|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-316 |
1.04e-146 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 414.87 E-value: 1.04e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSE-NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMD-EGMLRRYPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 162 EPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDfVLLDDRSEYAKKFFESK 241
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEE-ILANPANDFVADFVGAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 242 DFMAYLNTIKIKDLVIKQSDIsfdlydsrslVKYDSTVLQGIQKSIEVGKETILTVDEENNPYGWFSLTEIYKKL 316
Cdd:COG1125 241 RGLRRLSLLRVEDLMLPEPPT----------VSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRAL 305
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-241 |
4.15e-115 |
|
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: 332.34 E-value: 4.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSEN-VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLR-RYPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 162 EPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDFvLLDDRSEYAKKFFESK 241
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI-LRSPANDFVAEFVGAD 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
6.28e-103 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 302.01 E-value: 6.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAY----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydlieLR 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPE 156
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503125592 157 IILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLL 210
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
3.88e-97 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 290.85 E-value: 3.88e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIG 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
1.30e-95 |
|
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: 281.72 E-value: 1.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVI 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--DVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-211 |
1.19e-93 |
|
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: 277.05 E-value: 1.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydlieLRRGI 79
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 160 MDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLN 211
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
1.08e-87 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 266.55 E-value: 1.08e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIG 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-216 |
1.05e-85 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 261.23 E-value: 1.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeYDLIELRRGIGYVI 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-318 |
3.16e-83 |
|
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: 255.55 E-value: 3.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 11 KAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIEL----RRGIGYVIQQI 86
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGA 166
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 167 VDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKrDFVLLDDRSEYAKKFFESKDFmay 246
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTP-DEILRNPANEYVEEFIGKVDL--- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 247 lntIKIKDLvikqSDISFDLYDSRSLVKYDSTVLQGIQKSIEVGKETILTVDEENNPYGWFSLTEIYKKLNS 318
Cdd:TIGR01186 236 ---SQVFDA----ERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKK 300
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-225 |
1.34e-79 |
|
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: 241.76 E-value: 1.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIdeYDLIELRRGIGYVI 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIER--------NEKKRDFV 225
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQigtpeeiyEEPANRFV 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-242 |
5.47e-79 |
|
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: 241.39 E-value: 5.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRRG-IGYV 82
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamSRKELRELRRKkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 163 PFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDfVLLDDRSEYAKKFFESKD 242
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE-ILTNPANDYVREFFRGVD 265
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-216 |
5.88e-79 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 245.40 E-value: 5.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRR-GIGYVIQQIGLLPHLTVEDNI 98
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDItklSKKELRELRRkKMSMVFQHFALLPHRTVLENV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDE 178
Cdd:COG4175 127 AFGLEIQGVPKAERRERAREALELVGL-AGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDE 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 503125592 179 LIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:COG4175 206 LLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-219 |
6.10e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.55 E-value: 6.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAY----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIE 74
Cdd:COG1136 3 PLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRG-IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:COG1136 83 LRRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDiEEAIKLGTRIVLLNDGVIERNE 219
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
2.43e-76 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 232.77 E-value: 2.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIEL---- 75
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANP 155
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAiKLGTRIVLLNDGVI 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-215 |
5.13e-76 |
|
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: 232.95 E-value: 5.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRRG 78
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLD-LLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 158 ILMDEPFGAVDEITRRNLqDELI-KIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1127 163 LLYDEPTAGLDPITSAVI-DELIrELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
4.13e-74 |
|
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: 227.14 E-value: 4.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIGYVI 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-213 |
4.30e-73 |
|
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: 223.22 E-value: 4.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLI--ELRRGIGY 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVldllkkpepekksvakeliklvgmdegmlrrypkeLSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 162 EPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
1.26e-71 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 222.43 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENV----VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLielR 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIgyVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPE 156
Cdd:COG4525 78 RGV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503125592 157 IILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLL 210
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-216 |
8.60e-71 |
|
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: 219.52 E-value: 8.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVI 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKK----PEPEKKSVAKELIKLVGMDeGMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 160 MDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-217 |
8.52e-70 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 216.97 E-value: 8.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVI 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ--DATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIER 217
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQ 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-221 |
4.43e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 214.53 E-value: 4.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGK---LIDEYDLIELRRG 78
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEII 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKK 221
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-216 |
3.85e-68 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 217.12 E-value: 3.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIGYV 82
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503125592 163 PFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-215 |
4.83e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 212.23 E-value: 4.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGYVI 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDeLIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1131 159 TSGLDPEARRELWE-LLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-215 |
3.25e-67 |
|
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: 209.88 E-value: 3.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQ----QIgLLPhlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEII 158
Cdd:COG1122 81 FQnpddQL-FAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-216 |
1.09e-66 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 208.90 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID---EYDLIELRRGIG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVL-DLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 160 MDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-236 |
4.52e-66 |
|
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: 215.54 E-value: 4.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY-----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEY---DLIE 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQ----QigLLPHLTVEDNICFVLDLLKK-PEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVAR 149
Cdd:COG1123 340 LRRRVQMVFQdpysS--LNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 150 ALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKRdfVLLD 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGrIVEDGPTEE--VFAN 495
|
....*...
gi 503125592 229 DRSEYAKK 236
Cdd:COG1123 496 PQHPYTRA 503
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-215 |
1.37e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 206.00 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID--EYDLIELRRGIG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVL-DLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLAD-KADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 160 MDEPFGAVD-EITR------RNLQDElikihsklKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1126 160 FDEPTSALDpELVGevldvmRDLAKE--------GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-216 |
1.56e-63 |
|
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: 204.50 E-value: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIG 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT--RLPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDeGMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLP-GSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-213 |
2.85e-63 |
|
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: 199.23 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQigllP-----HLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:cd03225 81 FQN----PddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
3.69e-63 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 199.93 E-value: 3.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideyDLIELRRGIG 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPH--LTVEDnicFVL-------DLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARAL 151
Cdd:COG1121 79 YVPQRAEVDWDfpITVRD---VVLmgrygrrGLFRRPSRADREAVDEALERVGL-EDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-216 |
9.71e-63 |
|
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: 197.90 E-value: 9.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIE---QGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDE----YDLIELRRGIGYVIQQIGLLPH 91
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 92 LTVEDNICFVLDllKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEIT 171
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503125592 172 RRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-217 |
3.60e-62 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 201.08 E-value: 3.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVI 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPE-PEKKSVAKELIKLVGMD--EGMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRErPNAAAIKAKVTQLLEMVqlAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIER 217
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-217 |
3.64e-62 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 198.00 E-value: 3.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLielRRGIgyV 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---ERGV--V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 163 PFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG---VIER 217
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGpgrVVER 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-215 |
1.16e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.43 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAY-SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEY---DLIELRR 77
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNIC--------FVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVAR 149
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQR-ADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 150 ALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-215 |
2.10e-60 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 191.97 E-value: 2.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI--DEYDLIELRRGIGY 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVL-DLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 161 DEPFGAVD-EITRRNLqdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03262 160 DEPTSALDpELVGEVL--DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-237 |
2.84e-60 |
|
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: 192.55 E-value: 2.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSEnVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVI 83
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--DITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDfVLLDDRSEYAKKF 237
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE-VFKKPKNEFVAEF 229
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-215 |
7.99e-60 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 194.91 E-value: 7.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEnVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYV 82
Cdd:NF040840 1 MIRIENLSKDWKE-FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGK--DITNLPPEKRGIAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:NF040840 78 YQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISH-LLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 163 PFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-216 |
3.53e-59 |
|
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: 189.33 E-value: 3.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGK---LIDEYDLIEL 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-218 |
1.07e-58 |
|
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: 188.10 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSE----NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIEL 75
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIG--LLPHLTVEDNICFVLDLLKKP--EPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARAL 151
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERN 218
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGkIVEEG 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-215 |
3.17e-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: 184.91 E-value: 3.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGYVI 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNIcfvldllkkpepekksvakeliklvgmdegmlrrypkELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03230 80 EEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-217 |
6.37e-58 |
|
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: 189.24 E-value: 6.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 34 LLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL---RRGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEP 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI-----MLDGEDVTNVpphLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 111 EKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTI 190
Cdd:TIGR01187 76 EIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*..
gi 503125592 191 IFVTHDIEEAIKLGTRIVLLNDGVIER 217
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQ 181
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-240 |
2.44e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 187.98 E-value: 2.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYS----ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIEL 75
Cdd:COG1135 1 MIELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 156 EIILMDEPFGAVD-EITRRNLqdELIK-IHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKRdfVLLDDRSE 232
Cdd:COG1135 160 KVLLCDEATSALDpETTRSIL--DLLKdINRELGLTIVLITHEMDVVRRICDRVAVLENGrIVEQGPVLD--VFANPQSE 235
|
....*...
gi 503125592 233 YAKKFFES 240
Cdd:COG1135 236 LTRRFLPT 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-216 |
3.05e-57 |
|
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: 184.31 E-value: 3.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLL-----IPDSGEIKVKGKLI--DEYDLIELR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIGLLPhLTVEDNICFVLDL-LKKPEPEKKSVAKELIKLVGM-DEGMLRRYPKELSGGQQQRVGVARALAAN 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLhGIKLKEELDERVEEALRKAALwDEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQdELIKihsKLKK--TIIFVTHDIEEAIKLGTRIVLLNDG-VIE 216
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIE-ELIA---ELKKeyTIVIVTHNMQQAARVADRTAFLLNGrLVE 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
6.45e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 182.71 E-value: 6.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVI 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHlTVEDNICFVLDLLKKPEPEKKsvAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-240 |
2.06e-56 |
|
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: 183.08 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSE----NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGI 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIG--LLPHLTVEDNICFVLDLLKKPEPEKKsvAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERnEKKRDFVLLDDRSEYAKKF 237
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE-ELTVADLLAGPKHPYTREL 238
|
...
gi 503125592 238 FES 240
Cdd:COG1124 239 LAA 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-239 |
3.09e-56 |
|
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: 182.36 E-value: 3.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLiELRRGIGYVI 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 164 FGAVDEITRRNLQDELIKiHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDFVLLDDRSEYAKKFFE 239
Cdd:COG4555 160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVA 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-215 |
3.81e-56 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 186.00 E-value: 3.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIG 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDL--LKKPEPEKK-SVAKELIKLvgmdEGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLagAKKEEINQRvNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-215 |
4.06e-56 |
|
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: 182.00 E-value: 4.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEY---DLIELRRGI 79
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNIC--------FVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARAL 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-213 |
6.33e-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: 181.12 E-value: 6.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELrrgigYVIQQIGLLPHLTVEDNI 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFVLD--LLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQ 176
Cdd:TIGR01184 76 ALAVDrvLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 503125592 177 DELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-213 |
1.53e-55 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 179.37 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRRG 78
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANPEII 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKA-DAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-213 |
4.36e-55 |
|
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: 182.99 E-value: 4.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGK-LIDEYDLIEL---RRGIGYVIQQIGLLPHLTVEDNI 98
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvLQDSARGIFLpphRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFVLdllkKPEPEKKSVAK--ELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQ 176
Cdd:COG4148 99 LYGR----KRAPRAERRISfdEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 503125592 177 DELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-215 |
7.50e-55 |
|
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: 179.08 E-value: 7.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDnicFVL-------DLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:COG1120 81 PQEPPAPFGLTVRE---LVAlgryphlGLFGRPSAEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 156 EIILMDEPFGAVD-----EITrrnlqdELIK-IHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1120 157 PLLLLDEPTSHLDlahqlEVL------ELLRrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
9.75e-55 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 179.57 E-value: 9.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-----ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIEL 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQ----QiglLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARAL 151
Cdd:TIGR04521 81 RKKVGLVFQfpehQ---LFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRD 223
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-215 |
2.15e-54 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 177.59 E-value: 2.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGE-----IKVKGKLIDEYdliELRR 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDER---LIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNICF----VLDLLKKpepEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFgplrVRGASKE---EAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 154 NPEIILMDEPFGAVDEitrrNLQDELIKIHSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK09493 154 KPKLMLFDEPTSALDP----ELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-216 |
5.82e-54 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 176.36 E-value: 5.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG------KLIDEYDLIELRR 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNI----CFVLDLLKKPEPEKksvAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLieapCKVLGLSKEQAREK---AMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 154 NPEIILMDEPFGAVD-EITRrnlqdELIKIHSKLKKTII---FVTHDIEEAIKLGTRIVLLNDG-VIE 216
Cdd:COG4161 159 EPQVLLFDEPTAALDpEITA-----QVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGrIIE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-215 |
1.56e-53 |
|
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: 174.26 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideyDLIELRRGIGYVIQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 85 QIGLLPH--LTVEDnicFVL-------DLLKKPEPEKKSVAKELIKLVGMDEgmLRRYP-KELSGGQQQRVGVARALAAN 154
Cdd:cd03235 76 RRSIDRDfpISVRD---VVLmglyghkGLFRRLSKADKAKVDEALERVGLSE--LADRQiGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-212 |
2.66e-53 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 174.93 E-value: 2.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeydlielRRGI 79
Cdd:NF040729 2 LKIQNISKTFinnkKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVT-------KPGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 --GYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:NF040729 75 drGFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQL-TGKENLYPHQISGGMKQRTAVIRALACKPEV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLND 212
Cdd:NF040729 154 LLMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSR 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-215 |
1.10e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 172.63 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYseNVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL---RRGIG 80
Cdd:COG3840 2 LRLDDLTYRY--GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI-----LWNGQDLTALppaERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLD-LLKKPEPEKKSVAKELIKlVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRpGLKLTAEQRAQVEQALER-VGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 160 MDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-215 |
3.33e-52 |
|
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: 179.33 E-value: 3.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLIDEYDLIELR 76
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIG--LLPhLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAAN 154
Cdd:COG1123 83 RRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-215 |
3.79e-52 |
|
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: 171.71 E-value: 3.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRRG 78
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNIC--------FVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARA 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLhgrlgykpTWRSLLGRFSEEDKERALSALERVGLADKAYQR-ADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-215 |
5.53e-52 |
|
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: 172.23 E-value: 5.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG-KLIDEYDLIELRRGIG 80
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQ----QI-GLlphlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:TIGR04520 81 MVFQnpdnQFvGA----TVEDDVAFGLENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIkLGTRIVLLNDGVI 215
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-213 |
6.51e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 175.41 E-value: 6.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGklIDEYDLIELRRGIGYV 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503125592 163 PFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-213 |
2.53e-51 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 168.84 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS--ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeYDLIELRRGIGY 81
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 162 EPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-215 |
2.62e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 172.98 E-value: 2.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIE---LRRGIG 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-----FIDGEDVTHrsiQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-215 |
1.21e-50 |
|
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: 167.95 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSG-EIKVKGKLIDEYDLIELRRGI 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYV---IQQiGLLPHLTVEDNIC---F-VLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALA 152
Cdd:COG1119 81 GLVspaLQL-RFPRDETVLDVVLsgfFdSIGLYREPTDEQRERARELLELLGLAHLADRPF-GTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-216 |
1.37e-50 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 171.18 E-value: 1.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydlIELR-RG 78
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE---LEPAdRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEII 158
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-242 |
2.38e-50 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 171.75 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 6 FNDVSKAYSENVVLDKF---------SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG---KLIDEYDLI 73
Cdd:PRK10070 22 FKYIEQGLSKEQILEKTglslgvkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 74 ELRRG-IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK10070 102 EVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKrDFVLLDDRSE 232
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP-DEILNNPAND 259
|
250
....*....|
gi 503125592 233 YAKKFFESKD 242
Cdd:PRK10070 260 YVRTFFRGVD 269
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-215 |
3.72e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG------KLIDEYDLIELRR 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNI----CFVLDLLKkpePEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLieapCRVLGLSK---DQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 154 NPEIILMDEPFGAVD-EITrrnlqDELIKIHSKLKKTII---FVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK11124 159 EPQVLLFDEPTAALDpEIT-----AQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-213 |
5.20e-50 |
|
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: 163.18 E-value: 5.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQ 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 85 qigllphltvednicfvldllkkpepekksvakeliklvgmdegmlrrypkeLSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 165 GAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd00267 109 SGLDPASRERLL-ELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-215 |
1.20e-48 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 161.81 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVV-LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD---LIELRRGI 79
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 160 MDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
1.31e-48 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 160.24 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLpHLTVEDNIcfvldllkkpepekksvakeliklvgmdegmlrrypkeLSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03228 81 VPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 162 EPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIeEAIKLGTRIVLLNDG 213
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-212 |
1.48e-48 |
|
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: 161.11 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGY 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLDLLKKPEPEkkSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503125592 162 EPFGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIEEAikLGTRIVLLND 212
Cdd:COG4133 157 EPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
4.63e-48 |
|
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: 159.14 E-value: 4.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 85 qigllphltvednicfvldllkkpepekksvakeLIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:cd03214 81 ----------------------------------ALELLGLAH-LADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 165 GAVDeITRrnlQDELIKIHSKLK----KTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03214 126 SHLD-IAH---QIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-215 |
8.28e-48 |
|
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: 159.58 E-value: 8.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVldKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL---RRGIG 80
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-----LINGVDVTAAppaDRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-216 |
8.33e-48 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 160.29 E-value: 8.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIE 74
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfalDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRG-IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKsvAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:COG4181 87 LRARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDARAR--ARALLERVGLGH-RLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGtRIVLLNDGVIE 216
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAGRLV 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-164 |
1.42e-47 |
|
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: 157.04 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLPHLTVEDNI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 99 CFVLDLLKKPEPEKKSVAKELIKLVGMDEGM---LRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-215 |
2.05e-47 |
|
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: 169.24 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLpHLTVEDNICFVldllkKPEPEKKSVaKELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARA 150
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG-----DPDATDEEI-IEAARLAGLHD-FIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDiEEAIKLGTRIVLLNDGVI 215
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDKGRI 687
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-215 |
6.62e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 163.39 E-value: 6.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY-SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQiGLLPHLTVEDNIcfvldLLKKPEPEKKSVAkELIKLVGMDEgMLRRYPK-------E----LSGGQQQRVGVARAL 151
Cdd:COG4988 417 PQN-PYLFAGTIRENL-----RLGRPDASDEELE-AALEAAGLDE-FVAALPDgldtplgEggrgLSGGQAQRLALARAL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIhSKlKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRL-AK-GRTVILITHRL-ALLAQADRILVLDDGRI 549
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-239 |
1.09e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 155.29 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID-------EYDLI 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 74 -ELRRGIGYVIQQIGLLPHLTVEDNICFVLDLLKK-PEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARAL 151
Cdd:PRK11264 81 rQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGePKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 152 AANPEIILMDEPFGAVD-----EI--TRRNLQDElikihsklKKTIIFVTHDIEEAIKLGTRIVLLNDGVI-ERNEKKRD 223
Cdd:PRK11264 160 AMRPEVILFDEPTSALDpelvgEVlnTIRQLAQE--------KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQGPAKAL 231
|
250
....*....|....*.
gi 503125592 224 FVllDDRSEYAKKFFE 239
Cdd:PRK11264 232 FA--DPQQPRTRQFLE 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-213 |
3.57e-45 |
|
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: 156.81 E-value: 3.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 21 KFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDE----YDLIELRRGIGYVIQQIGLLPHLTVED 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 97 NICFVLdllKKPEPEKKSVAKE-LIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNL 175
Cdd:TIGR02142 95 NLRYGM---KRARPSERRISFErVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 503125592 176 QDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-198 |
5.08e-45 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 152.00 E-value: 5.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE----LRRGIGYVI 83
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGL-NLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 503125592 164 FGAVDEITRrnlqDELIKIHSKLK---KTIIFVTHDIE 198
Cdd:TIGR03608 162 TGSLDPKNR----DEVLDLLLELNdegKTIIIVTHDPE 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-215 |
5.33e-44 |
|
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: 150.96 E-value: 5.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID---EYDLIelRR 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpPHRIA--RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNI---------------CFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQ 142
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLAD-RADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 143 QRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-217 |
8.11e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.03 E-value: 8.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELR 76
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANPE 156
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 157 IILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIER 217
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQ 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-217 |
2.09e-43 |
|
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: 156.46 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQigllPHL---TVEDNIcfvldLLKKPE--PEKksvAKELIKLVGMDEgMLRRYPK-------E----LSGGQQQRV 145
Cdd:COG4987 414 VPQR----PHLfdtTLRENL-----RLARPDatDEE---LWAALERVGLGD-WLAALPDgldtwlgEggrrLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 146 GVARALAANPEIILMDEPFGAVDEITRRNLQDELIKiHSKlKKTIIFVTHDiEEAIKLGTRIVLLNDG-VIER 217
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALA-GRTVLLITHR-LAGLERMDRILVLEDGrIVEQ 550
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
2.75e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 149.76 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGI 79
Cdd:PRK13632 6 VMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQ-----IGLlphlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAAN 154
Cdd:PRK13632 86 GIIFQNpdnqfIGA----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMED-YLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
2.31e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.87 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI-------------DEY 70
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpaDRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 71 DLIELRRGIGYVIQQIGLLPHLTVEDNICFV-LDLLKKPEPEKKSVAKELIKLVGMDEgmlRR--YPKELSGGQQQRVGV 147
Cdd:COG4598 89 QLQRIRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLAD---KRdaYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 148 ARALAANPEIILMDEPFGAVD-----EITR--RNLQDElikihsklKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEK 220
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDpelvgEVLKvmRDLAEE--------GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
250
....*....|....*..
gi 503125592 221 KRDfVLLDDRSEYAKKF 237
Cdd:COG4598 238 PAE-VFGNPKSERLRQF 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-213 |
4.50e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 4.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydliELRRGIGYV 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNICFVLDL--LKKPEPEKKsvAKELIKLVGMDEgmlRRYPK--ELSGGQQQRVGVARALAANPEII 158
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLkgLSKAEAKRR--ADEWLERLGLGD---RANKKveELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-215 |
5.39e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 146.70 E-value: 5.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN--VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIG 80
Cdd:PRK13635 5 IIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQ-----IGllphLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:PRK13635 85 MVFQNpdnqfVG----ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMED-FLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKlGTRIVLLNDGVI 215
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-213 |
1.10e-41 |
|
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: 144.50 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIelRRGIG 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEIA--RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNI----------CFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARA 150
Cdd:cd03219 79 RTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLAD-LADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-217 |
1.27e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLpHLTVEDNIcfvldLLKKPEPEKKSVaKELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARAL 151
Cdd:COG1132 420 PQDTFLF-SGTIRENI-----RYGRPDATDEEV-EEAAKAAQAHE-FIEALPDgydtvvgergvNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHdieeaiKLGT-----RIVLLNDG-VIER 217
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH------RLSTirnadRILVLDDGrIVEQ 555
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-215 |
2.06e-41 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 143.97 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPD---SGEIKVKGKLI--DEYDLIEL 75
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndLVPGvriEGKVLFDGQDIydKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPhLTVEDNICFVLDLLK-KPEPEKKSVAKELIKLVGM-DE--GMLRRYPKELSGGQQQRVGVARAL 151
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGiKDKKELDEIVEESLKKAALwDEvkDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQdELIKihsKLKK--TIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIE-ELIQ---ELKKkyTIVIVTHNMQQAARISDRTAFFYDGEL 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-216 |
4.26e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.64 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPD---SGEIKVKGKLI--DEYDLIE 74
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQQIGLLPHlTVEDNICFVLDLLKKpepEKKSVAKELI----KLVGM-DE--GMLRRYPKELSGGQQQRVGV 147
Cdd:COG1117 90 LRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGI---KSKSELDEIVeeslRKAALwDEvkDRLKKSALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 148 ARALAANPEIILMDEPFGAVDEITRRNLqDELIKihsKLKK--TIIFVTHDIEEAIKLGTRIVLLNDG-VIE 216
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKI-EELIL---ELKKdyTIVIVTHNMQQAARVSDYTAFFYLGeLVE 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-215 |
4.40e-41 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 142.03 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeydlIELRRGIGYVI 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-215 |
4.51e-41 |
|
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: 142.34 E-value: 4.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLpHLTVEDNICfvldlLKKPEPEKKSVAkELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARA 150
Cdd:cd03245 83 VPQDVTLF-YGTLRDNIT-----LGAPLADDERIL-RAAELAGVTD-FVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-213 |
5.48e-41 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 142.16 E-value: 5.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDL---IELRRG-IGYVIQQIGLLPHLT 93
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYsqkIILRRElIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgmlRR--YPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEIT 171
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDN---RRnhKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503125592 172 RRNLQDELIKIHSKlKKTIIFVTHDiEEAIKLGTRIVLLNDG 213
Cdd:NF038007 177 ARAVLQQLKYINQK-GTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-211 |
6.50e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 141.47 E-value: 6.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLIDeyDLIELRRGIGY 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT--ALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLdllkkPE----PEKKSVAKELIKLVGMDeGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFAL-----PPtigrAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 158 ILMDEPFGAVDEITRRNLQD---ELIKihsKLKKTIIFVTHDIEEAIKLGTRIVLLN 211
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREfvfEQIR---QRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-197 |
7.86e-41 |
|
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: 144.43 E-value: 7.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY--SENVV--LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIP---DSGEIKVKGKLI---DEYDL 72
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 73 IELR-RGIGYVIQ--QIGLLPHLTVEDNICFVL---DLLKKPEPEKKsvAKELIKLVGMD--EGMLRRYPKELSGGQQQR 144
Cdd:COG0444 81 RKIRgREIQMIFQdpMTSLNPVMTVGDQIAEPLrihGGLSKAEARER--AIELLERVGLPdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 145 VGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDI 197
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDL 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-215 |
1.13e-40 |
|
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: 141.53 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL------RRGIGY 81
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-----LLDGQDITKLpmhkraRLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 162 EPFGAVDEITRRNLQdELIKiHSKLKKTIIFVT-HDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03218 159 EPFAGVDPIAVQDIQ-KIIK-ILKDRGIGVLITdHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
3.57e-40 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 140.20 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGklID-EYDLIELRR 77
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDvVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARALAANPEI 157
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRR-VGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 158 ILMDEPFGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03266 158 LLLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
5.86e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 140.16 E-value: 5.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL----- 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-----FLDGEDITHLpmhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 -RRGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgmLRRYP-KELSGGQQQRVGVARALAA 153
Cdd:COG1137 76 aRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITH--LRKSKaYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDeLIKihsKLK-KTI-IFVT-HDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQK-IIR---HLKeRGIgVLITdHNVRETLGICDRAYIISEGKV 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-265 |
1.08e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.93 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSL-----AIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI----DEYDLIE 74
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQ----QiglLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARA 150
Cdd:PRK13634 83 LRKKVGIVFQfpehQ---LFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDfvllddr 230
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 503125592 231 seyakkFFESKDFMAYL-----NTIKIKDLVIKQSDISFD 265
Cdd:PRK13634 233 ------IFADPDELEAIgldlpETVKFKRALEEKFGISFP 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-196 |
1.62e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.41 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRRGIGYVIQ--QIGLLPHLT 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVFQdpYASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICFVLDLLK-KPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITR 172
Cdd:COG4608 114 VGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190
....*....|....*....|....*....|.
gi 503125592 173 -------RNLQDELikihsKLkkTIIFVTHD 196
Cdd:COG4608 194 aqvlnllEDLQDEL-----GL--TYLFISHD 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-215 |
2.45e-39 |
|
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: 137.69 E-value: 2.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 21 KFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVIQQIGLLPHLTVEDNICF 100
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 101 VLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELI 180
Cdd:TIGR01277 94 GLHPGLKLNAEQQEKVVDAAQQVGIAD-YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 503125592 181 KIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-215 |
3.33e-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: 136.19 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS--ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHlTVEDNIcfvldllkkpepekksvakeliklvgmdegmlrrypkeLSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03246 81 LPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503125592 162 EPFGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:cd03246 122 EPNSHLDVEGERALN-QAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-215 |
4.94e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 138.27 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIELRRGIGYVIQQI 86
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-----LAGTAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLLPHLTVEDNICfvLDLLKKPEPEkksvAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGA 166
Cdd:PRK11247 91 RLLPWKKVIDNVG--LGLKGQWRDA----ALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 167 VDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-213 |
9.88e-39 |
|
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: 136.33 E-value: 9.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIEL 75
Cdd:TIGR02211 1 LLKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 R-RGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAAN 154
Cdd:TIGR02211 81 RnKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRI-NHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLgTRIVLLNDG 213
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-215 |
1.85e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 135.87 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 21 KFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKliDEYDLIELRRGIGYVIQQIGLLPHLTVEDNICF 100
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 101 VLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELI 180
Cdd:PRK10771 95 GLNPGLKLNAAQREKLHAIARQMGIED-LLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*
gi 503125592 181 KIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-215 |
4.48e-38 |
|
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: 134.42 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGYVI 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
6.39e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 133.32 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAY---SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRR 77
Cdd:PRK13650 2 SNIIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQ-----IGllphLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK13650 82 KIGMVFQNpdnqfVG----ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQD-FKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEaIKLGTRIVLLNDGVIE 216
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVE 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-215 |
7.66e-37 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 139.62 E-value: 7.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:TIGR03375 464 IEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLpHLTVEDNICfvldlLKKPEPEKKSVAkELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARA 150
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIA-----LGAPYADDEEIL-RAAELAGVTE-FVRRHPDgldmqigergrSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-215 |
1.10e-36 |
|
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: 130.41 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeyDLIELRRGIGYVI 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPepekKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKV-KGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03268 154 TNGLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
1.88e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 131.44 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMIN--GLLIPD---SGEIKVKGKLI--DEYDLIE 74
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQQIGLLPhLTVEDNICFVLDL--LKKPEPEKKSVAKELIKLVGMDEGMLRRYPKE--LSGGQQQRVGVARA 150
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLkgIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSAlgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKRDFV 225
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGdLIEYNDTKQMFM 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-213 |
2.40e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.30 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGI 79
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNICFVLdllkkpEPEKKSV---------AKELIKLVGMDEGmLRRYPKELSGGQQQRVGVARA 150
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGR------EPRRGGLidwramrrrARELLARLGLDID-PDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 151 LAANPEIILMDEPFGA--VDEItrrnlqDELIKIHSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:COG1129 155 LSRDARVLILDEPTASltEREV------ERLFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-213 |
5.83e-36 |
|
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: 128.85 E-value: 5.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGeFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGYVI 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 164 FGAVDEITR---RNLQDELIKihsklKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03264 158 TAGLDPEERirfRNLLSELGE-----DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-216 |
6.48e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.09 E-value: 6.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI-------------DEYDLIE 74
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQQIGLLPHLTVEDNI----CFVLDLLKKpepEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARA 150
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHMTVLENVmeapIQVLGLSKQ---EARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 151 LAANPEIILMDEPFGAVDEitrrNLQDELIKIHSKLK---KTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
1.13e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 130.59 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY-----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEI---------KVKGKLIDE 69
Cdd:PRK13651 3 IKVKNIVKIFnkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 70 Y--DLI-------------ELRRGIGYVIQ----QiglLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGML 130
Cdd:PRK13651 83 VleKLViqktrfkkikkikEIRRRVGVVFQfaeyQ---LFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 131 RRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLL 210
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
....*
gi 503125592 211 NDGVI 215
Cdd:PRK13651 239 KDGKI 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-216 |
1.84e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.78 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDE--YDLIELRRGIGYVIQ----Qigl 88
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQypeyQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 89 LPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMD-EGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAV 167
Cdd:PRK13637 96 LFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 168 DEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
3.19e-35 |
|
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: 125.23 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIGYV 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQqigllphltvednicfvldllkkpepekksvakeliklvgmdegmlrrypkeLSGGQQQRVGVARALAANPEIILMDE 162
Cdd:cd03216 81 YQ----------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 163 PFGA--VDEItrrnlqDELIKIHSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03216 109 PTAAltPAEV------ERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-215 |
8.38e-35 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 126.62 E-value: 8.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL------RRGIGY 81
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKI-----LIDGQDITHLpmheraRLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLDLLKK-PEPEKKSVAKELIKLVGMdeGMLRRYPK-ELSGGQQQRVGVARALAANPEIIL 159
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQI--SHLRDNKAmSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 160 MDEPFGAVDEITRRNLQdELIKiHSKLKKTIIFVT-HDIEEAIKLGTRIVLLNDGVI 215
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIK-KIIK-HLKERGIGVLITdHNVRETLDICDRAYIISDGKV 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-215 |
8.43e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.90 E-value: 8.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN------VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG-KLIDEYDLIEL 75
Cdd:PRK13633 4 MIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQ----QIgllPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgmLRRY-PKELSGGQQQRVGVARA 150
Cdd:PRK13633 84 RNKAGMVFQnpdnQI---VATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYE--YRRHaPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKlGTRIVLLNDGVI 215
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-209 |
8.66e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 132.41 E-value: 8.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHlTVEDNIcfvldLLKKPEPEKKSVaKELIKLVGMDE----------GMLRRYPKELSGGQQQRVGVARALA 152
Cdd:TIGR02857 402 PQHPFLFAG-TIAENI-----RLARPDASDAEI-REALERAGLDEfvaalpqgldTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIEEAIKLGTRIVL 209
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-216 |
1.02e-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: 126.19 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHlTVEDNIcfvldLLKKPEPEKKSVaKELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARAL 151
Cdd:cd03254 83 LQDTFLFSG-TIMENI-----RLGRPNATDEEV-IEAAKEAGAHD-FIMKLPNgydtvlgenggNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDIeEAIKLGTRIVLLNDG-VIE 216
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRL-STIKNADKILVLDDGkIIE 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-235 |
2.10e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 125.42 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS--ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIgLLPHLTVEDNICFvldllKKPEPEKKSV--------AKELIKlvGMDEG---MLRRYPKELSGGQQQRVGVARA 150
Cdd:cd03251 81 VSQDV-FLFNDTVAENIAY-----GRPGATREEVeeaaraanAHEFIM--ELPEGydtVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELikihSKLKK--TIIFVTHDIeEAIKLGTRIVLLNDGVIErnEKKRDFVLLD 228
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAAL----ERLMKnrTTFVIAHRL-STIENADRIVVLEDGKIV--ERGTHEELLA 225
|
....*..
gi 503125592 229 DRSEYAK 235
Cdd:cd03251 226 QGGVYAK 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-239 |
6.82e-34 |
|
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: 124.26 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLpHLTVEDNICFvlDLLKKPEPEKKSVAKELI---KLVGMDEG---MLRRYPKELSGGQQQRVGVARALAANPE 156
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRY--GRPDATDEEVIEAAKAAQihdKIMRFPDGydtIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 157 IILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRdfvLLDDRSEYAKK 236
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEE---LLAKGGLYAEM 232
|
...
gi 503125592 237 FFE 239
Cdd:cd03253 233 WKA 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-213 |
7.19e-34 |
|
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: 123.70 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYS-------ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVK--GKLID---- 68
Cdd:COG4778 3 TLLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 69 -EYDLIELRRG-IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVG 146
Cdd:COG4778 83 sPREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 147 VARALAANPEIILMDEPFGAVDEITRRNLQdELIKihsKLKK---TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVV-ELIE---EAKArgtAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-215 |
1.28e-33 |
|
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: 122.37 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYdliELRRGIGYVIQQI 86
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLlpHL---TVEDNicfvLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03226 81 DY--QLftdSVREE----LLLGLKELDAGNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDeLIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03226 154 TSGLDYKNMERVGE-LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-213 |
1.62e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 126.14 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 34 LLGPSGCGKTTILKMINGLLIPDSGEIKVKGK-LIDEYDLIEL---RRGIGYVIQQIGLLPHLTVEDNICFVLDllkkpe 109
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvLFDAEKGICLppeKRRIGYVFQDARLFPHYKVRGNLRYGMA------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 110 peKKSVAK--ELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLK 187
Cdd:PRK11144 103 --KSMVAQfdKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180
....*....|....*....|....*.
gi 503125592 188 KTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-213 |
2.27e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 128.22 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDeydlIE-----LRR 77
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR----IRsprdaIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLvgMDE-GM---LRRYPKELSGGQQQRVGVARALAA 153
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIREL--SERyGLdvdPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 154 NPEIILMDEPfGAV---DEItrrnlqDELIKIHSKLK---KTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:COG3845 159 GARILILDEP-TAVltpQEA------DELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-199 |
2.44e-33 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 122.52 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHlTVEDNICFVLdLLKKPEPEKKSVAKELIKLvGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPW-QIRNQQPDPAIFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 503125592 162 EPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEE 199
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-215 |
3.08e-33 |
|
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: 121.77 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIGYV 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNIcfVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:cd03224 81 PEGRRIFPELTVEENL--LLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 163 PF-----GAVDEITrrnlqdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03224 159 PSeglapKIVEEIF------EAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-218 |
3.55e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 129.07 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAY---SENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD---LIE 74
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRG-IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARALAA 153
Cdd:PRK10535 83 LRREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 154 NPEIILMDEPFGAVDEITrrnlQDELIKIHSKLKK---TIIFVTHDIEEAIKlGTRIVLLNDGVIERN 218
Cdd:PRK10535 162 GGQVILADEPTGALDSHS----GEEVMAILHQLRDrghTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-215 |
4.33e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 123.37 E-value: 4.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGE---IKVKGKLIDEYDLIELRR 77
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQ-----IGLlphlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK13640 85 KVGIVFQNpdnqfVGA----TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAiKLGTRIVLLNDGVI 215
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
4.70e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN-VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI--DEYDLIELRRGI 79
Cdd:PRK13639 1 ILETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQ----QIgLLPhlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:PRK13639 81 GIVFQnpddQL-FAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 156 EIILMDEPFGAVDEITrrnlQDELIKIHSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13639 157 EIIVLDEPTSGLDPMG----ASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-215 |
1.27e-32 |
|
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: 120.72 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY---SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIG 80
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQigllPHL---TVEDNICFVLDLLKKPEPE---KKSVAKELIK--------LVGmDEGmlrrypKELSGGQQQRVG 146
Cdd:cd03249 81 LVSQE----PVLfdgTIAENIRYGKPDATDEEVEeaaKKANIHDFIMslpdgydtLVG-ERG------SQLSGGQKQRIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 147 VARALAANPEIILMDEPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQNGQV 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-215 |
1.29e-32 |
|
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: 120.86 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDE---YDLIelRR 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlppHRIA--RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNicfvLDLLKKPEPEKKSVAKELiklvgmdEGMLRRYP--KE--------LSGGQQQRVGV 147
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEEN----LLLGAYARRDRAEVRADL-------ERVYELFPrlKErrrqragtLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 148 ARALAANPEIILMDEP------------FGAVDEITRRNLqdelikihsklkkTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG0410 148 GRALMSRPKLLLLDEPslglapliveeiFEIIRRLNREGV-------------TILLVEQNARFALEIADRAYVLERGRI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-213 |
1.35e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.69 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSE-NV---VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDL---IELR-RG 78
Cdd:PRK11629 9 DNLCKRYQEgSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRyPKELSGGQQQRVGVARALAANPEII 158
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGtRIVLLNDG 213
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-217 |
1.73e-32 |
|
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: 126.40 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 14 SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLPHlT 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICfvldLLKKPEPEKksvAKELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:COG4618 422 IAENIA----RFGDADPEK---VVAAAKLAGVHE-MILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 163 PFGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIeEAIKLGTRIVLLNDGVIER 217
Cdd:COG4618 494 PNSNLDDEGEAALA-AAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQA 546
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-210 |
3.94e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 12 AYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrRGIGYVIQQIGL--- 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 89 LPhLTVEDNICFVL----DLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:NF040873 70 LP-LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503125592 165 GAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAiKLGTRIVLL 210
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-215 |
4.68e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 124.91 E-value: 4.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY---SENVV--LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVK--GKLIDEYDLIEL 75
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRG-----IGYVIQQIGLLPHLTVEDNICFVLDLlKKPEPEKKSVAKELIKLVGMDE----GMLRRYPKELSGGQQQRVG 146
Cdd:TIGR03269 359 GRGrakryIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEekaeEILDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 147 VARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-210 |
6.02e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.56 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPDS---GEIKVKGKLI--DEYDLIELR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIGLLPHLTVEDNICFVLDL--LKKPEPEKKSVAKELIKLVGM-DE--GMLRRYPKELSGGQQQRVGVARAL 151
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLngLVKSKKELDERVEWALKKAALwDEvkDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDIEEAIKLGTRIVLL 210
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFL 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-203 |
6.50e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 119.87 E-value: 6.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD---LIELRRGI 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNICFVL-DLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEII 158
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKL 203
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSI 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-215 |
1.12e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.02 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSE---------NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 72 LIE---LRRGIGYVIQQ-IGLL-PHLTVEDNICFVL-DLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRV 145
Cdd:PRK10419 81 RAQrkaFRRDIQMVFQDsISAVnPRKTVREIIREPLrHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 146 GVARALAANPEIILMDEPFGAVDeitrRNLQDELIKIHSKLKK----TIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLD----LVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
1.33e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSE-NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQ----QIGllpHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgmLR-RYPKELSGGQQQRVGVARALAANPE 156
Cdd:PRK13647 84 VFQdpddQVF---SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWD--FRdKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 157 IILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-213 |
1.84e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.58 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDS---GEIKVKGKLIDEY-----DLIE 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQQIGLLPHLTVEDNIC--------FVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVG 146
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRV-STLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 147 VARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-234 |
2.80e-31 |
|
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: 117.20 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQiGLLPHLTVEDNICfvldlLKKPEPEKKSVAkELIKLVG-------MDEG---MLRRYPKELSGGQQQRVGVARAL 151
Cdd:cd03252 81 VLQE-NVLFNRSIRDNIA-----LADPGMSMERVI-EAAKLAGahdfiseLPEGydtIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIeEAIKLGTRIVLLNDGVIErnEKKRDFVLLDDRS 231
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVMEKGRIV--EQGSHDELLAENG 228
|
...
gi 503125592 232 EYA 234
Cdd:cd03252 229 LYA 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-215 |
2.91e-31 |
|
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: 116.86 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDE---YDLIelRRGIGY 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlppHERA--RAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLDLLKKPEpekKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRS---RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 162 EPF-----GAVDEItrrnlQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:TIGR03410 157 EPTegiqpSIIKDI-----GRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-213 |
3.33e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.30 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYDLIEL----- 75
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDISLLplhar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 -RRGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSV-AKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK10895 76 aRRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQdeliKIHSKLKKT---IIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIK----RIIEHLRDSglgVLITDHNVRETLAVCERAYIVSQG 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-238 |
4.55e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.01 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-----ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID----EYDLIE 74
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQ--QIGLLPHLTVEDnICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKD-VEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDfvLLDDRsE 232
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE--IFSDK-E 237
|
....*.
gi 503125592 233 YAKKFF 238
Cdd:PRK13641 238 WLKKHY 243
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-223 |
5.70e-31 |
|
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: 122.07 E-value: 5.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 14 SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLPHlT 93
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICFVLDllkKPEPEKksvAKELIKLVGMDEgMLRRYPK-----------ELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:TIGR01842 408 VAENIARFGE---NADPEK---IIEAAKLAGVHE-LILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 163 PFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIeEAIKLGTRIVLLNDGVIERNEKKRD 223
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDE 539
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-211 |
1.68e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.88 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIEL 75
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 R-RGIGYVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAAN 154
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLN 211
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-214 |
2.25e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.24 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIElRRGIGYVI 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDGV 214
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-215 |
2.79e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.80 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVI 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIGLLPHLTVEDNICFvld--llkKPEPEKKSVAKELIKLVGMDEgmLR-RYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:COG4604 82 QENHINSRLTVRELVAFgrfpyskgRLTAEDREIIDEAIAYLDLED--LAdRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 161 DEPFGAVD-----EITR--RNLQDElikihskLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG4604 160 DEPLNNLDmkhsvQMMKllRRLADE-------LGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-241 |
4.89e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPD---SGEIKVKGKLIDEYDLIEL 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPHLTVEDNICFVLDL--LKKPEPEKKSVAKELIKLVGMDEGMLRRY---PKELSGGQQQRVGVARA 150
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDELIKIhsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDfVLLDDR 230
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE-VFTNPR 237
|
250
....*....|.
gi 503125592 231 SEYAKKFFESK 241
Cdd:PRK14247 238 HELTEKYVTGR 248
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-200 |
4.99e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.88 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPD---SGEIKVKGKLI--DEYDLIEL 75
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPHlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDE--GMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALWDEvkDKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQdELIKihsKLKK--TIIFVTHDIEEA 200
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIE-ELMH---ELKEqyTIIIVTHNMQQA 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
6.20e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.29 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLiELRRGIGY 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 162 EPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
8.02e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.77 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHlTVEDNIcfvldLLKKPEP--EKKSVAKE---LIKLVGMDEGM---LRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNL-----LLAAPNAsdEALIEVLQqvgLEKLLEDDKGLnawLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQdELIKIHSKlKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQIL-ELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQI 551
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
8.72e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.08 E-value: 8.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYS--ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIG 80
Cdd:PRK13648 7 IIVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQ-----IGLlphlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgmLRRY-PKELSGGQQQRVGVARALAAN 154
Cdd:PRK13648 87 IVFQNpdnqfVGS----IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE--RADYePNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKlGTRIVLLNDGVI 215
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-213 |
1.28e-29 |
|
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: 111.79 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKF-----SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGklideydlielrrG 78
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQiGLLPHLTVEDNICFVLDLlkkpEPEK-KSVAK------ELIKLVGMDE------GMLrrypkeLSGGQQQRV 145
Cdd:cd03250 68 IAYVSQE-PWIQNGTIRENILFGKPF----DEERyEKVIKacalepDLEILPDGDLteigekGIN------LSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 146 GVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIeEAIKLGTRIVLLNDG 213
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-215 |
1.33e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.87 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MA-IIEFNDVSKAY----------------------SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDS 57
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 58 GEIKVKGKLIdeyDLIELrrgigyviqQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGM---LRRYp 134
Cdd:COG1134 81 GRVEVNGRVS---ALLEL---------GAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIdqpVKTY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 135 kelSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDeliKIHSKLK--KTIIFVTHDIEEAIKLGTRIVLLND 212
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLA---RIRELREsgRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
...
gi 503125592 213 GVI 215
Cdd:COG1134 222 GRL 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-216 |
1.93e-29 |
|
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: 111.86 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIdeyDLIELrrgigyviqQIGLLPHL 92
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLLGL---------GGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITR 172
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPV-KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503125592 173 RNLQDeliKIHSKLK--KTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:cd03220 179 EKCQR---RLRELLKqgKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
2.07e-29 |
|
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: 110.48 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSEN--VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDlIELRRGIGY 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQigllPHL---TVEDNIcfvldllkkpepekksvakeliklvgmdegmlrryPKELSGGQQQRVGVARALAANPEII 158
Cdd:cd03247 80 LNQR----PYLfdtTLRNNL-----------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 159 LMDEPFGAVDEITRRNLqdeLIKIHSKLK-KTIIFVTHDIeEAIKLGTRIVLLNDGVIE 216
Cdd:cd03247 121 LLDEPTVGLDPITERQL---LSLIFEVLKdKTLIWITHHL-TGIEHMDKILFLENGKII 175
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-196 |
6.22e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 115.92 E-value: 6.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY-SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQigllPHL---TVEDNIcfvldLLKKPEPEKKSVAKELIKlVGMDEgMLRRYP-----------KELSGGQQQRVGVA 148
Cdd:TIGR02868 415 AQD----AHLfdtTVRENL-----RLARPDATDEELWAALER-VGLAD-WLRALPdgldtvlgeggARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503125592 149 RALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHD 196
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
7.15e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 111.33 E-value: 7.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY-----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydLIELRR 77
Cdd:COG1101 1 MLELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 G--IGYVIQ--QIGLLPHLTVEDNIC----------FVLDLLKKpepeKKSVAKELIKLVGMD-EGMLRRYPKELSGGQQ 142
Cdd:COG1101 79 AkyIGRVFQdpMMGTAPSMTIEENLAlayrrgkrrgLRRGLTKK----RRELFRELLATLGLGlENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 143 QRVGVARALAANPEIILMDEPFGAVD--------EITrrnlqDELIKIHsKLkkTIIFVTHDIEEAIKLGTRIVLLNDGV 214
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpktaalvlELT-----EKIVEEN-NL--TTLMVTHNMEQALDYGNRLIMMHEGR 226
|
.
gi 503125592 215 I 215
Cdd:COG1101 227 I 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-215 |
1.11e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.80 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-----ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSG-----EIKVKGKLIDEYdLI 73
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdDITITHKTKDKY-IR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 74 ELRRGIGYVIQ-QIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK13646 82 PVRKRIGMVFQfPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-213 |
2.07e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIgLLPH-LTVEDNICF----VLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:PRK11231 82 PQHH-LTPEgITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 158 ILMDEPFGAVDeitrRNLQDELIKIHSKLK---KTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK11231 160 VLLDEPTTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-213 |
2.31e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.19 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY-SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE---LRRG 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLDLL-KKPEPEKKSVAKELIKLVGMDEGmlRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAgASGDDIRRRVSAALDKVGLLDKA--KNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 158 ILMDEPFGAVDEitrrNLQDELIKIHSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10908 159 LLADEPTGNLDD----ALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-223 |
3.14e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS-----ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEY----DLIE 74
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 LRRGIGYVIQ-QIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRD 223
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-213 |
5.21e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.37 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAY---SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKL------IDEYDLIELRRG 78
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNICFVLDLLK-KPEPEKKSVAKELIKLVGMDEGMLRRY---PKELSGGQQQRVGVARALAAN 154
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQdeliKIHSKLKK--TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIE----KLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
7.80e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 7.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGI 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQ----QIgLLPhlTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:PRK13652 81 GLVFQnpddQI-FSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-240 |
8.74e-28 |
|
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: 112.86 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLlIPDSGEIKVKGKLIDEYD---LIELRRGIgyviqQI-------GL 88
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRM-----QVvfqdpfgSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 89 LPHLTVEDNICFVLDLLKkPEP---EKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFG 165
Cdd:COG4172 376 SPRMTVGQIIAEGLRVHG-PGLsaaERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 166 AVDEITR-------RNLQDELikihsKLkkTIIFVTHDIE--EAikLGTRIVLLNDG-VIERNEkkRDFVLLDDRSEYAK 235
Cdd:COG4172 455 ALDVSVQaqildllRDLQREH-----GL--AYLFISHDLAvvRA--LAHRVMVMKDGkVVEQGP--TEQVFDAPQHPYTR 523
|
....*
gi 503125592 236 KFFES 240
Cdd:COG4172 524 ALLAA 528
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-203 |
1.79e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.82 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDsGEIKVKGKL------IDE--YDLIEL 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVeffnqnIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPhLTVEDNICFVLDLLK-KPEPEKKSVAKELIKLVGM-DE--GMLRRYPKELSGGQQQRVGVARAL 151
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwDEikHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKL 203
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-215 |
3.08e-27 |
|
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: 106.65 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGkLIDEYDLIELRRGIGYVI-QQIGLLPH 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 92 LTVEDNICFVLDLLKKPEPEKKSVAKELIKLvgMDEGMLRRYP-KELSGGQQQRVGVARALAANPEIILMDEPFGAVDEI 170
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSEL--LDLEELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503125592 171 TRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-215 |
4.29e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.55 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIG 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDnicfVLDLLKKP--------EPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQ----VVEMGRTPhrsrfdtwTETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 153 ANPEIILMDEPFGAVDeITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK09536 156 QATPVLLLDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-213 |
9.58e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 106.33 E-value: 9.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLL-----IPDSGEIKVKGKLIDEY-DLIELRRGIGY 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIFNYrDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPhLTVEDNICFVLDLLK-KPEPEKKSVAKELIKLVGMDEGMLRRY---PKELSGGQQQRVGVARALAANPEI 157
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKLkkTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDG 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-204 |
1.11e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.19 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELrrgIGYVIQQIGLLPHLTV 94
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA---CHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 95 EDNICFVLDLLKKPEPEkksvAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRN 174
Cdd:PRK13539 91 AENLEFWAAFLGGEELD----IAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180 190
....*....|....*....|....*....|....*
gi 503125592 175 LQdELIKIHSKLKKTIIFVTH---DIEEA--IKLG 204
Cdd:PRK13539 166 FA-ELIRAHLAQGGIVIAATHiplGLPGAreLDLG 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-240 |
1.24e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 105.69 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAY---------SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD 71
Cdd:COG4167 2 SALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 72 LIELRRGIGYVIQ--QIGLLPHLtvedNICFVLDL-LKK----PEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQR 144
Cdd:COG4167 82 YKYRCKHIRMIFQdpNTSLNPRL----NIGQILEEpLRLntdlTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 145 VGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKRd 223
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGeVVEYGKTAE- 236
|
250
....*....|....*..
gi 503125592 224 fVLLDDRSEYAKKFFES 240
Cdd:COG4167 237 -VFANPQHEVTKRLIES 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
1.24e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN-----VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG-----KLIDEYDL 72
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 73 I-----------ELRRGIGYVIQqiglLPHL-----TVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKE 136
Cdd:PRK13631 101 TnpyskkiknfkELRRRVSMVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 137 LSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDeLIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-215 |
1.27e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGYVI---QQigLL 89
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVFgqrSQ--LW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 90 PHLTVEDNicfvLDLLKK----PEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFG 165
Cdd:COG4586 109 WDLPAIDS----FRLLKAiyriPDAEYKKRLDELVELLDLGE-LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503125592 166 AVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-195 |
1.42e-26 |
|
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: 103.40 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIP--DSGEIKVKGKLIdeyDLIELRRGIGYVIQQIGLLPHLTVE 95
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 96 DNICFVLDLlkkpepekksvakeliklvgmdegmlrrypKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNL 175
Cdd:cd03213 101 ETLMFAAKL------------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180
....*....|....*....|
gi 503125592 176 QdELIKIHSKLKKTIIFVTH 195
Cdd:cd03213 151 M-SLLRRLADTGRTIICSIH 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-213 |
1.66e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 110.10 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIdEYDLIELRRGIGYVIQQIGLLPHLTVEDNI 98
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDE 178
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....*
gi 503125592 179 LIKIHSklKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:TIGR01257 1104 LLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-217 |
4.85e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 4.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 6 FNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIdeydlielrrgIGYVIQQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR-----------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 86 IGLLPHLTVEDNICFVLDLLKKPEPEKKSV--------------------------------AKELIKLVGMDEGMLRRY 133
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELEELeaklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 134 PKELSGGQQQRVGVARALAANPEIILMDEPfgavdeiTrrN---------LQDELikihSKLKKTIIFVTHD---IEEAI 201
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEP-------T--NhldlesiewLEEFL----KNYPGTVLVVSHDryfLDRVA 216
|
250
....*....|....*.
gi 503125592 202 klgTRIVLLNDGVIER 217
Cdd:COG0488 217 ---TRILELDRGKLTL 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-213 |
1.19e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIEL--RRGi 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarRRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 gyVI-QQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPkELSGGQQQRVGVARALA------ 152
Cdd:PRK13548 80 --VLpQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 153 ANPEIILMDEPFGAVDeitrrnL--QDELIKIHSKLKK----TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK13548 157 GPPRWLLLDEPTSALD------LahQHHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQG 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
2.33e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.12 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIEL--RRGigy 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQ---------------IGLLPHLTvednicfvldllkkPEPEKKSVAKELIKLVGMDEGMLRRYPkELSGGQQQRVG 146
Cdd:COG4559 79 VLPQhsslafpftveevvaLGRAPHGS--------------SAAQDRQIVREALALVGLAHLAGRSYQ-TLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 147 VARALA-------ANPEIILMDEPFGAVD------------EITRRNLqdelikihsklkkTIIFVTHDIEEAIKLGTRI 207
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDlahqhavlrlarQLARRGG-------------GVVAVLHDLNLAAQYADRI 210
|
....*.
gi 503125592 208 VLLNDG 213
Cdd:COG4559 211 LLLHQG 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-215 |
3.03e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.39 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV-----VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEI-----KVKGKLIDEYDLI 73
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 74 ELRRGIGYVIQqiglLPHL-----TVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVA 148
Cdd:PRK13645 87 RLRKEIGLVFQ----FPEYqlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 149 RALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-240 |
3.44e-25 |
|
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: 105.15 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAY----SENVVLDKFSLAIEQGEFLVLLGPSGCGKT----TILKminglLIPD-----SGEIKVKGKLI 67
Cdd:COG4172 4 MPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILR-----LLPDpaahpSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 68 DEYDLIELR--RG--IGYVIQQ--IGLLPHLTVEDNICFVLDL---LKKPEPEKKSVakELIKLVGMD--EGMLRRYPKE 136
Cdd:COG4172 79 LGLSERELRriRGnrIAMIFQEpmTSLNPLHTIGKQIAEVLRLhrgLSGAAARARAL--ELLERVGIPdpERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 137 LSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIeeAI--KLGTRIVLLNDG- 213
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL--GVvrRFADRVAVMRQGe 234
|
250 260
....*....|....*....|....*..
gi 503125592 214 VIERNEKKRdfVLLDDRSEYAKKFFES 240
Cdd:COG4172 235 IVEQGPTAE--LFAAPQHPYTRKLLAA 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
4.97e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 4.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVkGKLIDeydlielrrgIGYV 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQ-QIGLLPHLTVEDNICFVLDLLKKpepekksvakelIKLVGMDEGML------RRYPKELSGGQQQRVGVARALAANP 155
Cdd:COG0488 384 DQhQEELDPDKTVLDELRDGAPGGTE------------QEVRGYLGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKihskLKKTIIFVTHD---IEeaiKLGTRIVLLNDGVIE 216
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDD----FPGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
7.32e-25 |
|
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: 97.52 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLideydlielrrGIGYVI 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QqigllphltvednicfvldllkkpepekksvakeliklvgmdegmlrrypkeLSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03221 70 Q----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503125592 164 FGAVDEITRRNLQDELikihSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03221 98 TNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-195 |
7.75e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.80 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY---SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIG 80
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YViQQIGLLPHLTVEDNICFVLDllKKPEPEKKSVAKEliklVGMDE---GMLRRYPKE-------LSGGQQQRVGVARA 150
Cdd:TIGR00958 559 LV-GQEPVLFSGSVRENIAYGLT--DTPDEEIMAAAKA----ANAHDfimEFPNGYDTEvgekgsqLSGGQKQRIAIARA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503125592 151 LAANPEIILMDEPFGAVDEITRRNLQDElikiHSKLKKTIIFVTH 195
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQES----RSRASRTVLLIAH 672
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-236 |
9.58e-25 |
|
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: 99.75 E-value: 9.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLipDSGEIKVKGK-LIDEYDLIELR---RGIGYVIQ--QIGLLPHLTVED 96
Cdd:TIGR02770 6 NLSLKRGEVLALVGESGSGKSLTCLAILGLL--PPGLTQTSGEiLLDGRPLLPLSirgRHIATIMQnpRTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 97 NICFVLDLLKKPEPEKKSVAKELIKLVGMDEG--MLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRN 174
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDPeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 175 LQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKRDFVllDDRSEYAKK 236
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGrIVERGTVKEIFY--NPKHETTRK 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-213 |
1.22e-24 |
|
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: 97.89 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIGYVI---QQIGLLPHLT 93
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNIcfvldllkkpepekksvakeliklvgmdegMLRRYpkeLSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRR 173
Cdd:cd03215 95 VAENI------------------------------ALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503125592 174 NLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-215 |
1.82e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.78 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 6 FNDVSKaysENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID---EYDLIELRRGIGYV 82
Cdd:PRK10261 330 LNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQ--IGLLPHLTVEDNICFVLDL--LKKPEPEKKSVAkELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEII 158
Cdd:PRK10261 407 FQDpyASLDPRQTVGDSIMEPLRVhgLLPGKAAAARVA-WLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-197 |
1.92e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.94 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 20 DKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI---DEYDLIELRRGIGYVIQQ--IGLLPHLTV 94
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 95 EDNICFVLDLL--KKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEitr 172
Cdd:PRK15079 118 GEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV--- 194
|
170 180
....*....|....*....|....*....
gi 503125592 173 rNLQDELIKIHSKLKK----TIIFVTHDI 197
Cdd:PRK15079 195 -SIQAQVVNLLQQLQRemglSLIFIAHDL 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-215 |
2.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.68 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGklIDEYD---LIELRRG 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDfskLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQ-----IGllphLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:PRK13644 79 VGIVFQNpetqfVG----RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEaIKLGTRIVLLNDGVI 215
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-237 |
2.77e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 103.28 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQigllPHL---TVEDNIcfVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKEL-------SGGQQQRVGVARALA 152
Cdd:TIGR01193 554 PQE----PYIfsgSILENL--LLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELseegssiSGGQKQRIALARALL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKlkkTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRdfvLLDDRSE 232
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE---LLDRNGF 701
|
....*
gi 503125592 233 YAKKF 237
Cdd:TIGR01193 702 YASLI 706
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-217 |
2.81e-24 |
|
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: 103.10 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS--ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:TIGR03796 478 VELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHlTVEDNICFVLDLLkkPEPEKKSVAK------ELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:TIGR03796 558 VDQDIFLFEG-TVRDNLTLWDPTI--PDADLVRACKdaaihdVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELikihSKLKKTIIFVTHDIeEAIKLGTRIVLLNDG-VIER 217
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRL-STIRDCDEIIVLERGkVVQR 692
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-215 |
6.60e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENV-----VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI----DEYDLI 73
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 74 ELRRGIGYVIQ-QIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALA 152
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDELIKIHsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-224 |
1.83e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.13 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRR-GIGY 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNICFvlDLLKKPEPEKKsvAKELIKLVG------MDEGMLrrypkELSggQQQRVGVARALAANP 155
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILF--GLPKRQASMQK--MKQLLAALGcqldldSSAGSL-----EVA--DRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 156 EIILMDEPFGAVDEITRRNLqdeLIKIHSKLKKT--IIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDF 224
Cdd:PRK15439 160 RILILDEPTASLTPAETERL---FSRIRELLAQGvgIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-249 |
2.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQI-GLLPHLTVEDN 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 98 ICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQD 177
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 178 ELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKRDFVLLDDRSEYAKKFFESKDFMAYLNT 249
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLRK 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-224 |
3.30e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGK-TTILKMINglLIPDSGEIKVKGKLIDEYD---LIELRRGIGYVIQ--QIGL 88
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLR--LINSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 89 LPHLTVEDNICFVLDL----LKKPEPEKKSVakELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqptLSAAQREQQVI--AVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 165 GAVDeitrRNLQDELIKIHSKLKKT----IIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKRDF 224
Cdd:PRK15134 454 SSLD----KTVQAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQVIVLRQGeVVEQGDCERVF 514
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-235 |
4.40e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 95.67 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVK---GKLIDEYDLIE---- 74
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsGAELELYQLSEaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 75 --LRRGIGYVIQQI--GLLPHLTVEDNIC-FVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVAR 149
Cdd:TIGR02323 82 rlMRTEWGFVHQNPrdGLRMRVSAGANIGeRLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 150 ALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKkrDFVLLD 228
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGrVVESGLT--DQVLDD 239
|
....*..
gi 503125592 229 DRSEYAK 235
Cdd:TIGR02323 240 PQHPYTQ 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-215 |
4.57e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 95.23 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAY---SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGI 79
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQigllPHL---TVEDNICFVL---DLLKKPEPEKKSVAKELIKLV--GMDEGMLRRyPKELSGGQQQRVGVARAL 151
Cdd:cd03248 91 SLVGQE----PVLfarSLQDNIAYGLqscSFECVKEAAQKAHAHSFISELasGYDTEVGEK-GSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIeEAIKLGTRIVLLNDGVI 215
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-168 |
5.00e-23 |
|
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: 94.35 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLiELRRGIGYVIQQIGLLPHLTV 94
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 95 EDNICFVLDLLKkpePEKKSVaKELIKLVGMDeGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVD 168
Cdd:TIGR01189 91 LENLHFWAAIHG---GAQRTI-EDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-215 |
7.02e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIGYVI---QQIGLLPHLT 93
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICF-VLDLLKK----PEPEKKSVAKELIKLVGMdegmlrRYP------KELSGGQQQRVGVARALAANPEIILMDE 162
Cdd:COG1129 347 IRENITLaSLDRLSRggllDRRRERALAEEYIKRLRI------KTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 163 PF-----GAVDEITR--RNLQDElikihsklKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG1129 421 PTrgidvGAKAEIYRliRELAAE--------GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-215 |
8.85e-23 |
|
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: 94.26 E-value: 8.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLIDEYdliELRRGIGYVIQQIGLLPHLTVEDNIC 99
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 100 FVLdLLKKPEPEKKSVAKELIKLVGMDEGMLRR----YPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNl 175
Cdd:cd03234 104 YTA-ILRLPRKSSDAIRKKRVEDVLLRDLALTRiggnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503125592 176 qdeLIKIHSKL---KKTIIFVTHDI-EEAIKLGTRIVLLNDGVI 215
Cdd:cd03234 182 ---LVSTLSQLarrNRIVILTIHQPrSDLFRLFDRILLLSSGEI 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-197 |
9.95e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.80 E-value: 9.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLideydlielrrGIGYV 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-----------RIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGL---LPhLTVEDnicFvldLLKKPEPEKKSVakeLIKLVGMDEGMLRRYP-KELSGGQQQRVGVARALAANPEII 158
Cdd:PRK09544 73 PQKLYLdttLP-LTVNR---F---LRLRPGTKKEDI---LPALKRVQAGHLIDAPmQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDI 197
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-235 |
1.55e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.78 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIgllpHL---TVEDNICFVL-DLLKKPEPEKK---SVAKELIKlvGMDEG---MLRRYPKELSGGQQQRVGVARAL 151
Cdd:PRK11176 422 VSQNV----HLfndTIANNIAYARtEQYSREQIEEAarmAYAMDFIN--KMDNGldtVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQ---DELIKihsklKKTIIFVTH---DIEEAiklgTRIVLLNDG-VIERNEKKrdf 224
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQaalDELQK-----NRTSLVIAHrlsTIEKA----DEILVVEDGeIVERGTHA--- 563
|
250
....*....|.
gi 503125592 225 VLLDDRSEYAK 235
Cdd:PRK11176 564 ELLAQNGVYAQ 574
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-274 |
2.19e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.18 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPDSGEI--------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 61 ---KVKGKL----IDEYDLIE-----LRRGIGYVIQQ-IGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDE 127
Cdd:TIGR03269 81 pcpVCGGTLepeeVDFWNLSDklrrrIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 128 GMLRrYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRI 207
Cdd:TIGR03269 161 RITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 208 VLLNDGVIernekkrdfVLLDDRSEYAKKFFESKDFMAYLNTIKIKDLVIKQSDISFDLYD-SRSLVK 274
Cdd:TIGR03269 240 IWLENGEI---------KEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISvDRGVVK 298
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-214 |
1.55e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 91.53 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 22 FSLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLPHLTVednicF- 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV-----Fq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 101 VLDL---LKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARAL-----AANPE--IILMDEPFGAVDeI 170
Cdd:PRK03695 89 YLTLhqpDKTRTEAVASALNEVAEALGLDD-KLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLD-V 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503125592 171 TRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGV 214
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-215 |
1.90e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 12 AYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLPH 91
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 92 LTVEDNICF----VLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAV 167
Cdd:PRK10253 96 ITVQELVARgrypHQPLFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503125592 168 DEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-213 |
3.35e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.44 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG---KLIDEYDLIElrR 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemRFASTTAALA--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNICF--------VLDllkkpEPEKKSVAKELIKLVGMD---EGMLrrypKELSGGQQQRVG 146
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLgqlphkggIVN-----RRLLNYEAREQLEHLGVDidpDTPL----KYLSIGQRQMVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 147 VARALAANPEIILMDEPFGAVD--EITRrnlqdeLIKIHSKLK---KTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSarEIEQ------LFRVIRELRaegRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-213 |
3.35e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD-LIELRRGIGYV 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIGLLPHLTVEDNIcFVLDLLKKP--------EPEKKSVAKELIKLVGmdegmLRRYPKE----LSGGQQQRVGVARA 150
Cdd:PRK09700 86 YQELSVIDELTVLENL-YIGRHLTKKvcgvniidWREMRVRAAMMLLRVG-----LKVDLDEkvanLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 151 LAANPEIILMDEPfgaVDEITRRNLqDELIKIHSKLK---KTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK09700 160 LMLDAKVIIMDEP---TSSLTNKEV-DYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-198 |
3.40e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENV-VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID--EYDLIELRRGI 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQI-GLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgmLRRYPKE-LSGGQQQRVGVARALAANPEI 157
Cdd:PRK13636 85 GMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--LKDKPTHcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIE 198
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDID 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-215 |
4.75e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQiGLLPHLTVEDNIcfvl 102
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQN-PQLPHGTLRDNV---- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 103 dLLKKPEPE--------KKSVAKELIKLV--GMD----EGMLRrypkeLSGGQQQRVGVARALAANPEIILMDEPFGAVD 168
Cdd:PRK11174 444 -LLGNPDASdeqlqqalENAWVSEFLPLLpqGLDtpigDQAAG-----LSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503125592 169 EITRRNLQDELIKIHSklKKTIIFVTHDIEEaIKLGTRIVLLNDGVI 215
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVMQDGQI 561
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-195 |
2.16e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 86.05 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVS-KAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKvkgklideydlIELRRGIGYV 82
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQiGLLPHLTVEDNICfvldllkkpepekksvakeliklvgmdegmlrrYP--KELSGGQQQRVGVARALAANPEIILM 160
Cdd:cd03223 70 PQR-PYLPLGTLREQLI---------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*...
gi 503125592 161 DEPFGAVDEitrrnlqDELIKIHSKLKK---TIIFVTH 195
Cdd:cd03223 116 DEATSALDE-------ESEDRLYQLLKElgiTVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-168 |
2.51e-20 |
|
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: 87.16 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDlIELRRGIGYVIQQIGLLPHLTV 94
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 95 EDNICFVLDLlkkpepekKSVAKELIKLVGMDEGMLRRYP-KELSGGQQQRVGVARALAANPEIILMDEPFGAVD 168
Cdd:cd03231 91 LENLRFWHAD--------HSDEQVEEALARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-214 |
2.66e-19 |
|
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: 88.81 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrrgIGYVIQQIGLLPHlTVEDN 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 98 ICFVLDLlkkPEPEKKSVAK------ELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEIT 171
Cdd:TIGR01271 507 IIFGLSY---DEYRYTSVIKacqleeDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503125592 172 RRNLQDE-LIKIHSklKKTIIFVTHDIEEaIKLGTRIVLLNDGV 214
Cdd:TIGR01271 584 EKEIFEScLCKLMS--NKTRILVTSKLEH-LKKADKILLLHEGV 624
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
2.73e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGI 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNIC---FVLDllkkpepeKKSVAKELIKLVGMDEGMLRRYPKE---LSGGQQQRVGVARALAA 153
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAmggFFAE--------RDQFQERIKWVYELFPRLHERRIQRagtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-168 |
2.83e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDlIELRRGIGYVIQQIGLLPHLTV 94
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 95 EDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRypkeLSGGQQQRVGVARALAANPEIILMDEPFGAVD 168
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-195 |
3.18e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 83.85 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEyDLIELRRGIGYVIQQIGLLPHL 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNICFVLDLlkkpepekKSVAKELIKLVGMDE-GMLRRYP-KELSGGQQQRVGVARALAANPEIILMDEPFGAVDEI 170
Cdd:PRK13540 90 TLRENCLYDIHF--------SPGAVGITELCRLFSlEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 503125592 171 TRRNLQDElIKIHSKLKKTIIFVTH 195
Cdd:PRK13540 162 SLLTIITK-IQEHRAKGGAVLLTSH 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-197 |
3.72e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE---LRRGIGYVIQQ--IGLLPHLT 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNpyGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDnicfvldLLKKP--------EPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFG 165
Cdd:PRK11308 111 VGQ-------ILEEPllintslsAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 503125592 166 AVDEITR-------RNLQDElikihskLKKTIIFVTHDI 197
Cdd:PRK11308 184 ALDVSVQaqvlnlmMDLQQE-------LGLSYVFISHDL 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-215 |
3.80e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.89 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLPHLTVedni 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPV---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 cF-VLDLLKKPEPEKKSVAKELIKLVG----MDEgmLRRYPKELSGGQQQRVGVARAL-----AANPE--IILMDEPFGA 166
Cdd:COG4138 87 -FqYLALHQPAGASSEAVEQLLAQLAEalglEDK--LSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 167 VDeITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG4138 164 LD-VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-200 |
4.01e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 20 DKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDlIELRRGIGYVIQQIGLLPHLTVEDNic 99
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IATRRRVGYMSQAFSLYGELTVRQN-- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 100 fvLDL------LkkpePEKKSVAKeliklvgMDEgMLRRY---------PKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:NF033858 360 --LELharlfhL----PAAEIAAR-------VAE-MLERFdladvadalPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190
....*....|....*....|....*....|....*..
gi 503125592 165 GAVDEITRRNLQDELIKIhSKLKKTIIFV-THDIEEA 200
Cdd:NF033858 426 SGVDPVARDMFWRLLIEL-SREDGVTIFIsTHFMNEA 461
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-216 |
4.98e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.59 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVK---GKLIDEYDLIE------LRR 77
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrdGQLRDLYALSEaerrrlLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQI--GLLPHLTVEDNIcfvldllkkPEP----------EKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRV 145
Cdd:PRK11701 90 EWGFVHQHPrdGLRMQVSAGGNI---------GERlmavgarhygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 146 GVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIE 216
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVE 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-217 |
6.62e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY--SENVVLDkFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:PRK13657 335 VEFDDVSFSYdnSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLpHLTVEDNIcfvldLLKKP--------EPEKKSVAKELI--KLVGMDEGMLRRyPKELSGGQQQRVGVARAL 151
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNI-----RVGRPdatdeemrAAAERAQAHDFIerKPDGYDTVVGER-GRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQDELIKIhSKLKKTIIfVTH---DIEEAiklgTRIVLLNDG-VIER 217
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAHrlsTVRNA----DRILVFDNGrVVES 550
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-217 |
8.48e-19 |
|
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: 86.80 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY-SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQIgLLPHLTVEDNICFvldllKKP---EPEKKSVAK-----ELIK--------LVGmdEGMLRrypkeLSGGQQQRVG 146
Cdd:COG5265 438 PQDT-VLFNDTIAYNIAY-----GRPdasEEEVEAAARaaqihDFIEslpdgydtRVG--ERGLK-----LSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 147 VARALAANPEIILMDEPFGAVDEITRRNLQDELIKIhSKLKKTIIfVTHdieeaiKLGT-----RIVLLNDG-VIER 217
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLV-IAH------RLSTivdadEILVLEAGrIVER 573
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-210 |
1.16e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.96 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLlIPDSGEIKVKGKLIDEYDLIEL---------RRGIGYVIQ--QI 86
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADRFRWNGIDLLKLsprerrkiiGREIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLLPHLTVEDNICFVLdllkkPEPE-----------KKSVAKELIKLVG--MDEGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:COG4170 101 CLDPSAKIGDQLIEAI-----PSWTfkgkwwqrfkwRKKRAIELLHRVGikDHKDIMNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 154 NPEIILMDEPFGAVDEITrrnlQDELIKIHSKLKK----TIIFVTHDIEEAIKLGTRIVLL 210
Cdd:COG4170 176 QPRLLIADEPTNAMESTT----QAQIFRLLARLNQlqgtSILLISHDLESISQWADTITVL 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-216 |
1.41e-18 |
|
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: 86.61 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYS--ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIdEYDLIELRRGIG 80
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 161 DEPFGAVDEITRRNLQDELIKIhSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVIE 216
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-201 |
2.13e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 15 ENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLL--IPDSGEIKVKGKLIDEydlielrrgigyviqqigllpHL 92
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR---------------------EA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNICFVLDllkkpepekKSVAKELIKLVGMDEGML-RRYPKELSGGQQQRVGVARALAANPEIILMDEpFGAV-DEI 170
Cdd:COG2401 101 SLIDAIGRKGD---------FKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCSHlDRQ 170
|
170 180 190
....*....|....*....|....*....|...
gi 503125592 171 TRRNLQDELIKIHSKLKKTIIFVTH--DIEEAI 201
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHhyDVIDDL 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-224 |
2.35e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAY----SENVVLDKFSLAIEQGEFLVLLGPSGCGKT-TILKMINGLLIPD----SGEIKVKGKLIDEYD 71
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 72 LIELR--RG--IGYVIQQ--IGLLPHLTVEDNICFVLDLLK--KPEPEKKSVAKELIKlVGMDE--GMLRRYPKELSGGQ 141
Cdd:PRK15134 83 EQTLRgvRGnkIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRgmRREAARGEILNCLDR-VGIRQaaKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 142 QQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEK 220
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGrCVEQNRA 241
|
....
gi 503125592 221 KRDF 224
Cdd:PRK15134 242 ATLF 245
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-213 |
2.42e-18 |
|
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: 83.37 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrrgIGYVIQQIGLLPHlTVEDN 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 98 ICFVLDLlkkPEPEKKSVAK------ELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEIT 171
Cdd:cd03291 118 IIFGVSY---DEYRYKSVVKacqleeDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503125592 172 RRNLQDELIkihSKL--KKTIIFVTHDIEEaIKLGTRIVLLNDG 213
Cdd:cd03291 195 EKEIFESCV---CKLmaNKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-215 |
3.00e-18 |
|
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: 81.77 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSEN--VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGy 81
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIgllPHL---TVEDNicfvLDLLKKPEPE------KKSVAKELIK-LVGMDEGMLRRYPKELSGGQQQRVGVARAL 151
Cdd:cd03244 82 IIPQD---PVLfsgTIRSN----LDPFGEYSDEelwqalERVGLKEFVEsLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 152 AANPEIILMDEPFGAVDEITrrnlqDELIK--IHSKLK-KTIIFVTHDIEEAIKLGtRIVLLNDGVI 215
Cdd:cd03244 155 LRKSKILVLDEATASVDPET-----DALIQktIREAFKdCTVLTIAHRLDTIIDSD-RILVLDKGRV 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-243 |
6.37e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.16 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDS--GEIKVKGKLIDEydliELRRGIGYVIQQ 85
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 86 IGLLPHLTVEDNICFVlDLLKKPEP----EKKSVAKELIKLVGMDEG----MLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:PLN03211 149 DILYPHLTVRETLVFC-SLLRLPKSltkqEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 158 ILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTHdieeaiKLGTRIVLLNDGVIERNEKKrdfVLLDDRSEYAKKF 237
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH------QPSSRVYQMFDSVLVLSEGR---CLFFGKGSDAMAY 297
|
....*.
gi 503125592 238 FESKDF 243
Cdd:PLN03211 298 FESVGF 303
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-213 |
8.56e-18 |
|
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: 80.45 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIEL----RRGIGYVIQQIGLLpHLTV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 95 EDNICFVLDLLK---KPEPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVD-EI 170
Cdd:cd03290 96 EENITFGSPFNKqryKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503125592 171 TRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKlGTRIVLLNDG 213
Cdd:cd03290 176 SDHLMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-208 |
8.99e-18 |
|
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: 80.92 E-value: 8.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEF-----LVLLGPSGCGKTTILKMINGLLIPDSGEIKVkgklideydlieLRRGIGYVIQQIGLLPHLT 93
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------------ELDTVSYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEdnicfvlDLLKKPEPEKKSVAK---ELIKLVGMDEGMLRRYPkELSGGQQQRVGVARALAANPEIILMDEPFGAVDeI 170
Cdd:cd03237 78 VR-------DLLSSITKDFYTHPYfktEIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-V 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 503125592 171 TRRNLQDELIK-IHSKLKKTIIFVTHDIEEAIKLGTRIV 208
Cdd:cd03237 149 EQRLMASKVIRrFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-213 |
9.03e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.19 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 20 DKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIEL-RRGIGYVIQQIGLLPHLTVEDNI 98
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 C----------FVLDLLKKP-----EPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:PRK11300 102 LvaqhqqlktgLFSGLLKTPafrraESEALDRAATWLERVGLLE-HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-195 |
1.40e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVS-KAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKV--KGKLIdeydlielrrgig 80
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVL------------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIgLLPHLTVEDNICFvldllkkPEPEKK---SVAKELIKLVGMDE--GML---RRYPKELSGGQQQRVGVARALA 152
Cdd:COG4178 430 FLPQRP-YLPLGTLREALLY-------PATAEAfsdAELREALEAVGLGHlaERLdeeADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503125592 153 ANPEIILMDEPFGAVDEITRRN----LQDELIKIhsklkkTIIFVTH 195
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAAlyqlLREELPGT------TVISVGH 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-213 |
5.21e-17 |
|
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: 78.22 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHlTVEDNIcfvldllkkpEPEKKSVAKELIKLVGMDEGMLrrypkELSGGQQQRVGVARALAANPEIILMD 161
Cdd:cd03369 87 IPQDPTLFSG-TIRSNL----------DPFDEYSDEEIYGALRVSEGGL-----NLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 162 EPFGAVDEITrrnlqDELIK--IHSKLKK-TIIFVTHDIEEAIKLgTRIVLLNDG 213
Cdd:cd03369 151 EATASIDYAT-----DALIQktIREEFTNsTILTIAHRLRTIIDY-DKILVMDAG 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-210 |
1.23e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.20 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 12 AYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydlIELRRGIGYVIQQIGLL 89
Cdd:PRK13543 18 AFSRNEepVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 90 PHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRrypkELSGGQQQRVGVARALAANPEIILMDEPFGAVDe 169
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503125592 170 ITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLL 210
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-213 |
1.84e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID--EYDLIELRRGIGYVI----QQI 86
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFqdpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GllpHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVgmDEGMLRRYPKE-LSGGQQQRVGVARALAANPEIILMDEPFG 165
Cdd:PRK13638 91 F---YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503125592 166 AVDEITRRNLQDELIKIHSKLKKTIIfVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-217 |
1.90e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY-SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYV 82
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 iQQIGLLPHLTVEDNICFVLDLlkkpEPEKKSVAKELIKLV----GMDEGMLRRYPKE---LSGGQQQRVGVARALAANP 155
Cdd:PRK10790 421 -QQDPVVLADTFLANVTLGRDI----SEEQVWQALETVQLAelarSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIEEAIKLGTRIVLLNDGVIER 217
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-179 |
2.36e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.21 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVkGKLIDeydlielrrgIGYV 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQ-IGLLPHLTVEDNICFVLDLLKKPEPEKKSVA---------KELIKLVGmdegmlrrypkELSGGQQQRVGVARALA 152
Cdd:TIGR03719 391 DQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG-----------QLSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....*..
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDEL 179
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-215 |
2.42e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD-LIELRRGIGYVI---QQIGLLPHLTVEDNI 98
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrQSSGLYLDAPLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFV----LDLLKKPEPEKKSVAKEL----IKLVGMDEGMlrrypKELSGGQQQRVGVARALAANPEIILMDEPFGAVDeI 170
Cdd:PRK15439 363 CALthnrRGFWIKPARENAVLERYRralnIKFNHAEQAA-----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-V 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503125592 171 TRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-215 |
3.83e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.78 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrRGIGYVI 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-----------ANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQigllpHLTVEDNICFVLDLL---KKPEPEKKSVAKELIKLV-GMDEgmLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:PRK15064 389 QD-----HAYDFENDLTLFDWMsqwRQEGDDEQAVRGTLGRLLfSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 160 MDEPFGAVDEITRRNLQDELikihSKLKKTIIFVTHDIEEAIKLGTRIV-LLNDGVI 215
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIeITPDGVV 514
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-217 |
5.09e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYdliELRRG-IGYVIQQIGLL-----PHLTVED 96
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-----LIDDH---PLHFGdYSYRSQRIRMIfqdpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 97 NICFVLDL-------LKKPEPEKKsvAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDE 169
Cdd:PRK15112 105 RISQILDFplrlntdLEPEQREKQ--IIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 170 ITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIER 217
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGeVVER 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-213 |
5.81e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 78.23 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 8 DVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIGYVIQQI 86
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLvgMDEGMLRRYPKE----LSGGQQQRVGVARALAANPEIILMDE 162
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAI--FDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503125592 163 PFGAVDEitrrNLQDELIKIHSKLKKT---IIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10982 161 PTSSLTE----KEVNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDG 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-197 |
6.73e-16 |
|
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: 77.90 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEnvvldkFSLAIE-----QGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrr 77
Cdd:COG1245 341 LVEYPDLTKSYGG------FSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK------------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 gIGYVIQQIGLLPHLTVEdnicfvlDLLKKPEPEKKSVAK---ELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAAN 154
Cdd:COG1245 403 -ISYKPQYISPDYDGTVE-------EFLRSANTDDFGSSYyktEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503125592 155 PEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDI 197
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-215 |
8.30e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.68 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLI----------DE- 69
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqqdpprNVe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 70 ---YDLI-ELRRGIGYVIQQIGLLPHLTVED----------NICFVLDLLKKPEPEKKsvAKELIKLVGMD-EGMLrryp 134
Cdd:PRK11147 81 gtvYDFVaEGIEEQAEYLKRYHDISHLVETDpseknlnelaKLQEQLDHHNLWQLENR--INEVLAQLGLDpDAAL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 135 KELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIkihsKLKKTIIFVTHDIEEAIKLGTRIVLLNDGV 214
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
.
gi 503125592 215 I 215
Cdd:PRK11147 231 L 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-254 |
8.41e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.09 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 14 SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDsgeikvkgklidEYDLIELRRGIGYViQQIGLLPHLT 93
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA------------ETSSVVIRGSVAYV-PQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICFVLDLlkkpEPEK-------KSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGA 166
Cdd:PLN03232 695 VRENILFGSDF----ESERywraidvTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 167 VDEITRRNLQDELIKiHSKLKKTIIFVTHDIeEAIKLGTRIVLLNDGVIernEKKRDFVLLDDRSEYAKKFFESKDFMAY 246
Cdd:PLN03232 771 LDAHVAHQVFDSCMK-DELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI---KEEGTFAELSKSGSLFKKLMENAGKMDA 845
|
....*...
gi 503125592 247 LNTIKIKD 254
Cdd:PLN03232 846 TQEVNTND 853
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-215 |
8.93e-16 |
|
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: 78.06 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 12 AYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILkmiNGLLipdsGEI-KVKGKlideydlIELRRGIGYVIQQiGLLP 90
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL---SALL----AEMdKVEGH-------VHMKGSVAYVPQQ-AWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 91 HLTVEDNICFVLDLlkkPEPEKKSVAK------ELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:TIGR00957 712 NDSLRENILFGKAL---NEKYYQQVLEacallpDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 165 GAVDEITRRNLQDELIKIHSKLK-KTIIFVTHDIEEAIKLGTrIVLLNDGVI 215
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVLKnKTRILVTHGISYLPQVDV-IIVMSGGKI 839
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-215 |
1.19e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 17 VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRR-GIGYVI---QQIGLLPHL 92
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlGVAYIPedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNIcfVLDLLKKPEPEK---------KSVAKELIKlvgmdegmlrRY----------PKELSGGQQQRVGVARALAA 153
Cdd:COG3845 352 SVAENL--ILGRYRRPPFSRggfldrkaiRAFAEELIE----------EFdvrtpgpdtpARSLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 154 NPEIILMDEP-----FGAVDEitrrnlqdelikIHSKLK------KTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:COG3845 420 DPKLLIAAQPtrgldVGAIEF------------IHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-215 |
1.20e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 16 NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLL--------IPDSGEIKVKGK---LIDEYDLIELR-------- 76
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEplaAIDAPRLARLRavlpqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIGLL---PH------LTVEDnicfvldllkkpepekKSVAKELIKLVGMDeGMLRRYPKELSGGQQQRVGV 147
Cdd:PRK13547 94 PAFAFSAREIVLLgryPHarragaLTHRD----------------GEIAWQALALAGAT-ALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 148 ARALA---------ANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-197 |
1.33e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSE-NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEydliELRRG-IGY 81
Cdd:PRK15056 7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGL---LPHLtVEDNICF----VLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAAN 154
Cdd:PRK15056 83 VPQSEEVdwsFPVL-VEDVVMMgrygHMGWLRRAKKRDRQIVTAALARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503125592 155 PEIILMDEPFGAVDEITR-------RNLQDElikihsklKKTIIFVTHDI 197
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEariisllRELRDE--------GKTMLVSTHNL 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-217 |
1.69e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.06 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 14 SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGyVIQQIGLLPHLT 93
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA-VVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICfvldlLKKPEPEKKSVaKELIKLVGMDEGMLRR---YPKE-------LSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:PRK10789 405 VANNIA-----LGRPDATQQEI-EHVARLASVHDDILRLpqgYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 164 FGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIeEAIKLGTRIVLLNDG-VIER 217
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGE--GRTVIISAHRL-SALTEASEILVMQHGhIAQR 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-197 |
1.94e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEnvvldkFSLAIE-----QGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrr 77
Cdd:PRK13409 340 LVEYPDLTKKLGD------FSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK------------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 gIGYVIQQIGLLPHLTVEdnicfvlDLLKKPEPEKKS--VAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:PRK13409 402 -ISYKPQYIKPDYDGTVE-------DLLRSITDDLGSsyYKSEIIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDI 197
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-225 |
3.15e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.16 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENvvldKFS-----LAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRG 78
Cdd:PRK10522 323 LELRNVTFAYQDN----GFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNicfvldllkkPEPEKKSVAKELIKL-----VGMDEGMLRRYpkELSGGQQQRVGVARALAA 153
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPEG----------KPANPALVEKWLERLkmahkLELEDGRISNL--KLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDiEEAIKLGTRIVLLNDGVI------ERNEKKRDFV 225
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLseltgeERDAASRDAV 543
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-213 |
3.53e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQI 86
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLLPHLTVEDNICF-------VLDLLKKPEPEKksvAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVARALAANPEIIL 159
Cdd:PRK10575 95 PAAEGMTVRELVAIgrypwhgALGRFGAADREK---VEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 160 MDEPFGAVDeITRrnlQDELIKIHSKLKK----TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10575 171 LDEPTSALD-IAH---QVDVLALVHRLSQerglTVIAVLHDINMAARYCDYLVALRGG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-195 |
4.72e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.18 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGllIPD----SGEIKVKGKlideyDLIEL------RRGIGYVIQQIG 87
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGE-----DILELspderaRAGIFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 88 LLPHLTVED---NICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKE-LSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:COG0396 88 EIPGVSVSNflrTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190
....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKlKKTIIFVTH 195
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSP-DRGILIITH 198
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-197 |
5.47e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.38 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 22 FSLAieQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLI---DEYDLIELR-RGIGYVIQQ--IGLLPHL 92
Cdd:PRK09473 37 FSLR--AGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlPEKELNKLRaEQISMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNICFVLDLLK---KPEPEKKSVakELIKLVGMDEGM--LRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAV 167
Cdd:PRK09473 115 RVGEQLMEVLMLHKgmsKAEAFEESV--RMLDAVKMPEARkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190
....*....|....*....|....*....|....
gi 503125592 168 DeITrrnLQDELIKIHSKLKK----TIIFVTHDI 197
Cdd:PRK09473 193 D-VT---VQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
50-212 |
5.82e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 50 NGLLIPDSGEIKVKGKLIDEYDLIELRRgIGYVIQQIGLLPHLTVEDNICFvldllKKPEPEKKSVaKELIKLVGMDEGM 129
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDICDYNLKDLRN-LFSIVSQEPMLFNMSIYENIKF-----GKEDATREDV-KRACKFAAIDEFI 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 130 ----------LRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIeE 199
Cdd:PTZ00265 1342 eslpnkydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-A 1420
|
170
....*....|...
gi 503125592 200 AIKLGTRIVLLND 212
Cdd:PTZ00265 1421 SIKRSDKIVVFNN 1433
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-216 |
5.98e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVV----LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLlIPDSGEIKVKGKLIDEYDLIEL- 75
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKLEFNGQDLQRIs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 ----RRGIGYVIQQI------GLLPHLTVEDNIcfvLDLLKKPE----PEKKSVAKELIKLVGMD--EGMLRRYPKELSG 139
Cdd:PRK11022 80 ekerRNLVGAEVAMIfqdpmtSLNPCYTVGFQI---MEAIKVHQggnkKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503125592 140 GQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG-VIE 216
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGqVVE 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-213 |
6.07e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD--LIELR----------RG--IGYVIQQ--I 86
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSeqsaaqmrhvRGadMAMIFQEpmT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 GLLPHLTVEDNICFVLDLLKKPEPEKKSV-AKELIKLVGMDEG--MLRRYPKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:PRK10261 116 SLNPVFTVGEQIAESIRLHQGASREEAMVeAKRMLDQVRIPEAqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEP 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVD-EITRRNLQdeLIKI-HSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10261 196 TTALDvTIQAQILQ--LIKVlQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-213 |
6.12e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPD---SGEIKVKGKLIDEYDLIEL-RRG 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLTVEDNIcFVLDLLKKP-----EPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENI-FLGNEITLPggrmaYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDeLIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLD-IIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-179 |
3.18e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVkGKLIDeydlielrrgIGYV 82
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQ-IGLLPHLTVEDNICFVLDLLKKPEPEKKSVA---------KELIKLVGMdegmlrrypkeLSGGQQQRVGVARALA 152
Cdd:PRK11819 393 DQSrDALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVGV-----------LSGGERNRLHLAKTLK 461
|
170 180
....*....|....*....|....*..
gi 503125592 153 ANPEIILMDEPFGAVDEITRRNLQDEL 179
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVETLRALEEAL 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
7.56e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 1 MAIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPD---SGEIKVKGKLIDEYDLIEL-R 76
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGYVIQQIGLLPHLTVEDNIcFVLDllkkpEPEKKSV---------AKELIKLVGMDEGMLRRYpKELSGGQQQRVGV 147
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENI-FLGN-----EITPGGImdydamylrAQKLLAQLKLDINPATPV-GNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 148 ARALAANPEIILMDEPFGAVDEITRRNLQDelikIHSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLD----IIRDLKAhgiACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-213 |
1.02e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.83 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLIDEYDLIeLRRGIGYVIQQIGLLPHLTVE 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK-YPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 96 DNICFVLDLLKKpepekksvakeliklvgmdegmlrRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNL 175
Cdd:cd03233 102 ETLDFALRCKGN------------------------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 503125592 176 QDELIKIHSKLKKTIIF-VTHDIEEAIKLGTRIVLLNDG 213
Cdd:cd03233 158 LKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEG 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-213 |
1.19e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 25 AIEQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLIdeyDLIELRRGIGYVIQQIGLLPHLTVEDNICFV 101
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 102 LDL-LKK--PEPEKKSVAKELIKLVGM---------DEGMLrrypKELSGGQQQRVGVARALAANPEIILMDEPFGAVDE 169
Cdd:TIGR00955 124 AHLrMPRrvTKKEKRERVDEVLQALGLrkcantrigVPGRV----KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503125592 170 ITRRNLQDELIKIHSKlKKTIIFVTHD-IEEAIKLGTRIVLLNDG 213
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEG 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-213 |
1.34e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 2 AIIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRR-GIG 80
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEaGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNIC----FVLDLLKKPEPEKKSVAKELIKLVGMDEGMlRRYPKELSGGQQQRVGVARALAANPE 156
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 157 IILMDEPfgaVDEITRRNLQdELIKIHSKLKKT---IIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10762 162 VIIMDEP---TDALTDTETE-SLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-210 |
1.93e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLlIPDSGEIKVKGKLIDEYDLIEL-----RRGIGYVIQQIGLLPH- 91
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLsprerRKLVGHNVSMIFQEPQs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 92 -LTVEDNICfvlDLLKKPEPE-------------KKSVAKELIKLVGMDE--GMLRRYPKELSGGQQQRVGVARALAANP 155
Cdd:PRK15093 101 cLDPSERVG---RQLMQNIPGwtykgrwwqrfgwRKRRAIELLHRVGIKDhkDAMRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 156 EIILMDEPFGAVDEITrrnlQDELIKIHSKLKK----TIIFVTHDIEEAIKLGTRIVLL 210
Cdd:PRK15093 178 RLLIADEPTNAMEPTT----QAQIFRLLTRLNQnnntTILLISHDLQMLSQWADKINVL 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-197 |
3.58e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENvvldKFSL----AIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEI-----------KVKGKLIDEYdLIELRR 77
Cdd:COG1245 83 YGEN----GFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQDY-FKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 G---IGYVIQQIGLLPHL---TVEdnicfvlDLLKKpePEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARAL 151
Cdd:COG1245 158 GeikVAHKPQYVDLIPKVfkgTVR-------ELLEK--VDERGKLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503125592 152 AANPEIILMDEPFGAVDEITRRNLQdELIKIHSKLKKTIIFVTHDI 197
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVA-RLIRELAEEGKYVLVVEHDL 272
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-220 |
7.11e-13 |
|
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: 69.06 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAY-----SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRG 78
Cdd:COG4615 328 LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 79 IGYVIQQIGLLPHLtvednicfvLDLLKKPEPEKksvAKELIKLVGMDE------GMLRRypKELSGGQQQRVGVARALA 152
Cdd:COG4615 408 FSAVFSDFHLFDRL---------LGLDGEADPAR---ARELLERLELDHkvsvedGRFST--TDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 153 ANPEIILMDEpfGAVDeitrrnlQD---------ELIkihSKLK---KTIIFVTHDiEEAIKLGTRIVLLNDGVIERNEK 220
Cdd:COG4615 474 EDRPILVFDE--WAAD-------QDpefrrvfytELL---PELKargKTVIAISHD-DRYFDLADRVLKMDYGKLVELTG 540
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-215 |
1.07e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLID-EYDLIELRRGIGYVIQ---QIGLLPHLTVEDNI 98
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNFSIAQNM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CfVLDLLKKP----------EPEKKSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVD 168
Cdd:PRK09700 363 A-ISRSLKDGgykgamglfhEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503125592 169 EITRrnlqDELIKIHSKLK---KTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK09700 442 VGAK----AEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-224 |
1.15e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.65 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 17 VVLDKFSLAIEQGEFLVLLGPSGCGKTTILkmingllipdsgeikvkGKLIDEYDLIELR----RGIGYVIQQIGLLpHL 92
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLL-----------------QSLLSQFEISEGRvwaeRSIAYVPQQAWIM-NA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNICFVldllkKPEPEKK--------SVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:PTZ00243 736 TVRGNILFF-----DEEDAARladavrvsQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 165 GAVDEITRRNLQDELIKIHSKlKKTIIFVTHDIeEAIKLGTRIVLLNDGVIERNEKKRDF 224
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALA-GKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADF 868
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-215 |
1.24e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 14 SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVkgklideydlieLRRGIGYViQQIGLLPHLT 93
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYV-PQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICFVLDLlkkpEPEK-------KSVAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGA 166
Cdd:PLN03130 695 VRDNILFGSPF----DPERyeraidvTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 167 VDEITRRNLQDELIKIHSKlKKTIIFVTHDIEEAIKLgTRIVLLNDGVI 215
Cdd:PLN03130 771 LDAHVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-196 |
5.70e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 5 EFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLideydlielrrGIGYVIQ 84
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL-----------EVAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 85 -QIGLLPHLTVEDNicfvldllkkpepekksVA--KELIKLVGMDEGML------------RRYP-KELSGGQQQRVGVA 148
Cdd:PRK11147 390 hRAELDPEKTVMDN-----------------LAegKQEVMVNGRPRHVLgylqdflfhpkrAMTPvKALSGGERNRLLLA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503125592 149 RALAANPEIILMDEPFGAVDeITRRNLQDELIkihSKLKKTIIFVTHD 196
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLD-VETLELLEELL---DSYQGTVLLVSHD 496
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-200 |
6.40e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGllipD-----SGEIKVKGKLIDEYDLI-ELRR 77
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgySNDLTLFGRRRGSGETIwDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIgllpHL------TVEDNIC---F--------VLDLLKKpepekksVAKELIKLVGMDEGMLRRYPKELSGG 140
Cdd:PRK10938 337 HIGYVSSSL----HLdyrvstSVRNVILsgfFdsigiyqaVSDRQQK-------LAQQWLDILGIDKRTADAPFHSLSWG 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503125592 141 QQQRVGVARALAANPEIILMDEPFGAVDEITR---RNLQDELIkihSKLKKTIIFVTHDIEEA 200
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI---SEGETQLLFVSHHAEDA 465
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-215 |
7.41e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 17 VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPD----SGEIKVKGKlidEYDLIELR-RGIGYVIQ--QIGLL 89
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRgRKIATIMQnpRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 90 PHLTVEDNICFVLDLLKKPEPEkkSVAKELIKLVGMDEG--MLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAV 167
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503125592 168 DEITRRNLQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-215 |
1.05e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 22 FSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIgyVI-----QQIGLLPHLTVE 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGI--MLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 96 DNI---C--------FVLDLLKKPEPEKKSVAKELIKLVGMDEGMlrrypKELSGGQQQRVGVARALAANPEIILMDEP- 163
Cdd:PRK11288 350 DNInisArrhhlragCLINNRWEAENADRFIRSLNIKTPSREQLI-----MNLSGGNQQKAILGRWLSEDMKVILLDEPt 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 164 ----FGAVDEITrrnlqdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK11288 425 rgidVGAKHEIY------NVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-274 |
1.19e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.07 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideydlielrrgIGYVIQQIGLLPHLTVEDNI 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRrnlQDE 178
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGE-FIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA---QKC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 179 LIKIHS--KLKKTIIFVTHDIEEAIKLGTRIVLLNDGvierneKKRDFVLLDDrseyakkffESKDFMAYLNTIKIKDLV 256
Cdd:PRK13546 183 LDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGG------KLKDYGELDD---------VLPKYEAFLNDFKKKSKA 247
|
250
....*....|....*...
gi 503125592 257 iKQSDISFDLYDSRSLVK 274
Cdd:PRK13546 248 -EQKEFRNKLDESRFVIK 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-215 |
1.36e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVvldkfSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIE-LRRGIGYV 82
Cdd:PRK10762 258 LKVDNLSGPGVNDV-----SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 IQQI---GLLPHLTVEDNICFV-LDLLKKP------EPEKKSVAKEL----IKLVGMDEGMlrrypKELSGGQQQRVGVA 148
Cdd:PRK10762 333 SEDRkrdGLVLGMSVKENMSLTaLRYFSRAggslkhADEQQAVSDFIrlfnIKTPSMEQAI-----GLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 149 RALAANPEIILMDEPFGAVD-----EITrrnlqdELIkihSKLKK---TIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDvgakkEIY------QLI---NQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-163 |
2.44e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMI----NGLLIpdSGEIKVKGKLIDEydliELRRGIGYVIQQIGLLPHLTV 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLagrkTAGVI--TGEILINGRPLDK----NFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 95 EDNICFVLDLlkkpepekksvakeliklvgmdegmlrrypKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:cd03232 97 REALRFSALL------------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-237 |
8.35e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSE--NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDsGEIKVKGKLIDEYDLIELRRGIGYVIQ 84
Cdd:TIGR01271 1221 QGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 85 QIgllphltvednicFVLD--LLKKPEPEKKSVAKELIKL---VGMdEGMLRRYPKEL-----------SGGQQQRVGVA 148
Cdd:TIGR01271 1300 KV-------------FIFSgtFRKNLDPYEQWSDEEIWKVaeeVGL-KSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 149 RALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLkkTIIFVTHDIEEAIKLGTRIvllndgVIERNEKKR-DFV-- 225
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRVEALLECQQFL------VIEGSSVKQyDSIqk 1437
|
250
....*....|..
gi 503125592 226 LLDDRSEYAKKF 237
Cdd:TIGR01271 1438 LLNETSLFKQAM 1449
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-197 |
1.19e-10 |
|
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: 60.84 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 7 NDVSKAYSENvvldKFSL----AIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG---KLIDEYDLIELRR-- 77
Cdd:cd03236 4 DEPVHRYGPN----SFKLhrlpVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDEFRGSELQNyf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 ------GIGYVI--QQIGLLPHlTVEDNicfVLDLLKKPEpeKKSVAKELIKLVGMdEGMLRRYPKELSGGQQQRVGVAR 149
Cdd:cd03236 80 tkllegDVKVIVkpQYVDLIPK-AVKGK---VGELLKKKD--ERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503125592 150 ALAANPEIILMDEPFGAVDeITRRNLQDELIKIHSKLKKTIIFVTHDI 197
Cdd:cd03236 153 ALARDADFYFFDEPSSYLD-IKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-196 |
1.23e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSEN-VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKvkgklideydlIELRRGIGY 81
Cdd:TIGR03719 4 IYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----------PQPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNI----CFVLDLLKK----------PEPEKKSVAKELIKL-----------------VGMDEgmL 130
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVeegvAEIKDALDRfneisakyaePDADFDKLAAEQAELqeiidaadawdldsqleIAMDA--L 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503125592 131 RRYPKE-----LSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIkihsKLKKTIIFVTHD 196
Cdd:TIGR03719 151 RCPPWDadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHD 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-197 |
1.71e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 22 FSLAI-EQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKG---KLIDEY----------DLIELRRGIGYVIQQIG 87
Cdd:PRK13409 91 YGLPIpKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKRFrgtelqnyfkKLYNGEIKVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 88 LLPHL---TVEdnicfvlDLLKKpePEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPF 164
Cdd:PRK13409 171 LIPKVfkgKVR-------ELLKK--VDERGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|...
gi 503125592 165 GAVDEITRRNLQDeLIKIHSKlKKTIIFVTHDI 197
Cdd:PRK13409 241 SYLDIRQRLNVAR-LIRELAE-GKYVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-168 |
2.04e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 17 VVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLL---IPDSGEIKVKGKLIDEydliELRRGIGYVIQQIGLLPHLT 93
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDS----SFQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICF--VLDLLKK-PEPEKKSVAKELIKLVGMDE--GMLRRYPKE-LSGGQQQRVGVARALAANPEIIL-MDEPFGA 166
Cdd:TIGR00956 853 VRESLRFsaYLRQPKSvSKSEKMEYVEEVIKLLEMESyaDAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
..
gi 503125592 167 VD 168
Cdd:TIGR00956 933 LD 934
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-225 |
2.09e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDS--GEIKVKGKLIDEYDLIEL-RRGI 79
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSeALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 GYVIQQIGLLPHLTVEDNIcFVLDllkkpEPEKKSV---------AKELIKLVGMDEGmlrryPKELSG----GQQQRVG 146
Cdd:NF040905 81 VIIHQELALIPYLSIAENI-FLGN-----ERAKRGVidwnetnrrARELLAKVGLDES-----PDTLVTdigvGKQQLVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 147 VARALAANPEIILMDEPFGAVDEITRRNLQDeLIKihsKLKK---TIIFVTHDIEEAIKLGTRIVLLNDG-VIERNEKKR 222
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLD-LLL---ELKAqgiTSIIISHKLNEIRRVADSITVLRDGrTIETLDCRA 225
|
...
gi 503125592 223 DFV 225
Cdd:NF040905 226 DEV 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-215 |
4.38e-10 |
|
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: 58.31 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPDSGEIKVKGKlideyDLIEL------ 75
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGE-----DITDLppeera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGYVIQQIGLLPHLTVEDNICFVldllkkpepekksvakeliklvgmDEGmlrrypkeLSGGQQQRVGVARALAANP 155
Cdd:cd03217 76 RLGIFLAFQYPPEIPGVKNADFLRYV------------------------NEG--------FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 156 EIILMDEPFGAVDEITRRNLQDELIKIHSKlKKTIIFVTH--DIEEAIKlGTRIVLLNDGVI 215
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyqRLLDYIK-PDRVHVLYDGRI 183
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-209 |
7.08e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 28 QGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVkgklideydlielrrgigyviqqigllphLTVEDNICFVLDLLKk 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------IDGEDILEEVLDQLL- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 108 pepekksvakeliklvgmdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDE-----LIKI 182
Cdd:smart00382 51 -------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLL 111
|
170 180
....*....|....*....|....*..
gi 503125592 183 HSKLKKTIIFVTHDIEEAIKLGTRIVL 209
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-236 |
9.04e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYS--ENVVLDK-FSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKgkliDEYDLIEL----- 75
Cdd:PTZ00265 383 IQFKNVRFHYDtrKDVEIYKdLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDInlkww 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 76 RRGIGyVIQQIGLLPHLTVEDNICFVLDLLKKPE---------------------------------------------- 109
Cdd:PTZ00265 459 RSKIG-VVSQDPLLFSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliem 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 110 ---------PEKKSVAKELI------KLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRN 174
Cdd:PTZ00265 538 rknyqtikdSEVVDVSKKVLihdfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503125592 175 LQDELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDgviERNEKKRDFVLLDDRSEYAKK 236
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNR---ERGSTVDVDIIGEDPTKDNKE 676
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-198 |
1.59e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.56 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSE--NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDsGEIKVKGKLIDEYDLIELRRGIGY 81
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIgllphltvednICFVLDLLKKPEPEKKSVAKELIKL---VGMdEGMLRRYPKEL-----------SGGQQQRVGV 147
Cdd:cd03289 82 IPQKV-----------FIFSGTFRKNLDPYGKWSDEEIWKVaeeVGL-KSVIEQFPGQLdfvlvdggcvlSHGHKQLMCL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503125592 148 ARALAANPEIILMDEPFGAVDEITRRNLQDELikIHSKLKKTIIFVTHDIE 198
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTL--KQAFADCTVILSEHRIE 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-202 |
1.68e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 14 SENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDlielRRGIGYVIQQIGLLPHLT 93
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 94 VEDNICFVLDLLKKPEPEKKSVakELIKLvgmdEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEiTRR 173
Cdd:PRK13541 87 VFENLKFWSEIYNSAETLYAAI--HYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK-ENR 159
|
170 180
....*....|....*....|....*....
gi 503125592 174 NLQDELIKIHSKLKKTIIFVTHdIEEAIK 202
Cdd:PRK13541 160 DLLNNLIVMKANSGGIVLLSSH-LESSIK 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-173 |
2.46e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKlideyDLIELR------ 76
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG-----DMADARhrravc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 -RgIGYVIQQIG--LLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEgMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:NF033858 76 pR-IAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180
....*....|....*....|
gi 503125592 154 NPEIILMDEPFGAVDEITRR 173
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRR 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-216 |
3.35e-09 |
|
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: 58.03 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSE--NVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGy 81
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT- 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNicfvLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKE-------LSGGQQQRVGVARALAAN 154
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMN----LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 155 PEIILMDEPFGAVDEITrrnlqDELIK--IHSKLKK-TIIFVTHDIeEAIKLGTRIVLLNDGVIE 216
Cdd:TIGR00957 1440 TKILVLDEATAAVDLET-----DNLIQstIRTQFEDcTVLTIAHRL-NTIMDYTRVIVLDKGEVA 1498
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-239 |
3.96e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 26 IEQGEFLVLLGPSGCGKTTILKMI----NGLLIPDSGEIKVKGklIDEYDLIELRRG-IGYVIQQIGLLPHLTVEDNICF 100
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG--ITPEEIKKHYRGdVVYNAETDVHFPHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 101 VLdLLKKPE--PE---KKSVAKELIKL--------------VGMDegMLRrypkELSGGQQQRVGVARALAANPEIILMD 161
Cdd:TIGR00956 162 AA-RCKTPQnrPDgvsREEYAKHIADVymatyglshtrntkVGND--FVR----GVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 162 EPFGAVD-----EITRrnlqdeLIKIHSKLKKTIIFVT--HDIEEAIKLGTRIVLLNDGVIernekkrdfVLLDDRSEyA 234
Cdd:TIGR00956 235 NATRGLDsatalEFIR------ALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQ---------IYFGPADK-A 298
|
....*
gi 503125592 235 KKFFE 239
Cdd:TIGR00956 299 KQYFE 303
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-195 |
5.80e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLliPD----SGEIKVKGKLIDEYDLIEL-RR 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEERaHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLTVEDNICFVLD----LLKKPEPEKKS---VAKELIKLVGMDEGMLRRYPKE-LSGGQQQRVGVAR 149
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLRLAYNskrkFQGLPELDPLEfleIINEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503125592 150 ALAANPEIILMDEPFGAVDeITRRNLQDELIKIHSKLKKTIIFVTH 195
Cdd:CHL00131 165 MALLDSELAILDETDSGLD-IDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-210 |
6.63e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.50 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 26 IEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEikvkgkliDEYDLIElrrgIGYVIQQIgllphltvednicfvldll 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------DEWDGIT----PVYKPQYI------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 106 kkpepekksvakeliklvgmdegmlrrypkELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSK 185
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 503125592 186 LKKTIIFVTHDIEEAIKLGTRIVLL 210
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-196 |
7.23e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 9 VSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEikvkgklideydlIELRRGI--GYVIQQi 86
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE-------------IGLAKGIklGYFAQH- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 87 gLLPHLTVEDNICFVLDLLKKPEPEKKsvAKELIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGA 166
Cdd:PRK10636 384 -QLEFLRADESPLQHLARLAPQELEQK--LRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190
....*....|....*....|....*....|
gi 503125592 167 VDEITRRNLQDELIKIHSKLkktiIFVTHD 196
Cdd:PRK10636 461 LDLDMRQALTEALIDFEGAL----VVVSHD 486
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-226 |
8.52e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGy 81
Cdd:PTZ00243 1309 LVFEGVQMRYREGLplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS- 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNicfvLDLLKKPEPEKKSVAKElikLVGMDEgmlrRYPKELSG--------------GQQQRVGV 147
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQN----VDPFLEASSAEVWAALE---LVGLRE----RVASESEGidsrvleggsnysvGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 148 ARA-LAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLkkTIIFVTHdieeaiKLGT-----RIVLLNDGVIERNEKK 221
Cdd:PTZ00243 1457 ARAlLKKGSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAH------RLHTvaqydKIIVMDHGAVAEMGSP 1528
|
....*
gi 503125592 222 RDFVL 226
Cdd:PTZ00243 1529 RELVM 1533
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-215 |
3.00e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCG--KTTILKMINGlliPDSGEIKVKGKLIDEyDLIELRRGIG- 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCA-NRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRYPKeLSGGQQQRVGVARALAANPEIILM 160
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 161 DEPFGAVDEITRRNLQDElIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDGVI 215
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-213 |
4.85e-08 |
|
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: 54.06 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPD--SGEIKVKGKLIDEYDLIE-LRRGIGYVIQ---QIGLLPHL 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGkfEGNVFINGKPVDIRNPAQaIRAGIAMVPEdrkRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNIcfVLDLLKKPEpeKKSVAKELIKLVGMDEGMLRRYPK---------ELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:TIGR02633 355 GVGKNI--TLSVLKSFC--FKMRIDAAAELQIIGSAIQRLKVKtaspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503125592 164 FGAVD-----EITRrnlqdeLIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:TIGR02633 431 TRGVDvgakyEIYK------LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-196 |
6.64e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 34 LLGPSGCGKTTILKMINGLLIPDSGEIKVK-----GKLIDEYDLIELRRGIGYVIQ-------------QIGLLPHLTVE 95
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQDQFAFEEFTVLDTVIMghtelwevkqerdRIYALPEMSEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 96 DNIcfvldllKKPEPEKK----------SVAKELIKLVGMDE----GMLRrypkELSGGQQQRVGVARALAANPEIILMD 161
Cdd:PRK15064 112 DGM-------KVADLEVKfaemdgytaeARAGELLLGVGIPEeqhyGLMS----EVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190
....*....|....*....|....*....|....*
gi 503125592 162 EPFGAVDEITRRNLQDELikihSKLKKTIIFVTHD 196
Cdd:PRK15064 181 EPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-196 |
1.73e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDK-FSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEI----KVKGKLIDEYDLIELRR 77
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKnLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 78 GIGYVIQQIGLLPHLtvednicfvldllkkpePEKKSVAKelIKLVGMDEGMLRRYPKELSGGQQQRVGVARALAANPEI 157
Cdd:PLN03073 588 SSNPLLYMMRCFPGV-----------------PEQKLRAH--LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190
....*....|....*....|....*....|....*....
gi 503125592 158 ILMDEPFGAVDeitrRNLQDELIKIHSKLKKTIIFVTHD 196
Cdd:PLN03073 649 LLLDEPSNHLD----LDAVEALIQGLVLFQGGVLMVSHD 683
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-235 |
3.19e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGy 81
Cdd:PLN03232 1235 IKFEDVHLRYRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS- 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 82 VIQQIGLLPHLTVEDNIcfvldllkKPEPEK------KSVAKELIKLV------GMD----EGmlrryPKELSGGQQQRV 145
Cdd:PLN03232 1314 IIPQSPVLFSGTVRFNI--------DPFSEHndadlwEALERAHIKDVidrnpfGLDaevsEG-----GENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 146 GVARALAANPEIILMDEPFGAVDEITrrnlqDELIK--IHSKLKK-TIIFVTHDIEEAIKLGTRIVLLNDGVIERNEKKR 222
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRT-----DSLIQrtIREEFKScTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQE 1455
|
250
....*....|...
gi 503125592 223 dfVLLDDRSEYAK 235
Cdd:PLN03232 1456 --LLSRDTSAFFR 1466
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-202 |
3.39e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVK------------GKLIDE------YDLI-ELRRGIGYVI 83
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlsfeqlQKLVSDewqrnnTDMLsPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 84 QQIgllphltvednicfVLDLLKKPEpekksVAKELIKLVGMDEGMLRRYpKELSGGQQQRVGVARALAANPEIILMDEP 163
Cdd:PRK10938 103 AEI--------------IQDEVKDPA-----RCEQLAQQFGITALLDRRF-KYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503125592 164 FGAVDEITRRNLQDELIKIHSKlKKTIIFVT---HDIEEAIK 202
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQS-GITLVLVLnrfDEIPDFVQ 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-216 |
3.67e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIkvkgkLIDEYD-----LIELR 76
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI-----LIDGCDiskfgLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIGyVIQQIGLLPHLTVEdnicFVLDllkkPEPEKKSV----AKELIKLvgmdEGMLRRYPKEL-----------SGGQ 141
Cdd:PLN03130 1313 KVLG-IIPQAPVLFSGTVR----FNLD----PFNEHNDAdlweSLERAHL----KDVIRRNSLGLdaevseagenfSVGQ 1379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503125592 142 QQRVGVARALAANPEIILMDEPFGAVDEITrrnlqDELIK--IHSKLKK-TIIFVTHDIEEAIKLgTRIVLLNDG-VIE 216
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRT-----DALIQktIREEFKScTMLIIAHRLNTIIDC-DRILVLDAGrVVE 1452
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-225 |
1.22e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLiPD--SGEIKVKGKLIDeydlIE-----LRRGIGYVIQ---QIG 87
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDGKPVK----IRnpqqaIAQGIAMVPEdrkRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 88 LLPHLTVEDNICF-VLDLLKKP-----EPEKKSVAKELIKL-VGMDEGMLRryPKELSGGQQQRVGVARALAANPEIILM 160
Cdd:PRK13549 352 IVPVMGVGKNITLaALDRFTGGsriddAAELKTILESIQRLkVKTASPELA--IARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 161 DEPFGAVD-----EITrrNLQDELIKIHSklkkTIIFVTHDIEEAIKLGTRIVLLNDGVIernekKRDFV 225
Cdd:PRK13549 430 DEPTRGIDvgakyEIY--KLINQLVQQGV----AIIVISSELPEVLGLSDRVLVMHEGKL-----KGDLI 488
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-168 |
1.66e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 25 AIEQGEFLVLLGPSGCGKTTILKMINGLLIPD--SGEIKVKG--KLIDEYDLIElrrgiGYVIQQIGLLPHLTVEDNICF 100
Cdd:PLN03140 902 AFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpKKQETFARIS-----GYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503125592 101 --VLDLLKK-PEPEKKSVAKELIKLVGMDEgmLRR----YP--KELSGGQQQRVGVARALAANPEIILMDEPFGAVD 168
Cdd:PLN03140 977 saFLRLPKEvSKEEKMMFVDEVMELVELDN--LKDaivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-213 |
1.79e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 19 LDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLideyDLIELRRgigyviqqiGLLPHLTVEDNI 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA----ALIAISS---------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 99 CFVLDLLKKPEPEKKSVAKELIKLVgmDEGMLRRYP-KELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQD 177
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFA--DIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 503125592 178 ELIKIHSKlKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK13545 185 KMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-213 |
2.90e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 23 SLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKVKGKLIDEYD-----------LIELRRGIGYV--------- 82
Cdd:PRK10982 268 SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYayldigfns 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 83 --------IQQIGLLPHLTVEDNICFVLDLLKKPEPEKKSvakelikLVGmdegmlrrypkELSGGQQQRVGVARALAAN 154
Cdd:PRK10982 348 lisnirnyKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRT-------QIG-----------SLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503125592 155 PEIILMDEP-----FGAVDEITrrnlqdELIKIHSKLKKTIIFVTHDIEEAIKLGTRIVLLNDG 213
Cdd:PRK10982 410 PEILMLDEPtrgidVGAKFEIY------QLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-167 |
2.01e-05 |
|
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: 45.90 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVL-DKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPDSGEIKV--KGKLIdeydlielrrgi 79
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLF------------ 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 80 gYVIQQigllPHLTV---EDNICF---VLDLLKKPEPEKksVAKELIKLVGMD----EGM----LRRYPKELSGGQQQRV 145
Cdd:TIGR00954 519 -YVPQR----PYMTLgtlRDQIIYpdsSEDMKRRGLSDK--DLEQILDNVQLThileREGgwsaVQDWMDVLSGGEKQRI 591
|
170 180
....*....|....*....|..
gi 503125592 146 GVARALAANPEIILMDEPFGAV 167
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAV 613
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-243 |
5.73e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 18 VLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGLLIPD---SGEIKVKGKLIDEYdliELRRGIGYVIQQIGLLPHLTV 94
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEF---VPRKTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 95 EDNICFV---------LDLLKK-----------PEPE----KKSVAKE----------LIKLVGMD--------EGMLRr 132
Cdd:PLN03140 257 KETLDFSarcqgvgtrYDLLSElarrekdagifPEAEvdlfMKATAMEgvksslitdyTLKILGLDickdtivgDEMIR- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 133 ypkELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIKIHSKLKKTIIF-VTHDIEEAIKLGTRIVLLN 211
Cdd:PLN03140 336 ---GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFDDIILLS 412
|
250 260 270
....*....|....*....|....*....|..
gi 503125592 212 DGVIERnEKKRDFVLlddrseyakKFFESKDF 243
Cdd:PLN03140 413 EGQIVY-QGPRDHIL---------EFFESCGF 434
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
9-208 |
1.34e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 9 VSKAYSENVVLDKFSlaIEQGEFLVLLGPSGCGKTTILKMIngllipdsgeIKVKGKLIDEydlielrrgigyviqqigl 88
Cdd:cd03238 3 VSGANVHNLQNLDVS--IPLNVLVVVTGVSGSGKSTLVNEG----------LYASGKARLI------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 89 lphltvednicfvlDLLKKPEPEKKSVAKELIKLVGMDEGMLR--RYPKELSGGQQQRVGVARALAANPE--IILMDEPF 164
Cdd:cd03238 52 --------------SFLPKFSRNKLIFIDQLQFLIDVGLGYLTlgQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503125592 165 GAVDEITRRNLQDELIKIHSkLKKTIIFVTHDiEEAIKLGTRIV 208
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLID-LGNTVILIEHN-LDVLSSADWII 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-210 |
2.05e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 129 MLRRYPKELSGGQQQRVGVARALAANPEIILMDEPFGAVDEITRRNLQDELIkihsKLKKTIIFVTHDIEEAIKLGTRIV 208
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSHAREFLNTVVTDIL 412
|
..
gi 503125592 209 LL 210
Cdd:PLN03073 413 HL 414
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-195 |
3.80e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 3 IIEFNDVSKAYSENVVLDKFSLAIEQGEFLVLLGPSGCGKTTILKMINGL--LIPDSGEIKVKGKlideyDLIEL----R 76
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGK-----DLLELspedR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 77 RGIG------YVIQQIGLLPHLTVEDNICFVLDLLKKPEPEK---KSVAKELIKLVGMDEGMLRRYPKE-LSGGQQQRVG 146
Cdd:PRK09580 76 AGEGifmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRfdfQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRND 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503125592 147 VARALAANPEIILMDEPFGAVDeITRRNLQDELIKIHSKLKKTIIFVTH 195
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-197 |
8.96e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 33 VLLGPSGCGKTTIL---------------KMINGLLIPDSGEIKVKGKLIDEYDLIELRRGIGYVIQQIGLLP------- 90
Cdd:COG0419 27 LIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEEASVELEFEHGGKRYRIERRQGEFAEFLEAKPserkeal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 91 -HLTVEDNICFVLDLLKKPEPEKKSVAKELIKLVGMDEGMLRRY-----PKELSGGQQQRVGVARALAanpeiILMDepF 164
Cdd:COG0419 107 kRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALADLLS-----LILD--F 179
|
170 180 190
....*....|....*....|....*....|...
gi 503125592 165 GAVDEITRRNLQDELIKIHsklkktiiFVTHDI 197
Cdd:COG0419 180 GSLDEERLERLLDALEELA--------IITHVI 204
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
13-208 |
1.61e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 13 YSENVVLDkFSLAIEQGEFLVLlGPSGCGKTTILKMINGLLIpdsGEIKVKGKLIDEYDLIELRRGIGYVIqqigllphL 92
Cdd:cd03279 14 FREEQVID-FTGLDNNGLFLIC-GPTGAGKSTILDAITYALY---GKTPRYGRQENLRSVFAPGEDTAEVS--------F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 93 TVEDNicfvlDLLKKPEPEKKSVAKELIKLVGMDEG----MLRRYPKELSGGQQQRVGVARALA----------ANPEII 158
Cdd:cd03279 81 TFQLG-----GKKYRVERSRGLDYDQFTRIVLLPQGefdrFLARPVSTLSGGETFLASLSLALAlsevlqnrggARLEAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503125592 159 LMDEPFGAVDEITRRNLQDELIKIHSkLKKTIIFVTHDIEEAIKLGTRIV 208
Cdd:cd03279 156 FIDEGFGTLDPEALEAVATALELIRT-ENRMVGVISHVEELKERIPQRLE 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-229 |
1.87e-03 |
|
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: 39.12 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 4 IEFNDVSKAYSENV--VLDKFSLAIEQGEFLVLLGPSGCGKTTI-LKMINGLLIPDsGEIKVKGKLIDEYDLIELRRGIG 80
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 81 YVIQQIGLLphltvEDNICFVLDLLKKPEPEKKSVAKELIKLVGMD-------EGMLRRYPKELSGGQQQRVGVARALAA 153
Cdd:cd03288 99 IILQDPILF-----SGSIRFNLDPECKCTDDRLWEALEIAQLKNMVkslpgglDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503125592 154 NPEIILMDEPFGAVDEITRRNLQDELIKIHSklKKTIIFVTHDIEEAIKLGTRIVlLNDGVIERNEKKRDFVLLDD 229
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAHRVSTILDADLVLV-LSRGILVECDTPENLLAQED 246
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-196 |
3.26e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 29 GEFLVLLGPSGCGKTTILKMIngllipdsgeikvkgKLIDEYDLIELRRGIGYVIQQIGLLPHLTvednICFVLDllkkp 108
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAI---------------GLALGGAQSATRRRSGVKAGCIVAAVSAE----LIFTRL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 109 epekksvakeliklvgmdegmlrrypkELSGGQQQRVGVARALA---ANPE-IILMDEPFGAVDEITRRNLQDeLIKIHS 184
Cdd:cd03227 77 ---------------------------QLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAE-AILEHL 128
|
170
....*....|..
gi 503125592 185 KLKKTIIFVTHD 196
Cdd:cd03227 129 VKGAQVIVITHL 140
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
92-208 |
4.87e-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: 38.84 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 92 LTVEDNICFVLDLlkKPEPEKKSVAKELIKL----------VGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIIL-- 159
Cdd:TIGR00630 436 LSIREAHEFFNQL--TLTPEEKKIAEEVLKEirerlgflidVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLyv 513
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 503125592 160 MDEP-FGAVDEITRRnlqdeLIKIHSKLKK---TIIFVTHDiEEAIKLGTRIV 208
Cdd:TIGR00630 514 LDEPsIGLHQRDNRR-----LINTLKRLRDlgnTLIVVEHD-EDTIRAADYVI 560
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
18-49 |
7.59e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 7.59e-03
10 20 30
....*....|....*....|....*....|...
gi 503125592 18 VLDKFSLAIEQGE-FLVLLGPSGCGKTTILKMI 49
Cdd:COG3267 31 ALARLEYALAQGGgFVVLTGEVGTGKTTLLRRL 63
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
123-208 |
7.62e-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: 37.24 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503125592 123 VGMDEGMLRRYPKELSGGQQQRVGVARALAANPEIIL--MDEPFGAVDEitRRNlqDELIKIHSKLKK---TIIFVTHDi 197
Cdd:cd03270 124 VGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHP--RDN--DRLIETLKRLRDlgnTVLVVEHD- 198
|
90
....*....|.
gi 503125592 198 EEAIKLGTRIV 208
Cdd:cd03270 199 EDTIRAADHVI 209
|
|
| |
