1 MSYVNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH----QvpQQRG 76
Cdd:PRK10938    1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfeQ--LQKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  77 IGMVFQSyaLFPNMTVEGNIAFGLKMKKLASDEIK-----REVAKVIGLVDLTGKEKFYphqLSGGQRQRVALARALVVK 151
Cdd:PRK10938   79 VSDEWQR--NNTDMLSPGEDDTGRTTAEIIQDEVKdparcEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 152 PRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQ 224
Cdd:PRK10938  154 PDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 21-233 1.35e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 56.05  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEithqvpqqrgiGMVFQSYALFPNMTVEGNIAFGL 100
Cdd:PRK13545   42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIENIELKG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 101 KMKKLASDEIKREVAKVIGLVDLtGKEKFYP-HQLSGGQRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDI 179
Cdd:PRK13545  111 LMMGLTKEKIKEIIPEIIEFADI-GKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 180 qKEMNLTTIFVTHDQEEAMIMSDRIFLMNKGEIVQAGTPEEIYTQpANEFVAGF 233
Cdd:PRK13545  190 -KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-YDEFLKKY 241
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 21-210 7.94e-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: 51.55  E-value: 7.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  21 DIEFSIEKGEFITLLGPSGCGKSTLLrsLAGLnpvdggeiwvngeeithqvpqqrgigmvfqsYALFPNMTVEGNIAFGl 100
Cdd:cd03238    13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGL-------------------------------YASGKARLISFLPKFS- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 101 KMKKLASDEIKREVAkvIGLVDLTGKEKFypHQLSGGQRQRVALARALVV--KPRILLLDEPLSALDAKIRKHLRQQIRD 178
Cdd:cd03238    59 RNKLIFIDQLQFLID--VGLGYLTLGQKL--STLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKG 134

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327293196 179 IQKEMNlTTIFVTHDqEEAMIMSDRIFLMNKG 210
Cdd:cd03238   135 LIDLGN-TVILIEHN-LDVLSSADWIIDFGPG 164
PLN03140 PLN03140
ABC transporter G family member; Provisional
 29-167 1.19e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 53.70  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   29 GEFITLLGPSGCGKSTLLRSLAGLNpvDGGeiWVNGEEITHQVPQQ-----RGIGMVFQSYALFPNMTVEGNIAFG--LK 101
Cdd:PLN03140   906 GVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKqetfaRISGYCEQNDIHSPQVTVRESLIYSafLR 981

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  102 MKKLASDEIKR----EVAK----------VIGLVDLTGkekfyphqLSGGQRQRVALARALVVKPRILLLDEPLSALDAK 167
Cdd:PLN03140   982 LPKEVSKEEKMmfvdEVMElveldnlkdaIVGLPGVTG--------LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 19-176 1.30e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 51.03  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  19 FEDIEFSIEKGEF----ITLL--------GPSGCGKSTLLRSLAGLNPVDGGEIWVNGEEITH-QVPQQRGIGmvfQSYA 85
Cdd:PRK13541    4 LHQLQFNIEQKNLfdlsITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIG---HNLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  86 LFPNMTVEGNIAFGLKMKKlaSDEIKREVAKVIGLVDLTgKEKFYphQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PRK13541   81 LKLEMTVFENLKFWSEIYN--SAETLYAAIHYFKLHDLL-DEKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155

                         170
                  ....*....|.
gi 1327293196 166 AKIRKHLRQQI 176
Cdd:PRK13541  156 KENRDLLNNLI 166
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
7-193 1.61e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.89  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTvfedieFSI------EKGEFITLLGPSGCGKSTLLRSLAG-----LNPVDGGEIWvngEEIThqvpqQR 75
Cdd:PRK13409   77 EEPVHRYGVNG------FKLyglpipKEGKVTGILGPNGIGKTTAVKILSGelipnLGDYEEEPSW---DEVL-----KR 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQSYalFPNMtVEGNI--------------AFGLKMKKL--ASDE--IKREVAKVIGLVDLTGKEKfypHQLSGG 137
Cdd:PRK13409  143 FRGTELQNY--FKKL-YNGEIkvvhkpqyvdlipkVFKGKVRELlkKVDErgKLDEVVERLGLENILDRDI---SELSGG 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 138 QRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKemNLTTIFVTHD 193
Cdd:PRK13409  217 ELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 83-221 2.37e-07

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: 52.32  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  83 SYALFPNMTVEGNIAF--GLKM---KKLASDEIKREVAKVIG-LVDLtGKEKFYPHQ----LSGGQRQRVALAR----AL 148
Cdd:TIGR00630 429 SIADVSELSIREAHEFfnQLTLtpeEKKIAEEVLKEIRERLGfLIDV-GLDYLSLSRaagtLSGGEAQRIRLATqigsGL 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 149 V-VkprILLLDEPlsaldaKIRKHLRQQIRDIQKEMNL-----TTIFVTHDqEEAMIMSDRIFLMNK------GEIVQAG 216
Cdd:TIGR00630 508 TgV---LYVLDEP------SIGLHQRDNRRLINTLKRLrdlgnTLIVVEHD-EDTIRAADYVIDIGPgagehgGEVVASG 577


                  ....*
gi 1327293196 217 TPEEI 221
Cdd:TIGR00630 578 TPEEI 582
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 7-193 3.14e-07

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: 51.71  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   7 KNLTKRFGDNTvfedieFSI------EKGEFITLLGPSGCGKSTLLRSLAG-----LNPVDGGEIWvngEEIThqvpqQR 75
Cdd:COG1245    77 EDPVHRYGENG------FRLyglpvpKKGKVTGILGPNGIGKSTALKILSGelkpnLGDYDEEPSW---DEVL-----KR 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  76 GIGMVFQSYalFpNMTVEGNI--------------AFGLKMKKLAS--DE--IKREVAKVIGLVDLTGKEKfypHQLSGG 137
Cdd:COG1245   143 FRGTELQDY--F-KKLANGEIkvahkpqyvdlipkVFKGTVRELLEkvDErgKLDELAEKLGLENILDRDI---SELSGG 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327293196 138 QRQRVALARALVVKPRILLLDEPLSALDAKIRKHLRQQIRDIQKEmNLTTIFVTHD 193
Cdd:COG1245   217 ELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
PLN03140 PLN03140
ABC transporter G family member; Provisional
 8-221 3.33e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 52.16  E-value: 3.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196    8 NLTKRfGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPV--DGGEIWVNGEEITHQVPQQRGiGMVFQSY 84
Cdd:PLN03140   171 NLAKK-TKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSlkVSGEITYNGYRLNEFVPRKTS-AYISQND 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   85 ALFPNMTVEGNIAFG--------------------------------LKMKKLASDEIKREVA-----KVIGL----VDL 123
Cdd:PLN03140   249 VHVGVMTVKETLDFSarcqgvgtrydllselarrekdagifpeaevdLFMKATAMEGVKSSLItdytlKILGLdickDTI 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  124 TGKEKFypHQLSGGQRQRVALARALVVKPRILLLDEPLSALDA----KIRKHLRQQIRdiqkeMNLTTIFVTHDQ--EEA 197
Cdd:PLN03140   329 VGDEMI--RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttyQIVKCLQQIVH-----LTEATVLMSLLQpaPET 401

                          250       260
                   ....*....|....*....|....
gi 1327293196  198 MIMSDRIFLMNKGEIVQAGTPEEI 221
Cdd:PLN03140   402 FDLFDDIILLSEGQIVYQGPRDHI 425
PLN03073 PLN03073
ABC transporter F family; Provisional
 4-165 3.37e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.78  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   4 VNAKNLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAgLNPVDG---------GEIWVNGEEIT------ 68
Cdd:PLN03073  178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDGipkncqilhVEQEVVGDDTTalqcvl 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  69 ------HQVPQQRGIGMVFQSYALFPNMTVEGNIAFGLKMKKLASDEIKREVAKVIGLVDLTGKE----------KFYP- 131
Cdd:PLN03073  257 ntdierTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEaraasilaglSFTPe 336

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1327293196 132 ------HQLSGGQRQRVALARALVVKPRILLLDEPLSALD 165
Cdd:PLN03073  337 mqvkatKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 133-195 3.49e-07

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 49.91  E-value: 3.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327293196 133 QLSGGQRQ------RVALARALVVKPRILLLDEPLSALDakiRKHLRQQIRDIQKEMNLTTIF----VTHDQE 195
Cdd:cd03240   115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQKNFqlivITHDEE 184
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 132-205 7.59e-07

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 48.51  E-value: 7.59e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327293196 132 HQLSGGQRQRVALARALV---VKPRIL-LLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDqEEAMIMSDRIF 205
Cdd:cd03227    76 LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHL-PELAELADKLI 151
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-213 3.09e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 48.63  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  18 VFEDIEFSIEKGEFITLLGPSGCGKSTLLRSL----AGLNPvdGGEIWVNGEEI-THQVPQ--QRGIGMVFQ---SYALF 87
Cdd:NF040905  275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsYGRNI--SGTVFKDGKEVdVSTVSDaiDAGLAYVTEdrkGYGLN 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  88 PNMTVEGNIAFGlKMKKLAS----DEIK-REVA---------KVIGLVDLTGKekfyphqLSGGQRQRVALARALVVKPR 153
Cdd:NF040905  353 LIDDIKRNITLA-NLGKVSRrgviDENEeIKVAeeyrkkmniKTPSVFQKVGN-------LSGGNQQKVVLSKWLFTDPD 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327293196 154 ILLLDEPLSALD--AK-----IRKHLRQQIRDIqkemnlttIFVTHDQEEAMIMSDRIFLMNKGEIV 213
Cdd:NF040905  425 VLILDEPTRGIDvgAKyeiytIINELAAEGKGV--------IVISSELPELLGMCDRIYVMNEGRIT 483
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 9-195 4.28e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 48.24  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   9 LTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAGLNPVDGGEI---------WVNGEEITHQVPqqrGIGM 79
Cdd:PRK10636    7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQETPALPQP---ALEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  80 VFQSYALFPNMTVEGNIA-----------FGLKMKKLASDEIKREVAKVIGLVDLTGKEKFYP-HQLSGGQRQRVALARA 147
Cdd:PRK10636   84 VIDGDREYRQLEAQLHDAnerndghaiatIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1327293196 148 LVVKPRILLLDEPLSALDAKIRKHLRQQIrdiqKEMNLTTIFVTHDQE 195
Cdd:PRK10636  164 LICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRD 207
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 8-193 3.17e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 45.65  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196   8 NLTKRFGDNTVFEDIEFSIEKGEFITLLGPSGCGKSTLLRSLAG-LNPVDGGEIWVNGEEI--THQ----VPQQRGIGMV 80
Cdd:PRK15064    6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSAGNVSLDPNERLgkLRQdqfaFEEFTVLDTV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  81 FQS--------------YALfPNMTVEGniafGLKMKKLASdeikrEVAKVIGL------------VDLTGKEKFYP-HQ 133
Cdd:PRK15064   86 IMGhtelwevkqerdriYAL-PEMSEED----GMKVADLEV-----KFAEMDGYtaearagelllgVGIPEEQHYGLmSE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 134 LSGGQRQRVALARALVVKPRILLLDEPLSALD-AKIRkhlrqQIRDIQKEMNLTTIFVTHD 193
Cdd:PRK15064  156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDiNTIR-----WLEDVLNERNSTMIIISHD 211
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
134-221 5.45e-05

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 45.02  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 134 LSGGQRQRVALARAL---------VvkprillLDEP------------LSALdakirKHLRqqirDIQkemNlTTIFVTH 192
Cdd:COG0178   486 LSGGEAQRIRLATQIgsglvgvlyV-------LDEPsiglhqrdndrlIETL-----KRLR----DLG---N-TVIVVEH 545

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1327293196 193 DqEEAMIMSDRIFLM------NKGEIVQAGTPEEI 221
Cdd:COG0178   546 D-EDTIRAADYIIDIgpgageHGGEVVAQGTPEEI 579
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 134-220 8.13e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.43  E-value: 8.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196  134 LSGGQRQRVALARALVVKPR--ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDqeEAMI-MSDRIFLMNK- 209
Cdd:PRK00635   477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD--EQMIsLADRIIDIGPg 553

                           90
                   ....*....|....*.
gi 1327293196  210 -----GEIVQAGTPEE 220
Cdd:PRK00635   554 agifgGEVLFNGSPRE 569
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 257-327 8.81e-05

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: 40.30  E-value: 8.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327293196 257 VAIRPESIYVKEQGRQYgehisapkTGTIRNHQLLGNVIRYQVDVDECELTVDLLNRSSERLLANGSQLEL 327
Cdd:pfam08402   1 LAIRPEKIRLAAAANGL--------SGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPAPGDRVGL 63
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 32-68 7.29e-04

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 39.39  E-value: 7.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1327293196  32 ITLLGPSGCGKSTLLRSLA---GLNPVDGGEIwvNGEEIT 68
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAkklGLPYLDTGGI--RTEEVG 39
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 18-50 1.90e-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: 39.39  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1327293196  18 VFEDIEFSIEKGE-FITLLGPSGCGKSTLLRSLA 50
Cdd:COG3267    31 ALARLEYALAQGGgFVVLTGEVGTGKTTLLRRLL 64
uvrA PRK00349
excinuclease ABC subunit UvrA;
134-221 2.15e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 40.06  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 134 LSGGQRQRVALA----RALV----VkprillLDEP------------LSALdakirKHLRqqirdiqkemNL--TTIFVT 191
Cdd:PRK00349  490 LSGGEAQRIRLAtqigSGLTgvlyV------LDEPsiglhqrdndrlIETL-----KHLR----------DLgnTLIVVE 548

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1327293196 192 HDqEEAMIMSDRIFLM------NKGEIVQAGTPEEI 221
Cdd:PRK00349  549 HD-EDTIRAADYIVDIgpgagvHGGEVVASGTPEEI 583
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 134-216 2.57e-03

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 38.78  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 134 LSGGQRQRVALARALVVKPR--ILLLDEPLSALDAKIRKHLRQQIRDIQKEMNlTTIFVTHDqEEAMIMSDRIFLM---- 207
Cdd:cd03270   138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHD-EDTIRAADHVIDIgpga 215

                          90
                  ....*....|.
gi 1327293196 208 --NKGEIVQAG 216
Cdd:cd03270   216 gvHGGEIVAQG 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 134-221 3.15e-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: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 134 LSGGQRQRVALARALVVK---PRILLLDEPLSALD-AKIRKHLR--QQIRD-----IQKEMNLTTIFVthdqeeamimSD 202
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfDDIKKLLEvlQRLVDkgntvVVIEHNLDVIKT----------AD 899

                          90       100
                  ....*....|....*....|....*
gi 1327293196 203 RIFLM------NKGEIVQAGTPEEI 221
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGTPEEV 924
recF PRK00064
recombination protein F; Reviewed
 154-214 8.38e-03

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 37.83  E-value: 8.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327293196 154 ILLLDEPLSALDAKIRKHLRQQIRDIQkemnlTTIFVT---HDQEEAMIMSDRIFLMNKGEIVQ 214
Cdd:PRK00064  303 ILLLDDVASELDDGRRAALLERLKGLG-----AQVFITttdLEDLADLLENAKIFHVEQGKITD 361
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
110-195 8.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327293196 110 IKREVAKVIGLVDLTGKEK---FyphqLSGGQRQ------RVALARALVVKPRILLLDEPLSALDAKIRKHL----RQQI 176
Cdd:PRK03918  766 VKAEENKVKLFVVYQGKERpltF----LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYL 841

                          90
                  ....*....|....*....
gi 1327293196 177 RDIQKemnltTIFVTHDQE 195
Cdd:PRK03918  842 RKIPQ-----VIIVSHDEE 855
PRK04182 PRK04182
cytidylate kinase; Provisional
 31-60 8.93e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 36.71  E-value: 8.93e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1327293196  31 FITLLGPSGCGKSTLLRSLA---GLNPVDGGEI 60
Cdd:PRK04182    2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEI 34
 
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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