|
Name |
Accession |
Description |
Interval |
E-value |
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-346 |
0e+00 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 754.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDI 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDA 240
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 241 NIFPATLTHDSVNIFNYHLPRPAQLATD--NTEITVGVRPEAITLSLQGDDSQRCTVTHVAYMGPQYEVTVDWHGQSMLL 318
Cdd:PRK11432 241 NIFPATLSGDYVDIYGYRLPRPAAFAFNlpDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQELLL 320
|
330 340
....*....|....*....|....*...
gi 757596975 319 QINATQLQPTVGENLYLQIHPYGMFILE 346
Cdd:PRK11432 321 QVNATQLQPDLGEHYYLEIHPYGMFLLA 348
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-346 |
0e+00 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 505.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQ 85
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFPA 245
Cdd:COG3842 165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 246 TLTH---DSVNIFNYHLPRPAQLA-TDNTEITVGVRPEAITLSLQGDDSQ-RCTVTHVAYMGPQYEVTVDW-HGQSMLLQ 319
Cdd:COG3842 245 TVLGdegGGVRTGGRTLEVPADAGlAAGGPVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLgDGQELVVR 324
|
330 340
....*....|....*....|....*...
gi 757596975 320 I-NATQLQPTVGENLYLQIHPYGMFILE 346
Cdd:COG3842 325 VpNRAALPLEPGDRVGLSWDPEDVVVLP 352
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-339 |
1.87e-167 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 470.32 E-value: 1.87e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGD--ANIFP 244
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 245 ATLTHDSVNIFNYHLPRPAQLAT-DNTEITVGVRPEAITLSLQGDDSQRCTVTHVAYMGPQYEVTVDWHGQSMLLQINAt 323
Cdd:COG3839 244 GTVEGGGVRLGGVRLPLPAALAAaAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLGGQELVARVPG- 322
|
330
....*....|....*.
gi 757596975 324 QLQPTVGENLYLQIHP 339
Cdd:COG3839 323 DTRLRPGDTVRLAFDP 338
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-344 |
2.94e-145 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 413.77 E-value: 2.94e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-TDRSIQQRDICMVFQ 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFPA 245
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 246 TLTHDSVNIFNyhLPRPAQLATDNTEITVGVRPEAITLSLQGDDSQ--RCTVTHVAYMGPQYEVTV---DWHGQSMLLQI 320
Cdd:COG1118 243 RVIGGQLEADG--LTLPVAEPLPDGPAVAGVRPHDIEVSREPEGENtfPATVARVSELGPEVRVELkleDGEGQPLEAEV 320
|
330 340
....*....|....*....|....*..
gi 757596975 321 N---ATQLQPTVGENLYLQIHPYGMFI 344
Cdd:COG1118 321 TkeaWAELGLAPGDPVYLRPRPARVFL 347
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-291 |
4.67e-127 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 368.89 E-value: 4.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDI 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDA 240
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEI 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 241 NIFPATLT--HDSVNI--------FNYHLPRPAQLatdNTEITVGVRPEAITLSLQGDDSQ 291
Cdd:PRK09452 249 NIFDATVIerLDEQRVranvegreCNIYVNFAVEP---GQKLHVLLRPEDLRVEEINDDEH 306
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-337 |
9.52e-127 |
|
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: 367.05 E-value: 9.52e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQ 85
Cdd:TIGR03265 4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:TIGR03265 84 SYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFPA 245
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 246 T-LTHDSVNIFNYHLPRPAQLATDNTEITVGVRPEAITLSLQGDDSQR--CTVTHVAYMGPQYEVTV---DWHGQSMLLQ 319
Cdd:TIGR03265 244 TrGGGSRARVGGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNAANLllARVEDMEFLGAFYRLRLrleGLPGQALVAD 323
|
330 340
....*....|....*....|.
gi 757596975 320 INATQLQPT---VGENLYLQI 337
Cdd:TIGR03265 324 VSASEVERLgirAGQPIWIEL 344
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-238 |
4.29e-124 |
|
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: 355.78 E-value: 4.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMG 238
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-219 |
8.73e-122 |
|
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: 349.13 E-value: 8.73e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-340 |
3.34e-118 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 345.68 E-value: 3.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQ 85
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDA--NIF 243
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPamNLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 244 PATLT-HDSVNIFNYH--LPRPAQLATDNTE-ITVGVRPEAITLSlQGDDSQRCTVTHVAYMGPQYEVTVDWHGQSMLLQ 319
Cdd:PRK11650 244 DGRVSaDGAAFELAGGiaLPLGGGYRQYAGRkLTLGIRPEHIALS-SAEGGVPLTVDTVELLGADNLAHGRWGGQPLVVR 322
|
330 340
....*....|....*....|....*.
gi 757596975 320 InATQLQPTVGENLYL-----QIHPY 340
Cdd:PRK11650 323 L-PHQERPAAGSTLWLhlpanQLHLF 347
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-239 |
8.40e-114 |
|
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: 330.07 E-value: 8.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKM----LGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGD 239
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-219 |
2.90e-108 |
|
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: 314.96 E-value: 2.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-242 |
2.96e-106 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 310.96 E-value: 2.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANI 242
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-339 |
1.80e-105 |
|
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: 312.12 E-value: 1.80e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 37 LLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKR 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 117 VDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 197 QSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFPATLTH--DSVNIFNYHLPRPAQLATD-----N 269
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIErkSEQVVLAGVEGRRCDIYTDvpvekD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 270 TEITVGVRPEAITL----SLQGDDSQRCTVTHVAYMGPQYEVTVDW-HGQSMLLQI----NATQLQPTVGENLYLQIHP 339
Cdd:TIGR01187 241 QPLHVVLRPEKIVIeeedEANSSNAIIGHVIDITYLGMTLEVHVRLeTGQKVLVSEffneDDPHMSPSIGDRVGLTWHP 319
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-335 |
6.80e-102 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 303.93 E-value: 6.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLglPK------AEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVL--PRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDA 240
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 241 NIFPATLTHDSVNIFNYHLPRPAQLATDNtEITVGVRPEAITLSLQGddSQRC----TVTHVAYMGPQYEVTV---DWHG 313
Cdd:PRK10851 241 NRLQGTIRGGQFHVGAHRWPLGYTPAYQG-PVDLFLRPWEVDISRRT--SLDSplpvQVLEVSPKGHYWQLVVqplGWYN 317
|
330 340
....*....|....*....|..
gi 757596975 314 QSMLLQINATQLQPTVGENLYL 335
Cdd:PRK10851 318 EPLTVVMHGDIDAPQRGERLFV 339
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
4.22e-100 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 295.85 E-value: 4.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHN-FVELKNVTKRF----GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSi 75
Cdd:COG1116 1 MSAAApALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 76 qqRDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:COG1116 80 --PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKG 213
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
7-311 |
1.15e-99 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 298.45 E-value: 1.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFG---TNTV-IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD--RSI---QQ 77
Cdd:NF040933 3 VRVENVTKIFKkgkKEVVaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgKIIvppED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:NF040933 83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFM 237
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 238 GDANIFPATLTHDSVNIFN-YHLPRPAQLAtDNTEITVGVRPEAITLSLQGDDS-------QRCTVTHVAYMGPQYEVTV 309
Cdd:NF040933 243 GDINLLEGKVEEEGLVDGNdLKIPLPNPKL-EAGEVIIGIRPEDIDISESDMRLppgfvevGKGRVKVSSYAGGVFRVVV 321
|
..
gi 757596975 310 DW 311
Cdd:NF040933 322 SP 323
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-335 |
2.31e-94 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 285.58 E-value: 2.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFPAT 246
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 247 LTH---DSVNIFNYHLPRPAQLAT-----DNTEITVGVRPEAITLSLQ----GDDSQRCTVTHVAYMGpqyEVTVdWHGQ 314
Cdd:PRK11607 260 LKErqeDGLVIDSPGLVHPLKVDAdasvvDNVPVHVALRPEKIMLCEEppadGCNFAVGEVIHIAYLG---DLSI-YHVR 335
|
330 340 350
....*....|....*....|....*....|
gi 757596975 315 SMLLQINATQLQ---------PTVGENLYL 335
Cdd:PRK11607 336 LKSGQMISAQLQnahryrkglPTWGDEVRL 365
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-238 |
2.56e-93 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 280.44 E-value: 2.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVF 84
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDL--AGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMG 238
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-302 |
2.78e-93 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 282.69 E-value: 2.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDA--NIFP 244
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmNFLP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 245 ATLTH---DSVNI-----FNYHLPRPAQLATDNTEITVGVRPEAITLSLQGDDSQRCTVTHVAYMG 302
Cdd:PRK11000 244 VKVTAtaiEQVQVelpnrQQVWLPVEGRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLG 309
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-215 |
5.24e-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: 276.27 E-value: 5.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSiqqRDICM 82
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNK--GKI 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-224 |
2.63e-89 |
|
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: 267.62 E-value: 2.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD----- 79
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYALFPHMSLGDNVGYGLKML-GLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-238 |
4.65e-87 |
|
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: 262.24 E-value: 4.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMV 83
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDL--AGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMG 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
22-310 |
8.28e-87 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 265.40 E-value: 8.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQSYALFPHMSLGDNVGY 101
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 102 GLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 182 LQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFPATLTHDSVNIFnyhlpr 261
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTI------ 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 262 paqLATDNTEIT----------VGVRPEAITLSLQGDDSQ-----RCTVTHVAYMGPQYEVTVD 310
Cdd:NF040840 250 ---LDTGNIKIElpeekkgkvrIGIRPEDITISTEKVKTSarnefKGKVEEIEDLGPLVKLTLD 310
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-242 |
6.05e-84 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 253.80 E-value: 6.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGtNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANI 242
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-230 |
1.49e-82 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 250.30 E-value: 1.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ----QRDICM 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGL-KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-228 |
1.29e-80 |
|
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: 254.44 E-value: 1.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN-----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ---- 77
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 -RDICMVFQ--SYALFPHMSLGDNVGYGLKMLG-LPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALI 152
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-227 |
7.58e-80 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 243.43 E-value: 7.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVFQ 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-224 |
1.46e-79 |
|
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: 242.79 E-value: 1.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ-----RDIC 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVGYGLKMLG-LPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-241 |
2.15e-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: 247.71 E-value: 2.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN-----------------------TV-IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGR 62
Cdd:COG4175 4 IEVRNLYKIFGKRperalklldqgkskdeilektgqTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 63 MFIDGEDVTD------RSIQQRDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQ 136
Cdd:COG4175 84 VLIDGEDITKlskkelRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIM 216
Cdd:COG4175 164 LSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
250 260
....*....|....*....|....*
gi 757596975 217 QLGSPQELYRQPASRFMASFMGDAN 241
Cdd:COG4175 244 QIGTPEEILTNPANDYVADFVEDVD 268
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-228 |
2.23e-78 |
|
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: 239.54 E-value: 2.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMV 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQS--YALFpHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-214 |
1.30e-77 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 235.54 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD----RSIQQRDICM 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGLkmlglpkaeirkrvdealelvdlagfadrfvdqiSGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-215 |
1.29e-75 |
|
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: 232.00 E-value: 1.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD--- 79
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ---ICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPK 156
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAvSDMVLVMNKGKI 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-239 |
1.35e-75 |
|
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: 233.69 E-value: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN-----------------------TV-IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGR 62
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkktgqTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 63 MFIDGEDVTD------RSIQQRDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQ 136
Cdd:cd03294 81 VLIDGQDIAAmsrkelRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIM 216
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|...
gi 757596975 217 QLGSPQELYRQPASRFMASFMGD 239
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRG 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-215 |
5.61e-74 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 228.00 E-value: 5.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD--- 79
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ---ICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPK 156
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQsEAFAVSDMVLVMNKGKI 215
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-230 |
5.71e-73 |
|
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: 226.22 E-value: 5.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGT----NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDI 80
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSY--ALFPHMSLGDNVGYGLKMLGLPkaEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-337 |
3.01e-72 |
|
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: 228.06 E-value: 3.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVidDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS------IQQRDICMVF 84
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSArgiflpPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKMLglPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANIFP 244
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 245 ATLT-HDSvnifNYHLPR----------PAQLATDNTEITVGVRPEAITLSLQ--GDDSQR----CTVTHV-AYMGPQYE 306
Cdd:COG4148 242 ATVAaHDP----DYGLTRlalgggrlwvPRLDLPPGTRVRVRIRARDVSLALEppEGSSILnilpGRVVEIePADGGQVL 317
|
330 340 350
....*....|....*....|....*....|....
gi 757596975 307 VTVDWHGQSMLLQI---NATQLQPTVGENLYLQI 337
Cdd:COG4148 318 VRLDLGGQTLLARItrrSADELGLAPGQTVYAQI 351
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-228 |
4.79e-72 |
|
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: 223.61 E-value: 4.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS-----IQQ 77
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-215 |
1.02e-71 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 222.02 E-value: 1.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ----QRDICM 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGL-KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-238 |
1.57e-71 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 221.94 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVidDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQSY 87
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSLGDNVGYGLKmlglPK----AEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:COG3840 81 NLFPHLTVAQNIGLGLR----PGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMG 238
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-236 |
3.93e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 224.57 E-value: 3.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ----- 77
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASF 236
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-214 |
1.26e-70 |
|
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: 218.88 E-value: 1.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMV 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQsyalFP-HMSLGDNVG----YGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:cd03225 81 FQ----NPdDQFFGPTVEeevaFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-215 |
2.85e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 216.07 E-value: 2.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN-TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD---RSIQQ--RDI 80
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrREIPYlrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 161 DEPLSNLDanlrRSMREKIRELQQQFN---ITSLYVTHDQSeafAVSDM---VLVMNKGKI 215
Cdd:COG2884 162 DEPTGNLD----PETSWEIMELLEEINrrgTTVLIATHDLE---LVDRMpkrVLELEDGRL 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-237 |
8.29e-69 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 215.34 E-value: 8.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDI----CM 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYG-LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFM 237
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-224 |
1.51e-67 |
|
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: 212.60 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVF 84
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-219 |
1.83e-65 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 206.59 E-value: 1.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF----GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD-----RSIQQ 77
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSY--ALFPHMSLGDNVGYGLKMLGLP--KAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALI 152
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-223 |
2.31e-65 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 205.41 E-value: 2.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP---TEGRMFIDGEDVTDRSIQQRDICMVF 84
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKMlGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:COG4136 83 QDDLLFPHLSVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVsdmvlvmnkGKIMQLGSPQE 223
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAA---------GRVLDLGNWQH 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-219 |
4.39e-65 |
|
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: 204.84 E-value: 4.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 14 KRFGTNTVidDLSLSIPqGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSI------QQRDICMVFQSY 87
Cdd:cd03297 8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKkinlppQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSLGDNVGYGLKmlGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd03297 85 ALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-227 |
6.12e-65 |
|
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: 205.48 E-value: 6.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVFQS 86
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-208 |
2.44e-64 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 204.71 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFG----TNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT----DRSIqqrd 79
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaDRGV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 icmVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG4525 81 ---VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA-FAVSDMVL 208
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAlFLATRLVV 207
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-227 |
3.15e-64 |
|
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: 204.59 E-value: 3.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS----IQQRdI 80
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweIRKK-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSyalfPhmslgDN----------VGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARA 150
Cdd:TIGR04520 80 GMVFQN----P-----DNqfvgatveddVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-224 |
5.47e-64 |
|
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: 202.41 E-value: 5.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEK-----PTEGRMFIDGEDVTDRSIQ----Q 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPhMSLGDNVGYGLKMLG-LPKAEIRKRVDEALELVDLAG-FADR-FVDQISGGQQQRVALARALILK 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-229 |
2.37e-63 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 204.20 E-value: 2.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRF---------GTNTV--IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGED 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 70 VTDRSIQQ-----RDICMVFQ-SYA-LFPHMSLGDNVGYGLKMLGL-PKAEIRKRVDEALELVDL-AGFADRFVDQISGG 140
Cdd:COG4608 82 ITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 141 QQQRVALARALILKPKVLLFDEPLSNLDAnlrrSMREKI----RELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIM 216
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDV----SIQAQVlnllEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250
....*....|...
gi 757596975 217 QLGSPQELYRQPA 229
Cdd:COG4608 238 EIAPRDELYARPL 250
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-229 |
2.59e-63 |
|
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: 201.81 E-value: 2.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS---IQQRDICMVF 84
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphrIARLGIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNV----------GYGLKMLGLPK-----AEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALAR 149
Cdd:COG0411 86 QNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPA 229
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-224 |
3.67e-63 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 201.05 E-value: 3.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT---DRSIQQ--RDI 80
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrGRALRRlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNV-----GY--GLK-MLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI 152
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVlagrlGRtsTWRsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 153 LKPKVLLFDEPLSNLD-ANLRRSMREkIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG3638 163 QEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-224 |
8.72e-62 |
|
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: 196.82 E-value: 8.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVFQ 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-215 |
2.47e-61 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 196.82 E-value: 2.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDrsiQQRDICMVFQSYA 88
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 LFPHMSLGDNVGYGLKmlglpkAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PRK11247 92 LLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 757596975 169 ANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
7-237 |
4.34e-61 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 196.20 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD-------------- 72
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 73 --RSIQQRdICMVFQSYALFPHMSLGDNVGYG-LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALAR 149
Cdd:TIGR03005 81 hlRQMRNK-IGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPA 229
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239
|
....*...
gi 757596975 230 SRFMASFM 237
Cdd:TIGR03005 240 EERTREFL 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-230 |
6.24e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 203.21 E-value: 6.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPT---EGRMFIDGEDVTDRSIQQR--D 79
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQS--YALFPhMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
1.94e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 194.15 E-value: 1.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ---- 76
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 -QRdicmvFQSYALFPhMSLGDNVGYGL----KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARAL 151
Cdd:COG1121 81 pQR-----AEVDWDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKImQLGSPQELYRQPA 229
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPEN 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-224 |
2.40e-60 |
|
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: 193.55 E-value: 2.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSI-----QQRDIC 81
Cdd:cd03256 2 EVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVGYGL--------KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALIL 153
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-235 |
5.64e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 196.18 E-value: 5.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ----- 77
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP----ASRFM 233
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREFI 241
|
..
gi 757596975 234 AS 235
Cdd:PRK11153 242 QS 243
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-228 |
5.85e-59 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 191.51 E-value: 5.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT-DRSIQQRDI 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 C----MVFQsyalFPHMSL-----GDNVGYGLKMLGLPKAEIRKRVDEALELVDL-AGFADR--FvdQISGGQQQRVALA 148
Cdd:TIGR04521 81 RkkvgLVFQ----FPEHQLfeetvYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERspF--ELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-229 |
7.58e-59 |
|
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: 192.58 E-value: 7.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP---TEGRMFIDGEDVTD------R 73
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 74 SIQQRDICMVFQ-SY-ALFPHMSLGDNVGYGLKM-LGLPKAEIRKRVDEALELVDL---AGFADRFVDQISGGQQQRVAL 147
Cdd:COG0444 82 KIRGREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
..
gi 757596975 228 PA 229
Cdd:COG0444 242 PR 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-229 |
1.83e-58 |
|
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: 188.80 E-value: 1.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMVF 84
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNV--------GYGLKMLGLPK--AEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILK 154
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartGSGLLLARARReeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPA 229
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-215 |
1.91e-58 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 186.45 E-value: 1.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVFQ 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYglkmlglpkaeirkrvdealelvdlagfadrfvdqiSGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 757596975 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-219 |
5.24e-58 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 187.91 E-value: 5.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDG------EDVTDRSIQQ--R 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRElrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALFPHMSLGDN-VGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-237 |
2.34e-57 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 185.99 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGE------DVTDRSIQQ--R 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALFPHMSLGDN-VGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSpQELYRQPASRFMASFM 237
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-215 |
3.04e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.94 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVFQ 85
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPhMSLGDNVGYGLKMLGLPKAeiRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-219 |
8.24e-56 |
|
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: 179.94 E-value: 8.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVFQ 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 syalfphmslgdnvgyglkmlglpkaeirkrvdeALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-214 |
3.99e-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: 3.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVI-DDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT---DRSIQQ--RDI 80
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAAlHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrGRQLPLlrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-224 |
1.68e-54 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 178.08 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFG--TNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-TDRSIQQRDICMV 83
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 164 LSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-235 |
7.43e-54 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 177.69 E-value: 7.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVtdRSIQQRD------- 79
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI--RLKPDRDgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ----------ICMVFQSYALFPHMSLGDNVGYG-LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALA 148
Cdd:COG4598 87 rrqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
250
....*....|.
gi 757596975 229 AS----RFMAS 235
Cdd:COG4598 246 KSerlrQFLSS 256
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-217 |
7.74e-54 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 176.18 E-value: 7.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDrsiQQRDICMVFQSY 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 AL---FPhMSLGDNVGYGL----KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQ 217
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-215 |
1.36e-53 |
|
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: 175.29 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTV-IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD---RSIQ--QRDI 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 161 DEPLSNLDANLRRsmreKIRELQQQFN---ITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03292 161 DEPTGNLDPDTTW----EIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-165 |
1.51e-53 |
|
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: 173.22 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVFQSYALFPHMSLGDNV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 100 GYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVD----QISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-225 |
2.15e-53 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 175.95 E-value: 2.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD---RSIQQ--RDI 80
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgKKLRKlrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGL--------KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI 152
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-286 |
5.27e-53 |
|
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: 178.38 E-value: 5.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVidDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDR------SIQQRDICMVF 84
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKMLGLPKAEIRKrvDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFM----ASFMGDA 240
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLaredQGSLIEG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 757596975 241 NIFPAT----LTHDSVNifNYHLPRPAQLATDNTEITVGVRPEAITLSLQ 286
Cdd:TIGR02142 240 VVAEHDqhygLTALRLG--GGHLWVPENLGPTGARLRLRVPARDVSLALQ 287
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-219 |
9.39e-53 |
|
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: 173.81 E-value: 9.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT----DRSIqqrdicmVFQSYALFPHMSLGD 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpDRMV-------VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 98 NVGYGLK--MLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
Cdd:TIGR01184 74 NIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 757596975 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
7-235 |
1.08e-52 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 174.99 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN---------TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSI 75
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 76 Q---QRDICMVFQ-SYALF-PHMSLGDNVGYGLK-MLGLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALA 148
Cdd:TIGR02769 83 RrafRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL--YR 226
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFK 242
|
....*....
gi 757596975 227 QPASRFMAS 235
Cdd:TIGR02769 243 HPAGRNLQS 251
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-219 |
2.12e-52 |
|
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: 172.08 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSiqQRDICMVFQS 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-242 |
2.15e-52 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 177.92 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 12 VTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD------RSIQQRDICMVFQ 85
Cdd:PRK10070 34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGDANI 242
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-225 |
3.82e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 173.76 E-value: 3.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNT---VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSI--QQRD 79
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSY-ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:PRK13650 83 IGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-214 |
4.11e-52 |
|
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: 169.73 E-value: 4.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDicmvfqsy 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 alfphmslgDNVGYglkmlglpkaeirkrvdealelvdlagfadrfVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd00267 73 ---------RRIGY--------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 757596975 168 DANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-224 |
1.69e-51 |
|
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: 181.57 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICM 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFpHMSLGDNVgyglkMLGLPKAEIrKRVDEALELVDLAGFADRFVD-----------QISGGQQQRVALARAL 151
Cdd:COG2274 554 VLQDVFLF-SGTIRENI-----TLGDPDATD-EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
7-231 |
2.68e-51 |
|
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: 170.55 E-value: 2.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGRMFIDGEDVTDRSIQ--- 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVR--IEGKVLFDGQDIYDKKIDvve 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 -QRDICMVFQSYALFPhMSLGDNVGYGLKMLGL-PKAEIRKRVDEALELVDL-AGFADRFVDQ---ISGGQQQRVALARA 150
Cdd:TIGR00972 80 lRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEVKDRLHDSalgLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKE 236
|
.
gi 757596975 231 R 231
Cdd:TIGR00972 237 K 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-219 |
4.21e-51 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 168.83 E-value: 4.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVidDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-217 |
8.34e-51 |
|
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: 168.77 E-value: 8.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---- 78
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 --DICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAeiRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPK 156
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQ 217
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-228 |
1.05e-50 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 169.45 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGRMFIDGEDVTDRSIQQ-- 77
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYDPDVDVve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 --RDICMVFQSYALFPhMSLGDNVGYGLKMLGL-PKAEIRKRVDEALELVDL----------AGFAdrfvdqISGGQQQR 144
Cdd:COG1117 90 lrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkdrlkkSALG------LSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 145 VALARALILKPKVLLFDEPLSNLD--ANLRrsMREKIRELQQQFNItsLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQ 222
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpiSTAK--IEELILELKKDYTI--VIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238
|
....*.
gi 757596975 223 ELYRQP 228
Cdd:COG1117 239 QIFTNP 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-247 |
1.48e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 169.48 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGT---------NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQ-- 76
Cdd:PRK10419 7 SGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 -QRDICMVFQSY--ALFPHMSLGDNVGYGLK-MLGLPKAEIRKRVDEALELVDLA-GFADRFVDQISGGQQQRVALARAL 151
Cdd:PRK10419 87 fRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQS--EAFAvsDMVLVMNKGKIM--QLGSPQELYRQ 227
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRlvERFC--QRVMVMDNGQIVetQPVGDKLTFSS 244
|
250 260
....*....|....*....|
gi 757596975 228 PASRFMASFMGDAniFPATL 247
Cdd:PRK10419 245 PAGRVLQNAVLPA--FPVRR 262
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-217 |
1.62e-50 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 168.72 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQrdiCMVFQSY 87
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEA-FAVSDMVLVM-NKGKIMQ 217
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAvFMATELVLLSpGPGRVVE 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-228 |
1.95e-50 |
|
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: 175.64 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 14 KRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTT----VLRLVaglekPTEGRMFIDGEDVTDRSIQQ-----RDICMVF 84
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRAlrplrRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QS-YA-LFPHMSLGDNVGYGLKML--GLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 160 FDEPLSNLDanlrRSMREKI----RELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:COG4172 449 LDEPTSALD----VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-227 |
1.97e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 169.84 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDI----CMVFQ--SYALFPHMSL 95
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDnVGYGLKMLGLPKAEIRKRVDEALELV--DLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
Cdd:PRK13637 103 KD-IAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-203 |
3.05e-50 |
|
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: 166.50 E-value: 3.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVFQ 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRkrVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITsLYVTHDQSEAFAV 203
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAV-LLTTHQPLELAAA 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-239 |
7.29e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 166.85 E-value: 7.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFI-DGEDVTDRSI--QQRDI--- 80
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIDTARSLsqQKGLIrql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 ----CMVFQSYALFPHMSLGDNVGYG-LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK11264 84 rqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELY---RQPASR- 231
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFadpQQPRTRq 242
|
....*...
gi 757596975 232 FMASFMGD 239
Cdd:PRK11264 243 FLEKFLLQ 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-215 |
1.37e-49 |
|
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: 165.08 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQS 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKaeirKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 757596975 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-231 |
1.34e-48 |
|
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: 163.10 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMV 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-227 |
1.60e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.90 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ-------Rd 79
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 icmvfqsyALFPHMSLGDNVGY--GLKmlGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:COG4152 81 --------GLYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 158 LLFDEPLSNLD---ANLrrsMREKIRELQQQfNITSLYVTH--DQSEAFAvsDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:COG4152 151 LILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEELC--DRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-227 |
1.83e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 164.42 E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 3 QHNFVELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--R 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSY-ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13635 82 QVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-219 |
1.19e-47 |
|
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: 160.23 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDIC 81
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-224 |
2.48e-47 |
|
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: 159.52 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMVF 84
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNvgygLKM--LGLPKAEIRKRVDEALELV-DLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03224 82 EGRRIFPELTVEEN----LLLgaYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-219 |
3.54e-47 |
|
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: 158.90 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGsMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD-ICMVFQ 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 166 NLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
9-215 |
1.90e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 157.19 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNT----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD----- 79
Cdd:NF038007 4 MQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrre 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 -ICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:NF038007 84 lIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQsEAFAVSDMVLVMNKGKI 215
Cdd:NF038007 164 LADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-227 |
2.20e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 165.72 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMV 83
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFpHMSLGDNVGYglkmlGLPKAEiRKRVDEALELVDLAGFADRFVD-----------QISGGQQQRVALARALI 152
Cdd:COG1132 420 PQDTFLF-SGTIRENIRY-----GRPDAT-DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQS---EAfavsDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLStirNA----DRILVLDDGRIVEQGTHEELLAR 564
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-230 |
4.60e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 156.67 E-value: 4.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 26 SLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQSYALFPHMSLGDNVGYGLKM 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 106 lGLP-KAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQ 184
Cdd:PRK10771 99 -GLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 757596975 185 QFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-214 |
5.76e-46 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 154.08 E-value: 5.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD---RSIQQRdIC 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldlESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFpHMSLGDNVgyglkmlglpkaeirkrvdealelvdlagfadrfvdqISGGQQQRVALARALILKPKVLLFD 161
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAfAVSDMVLVMNKGK 214
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-219 |
9.87e-46 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 155.02 E-value: 9.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 26 SLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQSYALFPHMSLGDNVGYGLKM 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 106 LGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQ 185
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 757596975 186 FNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-227 |
1.26e-45 |
|
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: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICMV 83
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFpHMSLGDNVgyglkMLGLPKAEiRKRVDEALELVDLAGFADRFVDQI-----------SGGQQQRVALARALI 152
Cdd:COG4988 417 PQNPYLF-AGTIRENL-----RLGRPDAS-DEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-197 |
1.54e-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: 154.31 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD------RSIQQRDICM 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnskkaSKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQ 197
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-224 |
9.23e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 154.38 E-value: 9.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGT--NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICM 82
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSY-ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFaVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-228 |
9.82e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 153.84 E-value: 9.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGRMFIDGEDVTDRSIQ----Q 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpievR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKMLGL--PKAEIRKRVDEALELVDL-AGFADRFVD---QISGGQQQRVALARAL 151
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
3.32e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 152.98 E-value: 3.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-- 76
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 QRDICMVFQS-YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-229 |
4.63e-44 |
|
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: 159.16 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICM 82
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFpHMSLGDNVgyglkMLGLPKA---EIRkrvdEALELVDLAGFADRFVD-----------QISGGQQQRVALA 148
Cdd:COG4987 414 VPQRPHLF-DTTLRENL-----RLARPDAtdeELW----AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVsDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 757596975 229 A 229
Cdd:COG4987 561 G 561
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-231 |
1.39e-43 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 151.46 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--- 77
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 --RDICMVFQSYALFPHMSLGDNVGYGLK-MLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILK 154
Cdd:PRK11831 82 vrKRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-224 |
1.97e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 150.23 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVF 84
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGL----KmlGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-231 |
2.50e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.79 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DIcmvf 84
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 qSY-----ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG1137 81 -GYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 160 FDEPLSNLD----ANLRRSmrekIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:COG1137 160 LDEPFAGVDpiavADIQKI----IRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-229 |
2.63e-43 |
|
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: 149.36 E-value: 2.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMVF 84
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNvgygLKM---LGLPKAEIRKRVDEALELV-DLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:COG0410 85 EGRRIFPSLTVEEN----LLLgayARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPA 229
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-240 |
6.00e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 149.35 E-value: 6.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 3 QHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-----TDRSIQQ 77
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RD----------ICMVFQSYALFPHMSLGDNVGYG-LKMLGLPKAEIRKRVDEALELVDLAGFA-DRFVDQISGGQQQRV 145
Cdd:PRK10619 82 ADknqlrllrtrLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 146 ALARALILKPKVLLFDEPLSNLDANLrrsMREKIRELQQ--QFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPEL---VGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
250
....*....|....*..
gi 757596975 224 LYRQPASRFMASFMGDA 240
Cdd:PRK10619 239 LFGNPQSPRLQQFLKGS 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-228 |
7.53e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 150.89 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQ---RDICMVFQS-YA-LFPHMS 94
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkaDPEAQKllrQKIQIVFQNpYGsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGYGLKM-LGLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:PRK11308 111 VGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-228 |
8.24e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 148.91 E-value: 8.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGRMFIDGEDV--TDRSIQQ 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKM--LGLPKAEIRKRVDEALELVDL-AGFADRF---VDQISGGQQQRVALARAL 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
8-228 |
9.35e-43 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 148.83 E-value: 9.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNT---------VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR 78
Cdd:COG4167 6 EVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 --DICMVFQ--SYALFPHMSLGdnvgyglKMLGLP--------KAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRV 145
Cdd:COG4167 86 ckHIRMIFQdpNTSLNPRLNIG-------QILEEPlrlntdltAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
...
gi 757596975 226 RQP 228
Cdd:COG4167 239 ANP 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-210 |
1.02e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.41 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSI---QQRDICM 82
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNV--GYGLKMLGL-PKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:COG1129 84 IHQELNLVPNLSVAENIflGREPRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVM 210
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-227 |
1.23e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 149.08 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTN------TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS---- 74
Cdd:PRK13633 3 EMIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 75 IQQRdICMVFQSyalfPHMSL-----GDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALAR 149
Cdd:PRK13633 83 IRNK-AGMVFQN----PDNQIvativEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-215 |
2.07e-42 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 144.88 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSiqqrdicmvfqs 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 yalfphmslgdnvgyglkmlglPKAEIRKRVdealelvdlagfadRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03216 69 ----------------------PRDARRAGI--------------AMVYQLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 757596975 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-223 |
1.05e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 146.03 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICM-VF-Q 85
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRaVLpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYAL-FPhMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI-------LKPKV 157
Cdd:COG4559 83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 158 LLFDEPLSNLD-ANLRRSMReKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:COG4559 162 LFLDEPTSALDlAHQHAVLR-LARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-215 |
1.61e-41 |
|
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: 143.94 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSiQQRDICMVFQS 86
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 --YALFPHmSLGDNVGYGLKMLGLPKAEIRkrvdEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 165 SNLDanlRRSMR---EKIRELQQQFNiTSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03226 155 SGLD---YKNMErvgELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-225 |
1.69e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 146.01 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 4 HNFVELKNVTKRFGTNTVIDDL---SLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QR 78
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSY-ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-223 |
1.74e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 145.30 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDicmvfQSY 87
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA-----RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFP-HMSLG------DNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI------LK 154
Cdd:PRK13548 79 AVLPqHSSLSfpftveEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 155 PKVLLFDEPLSNLDanLR---RSMReKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:PRK13548 159 PRWLLLDEPTSALD--LAhqhHVLR-LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-228 |
2.05e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 146.10 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP---TEGRMFIDGEDVTDRSIQQ-R 78
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDiR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 D-ICMVFQSY-ALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPK 156
Cdd:PRK13640 84 EkVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-228 |
6.53e-41 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 146.00 E-value: 6.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR-----DICMVFQS--YALFPHMS 94
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGYGLKML--GLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK15079 117 IGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-227 |
9.51e-41 |
|
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: 142.75 E-value: 9.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFG--TNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICM 82
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFpHMSLGDNVGYglkmlGLPKAEiRKRVDEALELVDLAGFADRFVD-----------QISGGQQQRVALARAL 151
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY-----GRPGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-224 |
1.33e-40 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 142.92 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEG-RMFI-----DGEDVTDrsIQQRd 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWE--LRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVfqSYALF----PHMSLGDNVGYGL-KMLGL---PKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARAL 151
Cdd:COG1119 80 IGLV--SPALQlrfpRDETVLDVVLSGFfDSIGLyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
10-215 |
2.82e-40 |
|
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: 141.33 E-value: 2.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-----TDRS-IQQRD 79
Cdd:TIGR02211 5 ENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklssNERAkLRNKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKI 215
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEMKDGQL 219
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
7-215 |
4.31e-40 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 140.54 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV---TDRSIQQ-- 77
Cdd:TIGR02982 2 ISIRNLNHYYGHGSlrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaSKKQLVQlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKML-GLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPK 156
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDqSEAFAVSDMVLVMNKGKI 215
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-224 |
4.43e-40 |
|
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: 141.21 E-value: 4.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTkrFGTNT---VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVtdRSIQQ----RD 79
Cdd:cd03253 1 IEFENVT--FAYDPgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLdslrRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYALFpHMSLGDNVGYGlkMLGLPKAEIRkrvdEALELVDLAGFADRFVDQ-----------ISGGQQQRVALA 148
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIRYG--RPDATDEEVI----EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
8.82e-40 |
|
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: 147.14 E-value: 8.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKT----TVLRLVAGLEKPTEGRMFIDGEDVTD 72
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 73 ------RSIQQRDICMVFQ--SYALFPHMSLGDNVGYGLKM-LGLPKAEIRKRVDEALELV---DLAGFADRFVDQISGG 140
Cdd:COG4172 81 lserelRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVgipDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDqseaFAV----SDMVLVMNKGKIM 216
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIV 236
|
250
....*....|...
gi 757596975 217 QLGSPQELYRQPA 229
Cdd:COG4172 237 EQGPTAELFAAPQ 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-214 |
8.84e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.01 E-value: 8.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSiqQRD-----IC 81
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS--PRDaialgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVGYGL---KMLGLPKAEIRKRVDEALEL----VDLagfaDRFVDQISGGQQQRVALARALILK 154
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERygldVDP----DAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 155 PKVLLFDEPLSNLD--------ANLRRsMREKirelqqqfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:COG3845 160 ARILILDEPTAVLTpqeadelfEILRR-LAAE--------GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-223 |
1.38e-38 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 137.84 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQrdicmVFQS 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFP--HM-----SLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK11231 78 LALLPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-229 |
1.89e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 138.23 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIdGEDVTDRSIQQRD-- 79
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 -----ICMVFQ--SYALFPHMSLGDnVGYGLKMLGLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARAL 151
Cdd:PRK13634 82 plrkkVGIVFQfpEHQLFEETVEKD-ICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPA 229
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-224 |
3.49e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.01 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD-ICMVFQ 85
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-234 |
5.74e-38 |
|
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: 135.35 E-value: 5.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMVF 84
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKmlGLPKAEiRKRVDEALELVD-LAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLA--ALPRRS-RKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMA 234
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-215 |
1.53e-37 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 132.34 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFG--TNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTdrsiqqrdicmvfq 85
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALfphMSLGDNVGYglkmlgLPKaeirkrvDEALelvdlagFADRFVDQI-SGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:cd03246 68 QWDP---NELGDHVGY------LPQ-------DDEL-------FSGSIAENIlSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 165 SNLDANLRRSMREKIRELQQQfNITSLYVTHdQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
10-231 |
1.53e-37 |
|
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: 134.71 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMVFQS 86
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLG-LPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 166 NLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVR 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-283 |
2.03e-37 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 138.44 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMV 83
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRfmASFmgD 239
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR--AAF--D 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 757596975 240 ANIF----PATlthDSVNIFNYHLPRPAQLATDNTEITVGVRPEAITL 283
Cdd:PRK09536 238 ARTAvgtdPAT---GAPTVTPLPDPDRTEAAADTRVHVVGGGQPAARA 282
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-227 |
3.21e-37 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 133.82 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGT---NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDIC 81
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPhMSLGDNVGYglkmlGLPKAEiRKRVDEALELVDLAGFADRFVD-----------QISGGQQQRVALARA 150
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRY-----GKPDAT-DEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-237 |
4.45e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.02 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGE------DV--TDRSIQQRDICMVFQSYALFPH 92
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIfqIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 93 MSLGDNVGYGLKMLGLP-KAEIRKRVDEALELVDL-AGFADRF---VDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 168 DANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFM 237
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-216 |
8.16e-37 |
|
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: 132.46 E-value: 8.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKR-FGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVF-Q 85
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIM 216
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-215 |
1.22e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 131.56 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDICM 82
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFpHMSLGDNVgyglkMLGLPKAEIRkRVDEALELVDLAGFA-------DRFV----DQISGGQQQRVALARAL 151
Cdd:cd03245 83 VPQDVTLF-YGTLRDNI-----TLGAPLADDE-RILRAAELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSeAFAVSDMVLVMNKGKI 215
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
1.32e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.43 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGE--DVTDRSIQQ--RD 79
Cdd:PRK13636 4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKlrES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQS--YALFPhMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13636 84 VGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-228 |
1.32e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 133.28 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT-DRS--IQQRD-IC 81
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKslLEVRKtVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSY--ALF-PhmSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:PRK13639 82 IVFQNPddQLFaP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-199 |
1.42e-36 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 131.76 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT----DRSIQ 76
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 QRDICmvFQSYALFphmslGDNVGYGLKmlgLPkAEIR-KRVDEALELVDLAGFA------DRFVDQISGGQQQRVALAR 149
Cdd:PRK10247 82 QVSYC--AQTPTLF-----GDTVYDNLI---FP-WQIRnQQPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSE 199
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-231 |
1.54e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 135.00 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVidDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS------IQQRDICMVF 84
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKmlglpkaeiRKRVDEALELVDLAGFA---DRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK11144 83 QDARLFPHYKVRGNLRYGMA---------KSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-228 |
4.84e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 131.31 E-value: 4.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGRMFIDGEDVTDRSIQ----Q 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNlnrlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPhMSLGDNVGYGLKMLGL-PKAEIRKRVDEALELVDLAGFADRFVDQ----ISGGQQQRVALARALI 152
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVM--NKGKIMQL---GSPQELYRQ 227
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTKKIFNS 246
|
.
gi 757596975 228 P 228
Cdd:PRK14258 247 P 247
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-230 |
5.42e-36 |
|
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: 130.18 E-value: 5.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP----TEGRMFIDGEDVTDRSIQQRDICMVFQS--YALFPHMSL 95
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFA---DRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-215 |
7.83e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 129.61 E-value: 7.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT---DRSIQ--QRDI 80
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 161 DEPLSNLDANLrrsmREKIRELQQQFN---ITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK10908 162 DEPTGNLDDAL----SEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-224 |
1.93e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 129.86 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDIC 81
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSY--ALFPhMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK13647 83 LVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-225 |
3.00e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 129.36 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 15 RFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGE--DVTDRSIQ--QRDICMVFQ--SYA 88
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLalRQQVATVFQdpEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 LFpHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PRK13638 90 IF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 169 ANLRRSMREKIRELQQQFNITSLyVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-224 |
4.06e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 130.21 E-value: 4.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ-QRDICMVF-QSYALFPHMSLGDNv 99
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEfARRIGVVFgQRSQLWWDLPAIDS- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 100 gygLKML----GLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
Cdd:COG4586 117 ---FRLLkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 757596975 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:COG4586 194 REFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-223 |
5.72e-35 |
|
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: 134.99 E-value: 5.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 4 HNFVELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRD 79
Cdd:TIGR03375 461 QGEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPADLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYALFpHMSLGDNVgyglkMLGLPKAEirkrvDEA-LELVDLAGfADRFVDQ---------------ISGGQQQ 143
Cdd:TIGR03375 541 IGYVPQDPRLF-YGTLRDNI-----ALGAPYAD-----DEEiLRAAELAG-VTEFVRRhpdgldmqigergrsLSGGQRQ 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKDQ 685
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-210 |
6.45e-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: 133.57 E-value: 6.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDICMV 83
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHmSLGDNVGYGLKmlGLPKAEIRkrvdEALELVDLAGFA-------DRFVDQ----ISGGQQQRVALARALI 152
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARP--DASDAEIR----EALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAfAVSDMVLVM 210
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-219 |
1.06e-34 |
|
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: 126.49 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF----------------------GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMF 64
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 65 IDGedvtdrsiqqRDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQR 144
Cdd:cd03220 81 VRG----------RVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-233 |
1.11e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 128.18 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ---RDICM 82
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQS-YALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEaFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFM 233
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-227 |
1.47e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 126.73 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHnfVELKNVTKRF----------------------GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP 58
Cdd:COG1134 1 MSSM--IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 59 TEGRMFIDGEdVTdrsiqqrdicmvfqsyALF-------PHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFAD 131
Cdd:COG1134 79 TSGRVEVNGR-VS----------------ALLelgagfhPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 132 RFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMN 211
Cdd:COG1134 142 QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|....*....
gi 757596975 212 KGKIMQLGSPQE---LYRQ 227
Cdd:COG1134 221 KGRLVMDGDPEEviaAYEA 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-240 |
2.01e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 126.64 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV---TDRSIQQRDICMVF 84
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglPGHQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMS------------LGDNVGYGL-KMLGLPKAEiRKRVDEA---LELVDLAGFADRFVDQISGGQQQRVALA 148
Cdd:PRK11300 87 QHVRLFREMTvienllvaqhqqLKTGLFSGLlKTPAFRRAE-SEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
250
....*....|..
gi 757596975 229 asRFMASFMGDA 240
Cdd:PRK11300 246 --DVIKAYLGEA 255
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-211 |
8.26e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 125.28 E-value: 8.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGRMFIDGEDVTDRSIQ--- 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPDVDpve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 -QRDICMVFQSYALFPHmSLGDNVGYGLKMLGLpKAEIRKRVDEALELvdlAGFADRFVDQI-------SGGQQQRVALA 148
Cdd:PRK14243 89 vRRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQ---AALWDEVKDKLkqsglslSGGQQQRLCIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDMVLVMN 211
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFN 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-228 |
1.04e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.69 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMV 83
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSY--ALFPhMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PRK13652 84 FQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
1.27e-33 |
|
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: 129.92 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-----GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFI----DGEDVTDRSIQQ 77
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RD-----ICMVFQSYALFPHMSLGDNVGYGLKmLGLPKaEIRKRvdEALELVDLAGFA--------DRFVDQISGGQQQR 144
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLTEAIG-LELPD-ELARM--KAVITLKMVGFDeekaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 757596975 225 YRQ 227
Cdd:TIGR03269 516 VEE 518
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-224 |
2.39e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 126.10 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS-IQQRDICMVFQ 85
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDN-VGYGlKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK13536 122 FDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 165 SNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-228 |
2.87e-33 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 130.08 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICM 82
Cdd:TIGR03797 452 IEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHmSLGDNVGYGLKMlglpkaeirkRVDEALELVDLAGFAD----------RFVDQ----ISGGQQQRVALA 148
Cdd:TIGR03797 532 VLQNGRLMSG-SIFENIAGGAPL----------TLDEAWEAARMAGLAEdirampmgmhTVISEgggtLSGGQRQRLLIA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELqqqfNITSLYVTHDQS---EAfavsDMVLVMNKGKIMQLGSPQELY 225
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLStirNA----DRIYVLDAGRVVQQGTYDELM 672
|
...
gi 757596975 226 RQP 228
Cdd:TIGR03797 673 ARE 675
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-200 |
1.47e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.03 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 15 RFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEdvtdrsiqqRDICMVFQSYAL---FP 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 92 hMSLGDNVGYGL----KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|...
gi 757596975 168 DANLRRSMREKIRELQQQfNITSLYVTHDQSEA 200
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
7-240 |
1.59e-32 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 122.21 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT---------VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSI 75
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 76 QQRDICMVFQ--SYALFPHMSLGDNVGYGLKM-LGLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARAL 151
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP--- 228
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhe 244
|
250
....*....|...
gi 757596975 229 -ASRFMASFMGDA 240
Cdd:PRK15112 245 lTKRLIAGHFGEA 257
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-224 |
1.72e-32 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 120.79 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICM 82
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHmSLGDNVgyglkMLGLPKAEiRKRVDEALELVDlagfADRFVDQ---------------ISGGQQQRVAL 147
Cdd:cd03254 82 VLQDTFLFSG-TIMENI-----RLGRPNAT-DEEVIEAAKEAG----AHDFIMKlpngydtvlgenggnLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-227 |
5.05e-32 |
|
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: 119.90 E-value: 5.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV--TDRSIQQRDICM 82
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFpHMSLGDNVGyglkmLGLPKAEIRkRVDEALELVDLAGFADRF---VDQI--------SGGQQQRVALARAL 151
Cdd:cd03252 81 VLQENVLF-NRSIRDNIA-----LADPGMSME-RVIEAAKLAGAHDFISELpegYDTIvgeqgaglSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-239 |
1.96e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 119.43 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--------QRDICM 82
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlefRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPhMSLGDNVGYGLKMLGL-PKAEIRKRVDEALELVDL-AGFADRFVD---QISGGQQQRVALARALILKPKV 157
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP----ASRFM 233
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYV 262
|
....*.
gi 757596975 234 ASFMGD 239
Cdd:PRK14271 263 AGLSGD 268
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-229 |
4.87e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.57 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFI---------DGEDVTD 72
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 73 RSIQQ---------RDICMVFQ--SYALFPHmSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDL-AGFADRFVDQISGG 140
Cdd:PRK13631 102 NPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGS 220
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*....
gi 757596975 221 PQELYRQPA 229
Cdd:PRK13631 260 PYEIFTDQH 268
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
7-227 |
9.00e-31 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 122.93 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT--VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV--TDRSIQQRDICM 82
Cdd:TIGR01846 456 ITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiADPAWLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHmSLGDNVGygLKMLGLPKAEIR--KRVDEALELVDL--AGFADRFVDQ---ISGGQQQRVALARALILKP 155
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIA--LCNPGAPFEHVIhaAKLAGAHDFISElpQGYNTEVGEKganLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLAL 681
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-224 |
1.43e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 116.65 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL---EKPTEGRMFIDGEDVTDRSIQQRDI--- 80
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 ----CMVFQSYALFPHMSLGDNVGYGlkMLGLP----------KAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVA 146
Cdd:PRK09984 85 rantGYIFQQFNLVNRLSVLENVLIG--ALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-231 |
7.26e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGRMFIDGEDV----TDRSIQQ 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPhMSLGDNVGYGLKMLGLPKAEIrkrVDEALElVDLAGFA------DRFVDQ---ISGGQQQRVALA 148
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVE-KSLKGASiwdevkDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFniTSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
...
gi 757596975 229 ASR 231
Cdd:PRK14239 239 KHK 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-215 |
1.58e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 111.75 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRfgtnTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD---ICMV 83
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 ---FQSYALFPHMSLGDNvgyglkmLGLPkaeirkrvdealelvdlagfadrfvDQISGGQQQRVALARALILKPKVLLF 160
Cdd:cd03215 81 pedRKREGLVLDLSVAEN-------IALS-------------------------SLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-227 |
1.83e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.07 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVID-----DLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS----IQQ 77
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 --RDICMVFQ--SYALFPHMSLGDnVGYGLKMLGLPKAEIRKRVDEALELVdlaGFADRFVDQ----ISGGQQQRVALAR 149
Cdd:PRK13649 83 irKKVGLVFQfpESQLFEETVLKD-VAFGPQNFGVSQEEAEALAREKLALV---GISESLFEKnpfeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-196 |
2.33e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.60 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS------IQQRDICMVFQSYALFPHMS 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaeLRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|..
gi 757596975 175 MREKIRELQQQFNITSLYVTHD 196
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHD 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-227 |
3.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.72 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD-------RSIQQRdICMVFQsyalFPHMS 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyiRPVRKR-IGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 L-GDNVG----YGLKMLGLPKAEIRkrvDEALELVDLAGFADRFVD----QISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK13646 98 LfEDTVEreiiFGPKNFKMNLDEVK---NYAHRLLMDLGFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-230 |
9.29e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRF----GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD------RSIQQ 77
Cdd:PRK10535 6 ELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK10535 86 EHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAfAVSDMVLVMNKGKIMQlGSPQELYRQPAS 230
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIVR-NPPAQEKVNVAG 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-228 |
1.52e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.36 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGT---NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDIC 81
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHmSLGDNVGYGLKMLglPKAEIRKRVDEAlelvdlagFADRFV---------------DQISGGQQQRVA 146
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLTDT--PDEEIMAAAKAA--------NAHDFImefpngydtevgekgSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSmrekIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYR 226
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 757596975 227 QP 228
Cdd:TIGR00958 703 DQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-227 |
1.63e-28 |
|
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: 116.07 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVtkRFGTN---TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVtdRSIQQ----RD 79
Cdd:COG5265 358 VRFENV--SFGYDperPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDVTQaslrAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYALFpHMSLGDNVGYGlkMLGLPKAEIRkrvdEALELVDLAGFADRFVDQI-----------SGGQQQRVALA 148
Cdd:COG5265 434 IGIVPQDTVLF-NDTIAYNIAYG--RPDASEEEVE----AAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQS---EAfavsDMVLVMNKGKIMQLGSPQELY 225
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStivDA----DEILVLEAGRIVERGTHAELL 580
|
..
gi 757596975 226 RQ 227
Cdd:COG5265 581 AQ 582
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-223 |
2.41e-28 |
|
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: 115.23 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 17 GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDICMVFQSYALFPHmS 94
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGyglkMLGLPKAEirkRVDEALELVDLAGFADRFVD-----------QISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:COG4618 422 IAENIA----RFGDADPE---KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-224 |
2.91e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.98 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR---DICMVFQS 86
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGLPKAEIRK-RVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 166 NLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK10895 167 GVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-236 |
3.26e-28 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 110.20 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGrmfidgedVTDRSIQQRdICMVF 84
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKRNGKLR-IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLgdNVGYGLKML-GLPKAEIRKrvdeALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:PRK09544 74 QKLYLDTTLPL--TVNRFLRLRpGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNkGKIMQLGSPQELYRQPasRFMASF 236
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-219 |
3.27e-28 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 109.28 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL---EKPTEGRMFIDGEDVtDRSIQQRDICMVFQSYALFPHMSLGD 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 98 NVGYGLKMLG---LPKAEIRKRV-DEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
Cdd:cd03234 101 TLTYTAILRLprkSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 757596975 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-223 |
6.42e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 110.56 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRM---FIDGED--------- 69
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 70 -VTDRSIQ-------------QRDICMVFQ--SYALFPHMSLGDnVGYGLKMLGLPKAEIRKRVDEALELVDL-AGFADR 132
Cdd:PRK13651 83 vLEKLVIQktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIEKD-IIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 133 FVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNK 212
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|.
gi 757596975 213 GKIMQLGSPQE 223
Cdd:PRK13651 241 GKIIKDGDTYD 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-170 |
6.47e-28 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 107.83 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-TDRSIQQRDICMVFQS 86
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGLKMLGlpkaEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
....
gi 757596975 167 LDAN 170
Cdd:TIGR01189 158 LDKA 161
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-224 |
7.53e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 109.69 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVFQSY 87
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:PRK10253 91 TTPGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-196 |
7.58e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGeDVTdrsiqqrdICMVFQSYA 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR--------IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 LFPHMSLGDNVGYGLKMLGLPKAEIRK-------------RVDEALELVD--------------LAGF------ADRFVD 135
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedleRLAELQEEFEalggweaearaeeiLSGLgfpeedLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsMREKIRELQQQFNITSLYVTHD 196
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE----SIEWLEEFLKNYPGTVLVVSHD 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-200 |
8.49e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 108.33 E-value: 8.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ 76
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 QR------DICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARA 150
Cdd:PRK10584 81 ARaklrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA 200
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-227 |
9.43e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.82 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 24 DLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ------RDICMVFQ--SYALFPHMSL 95
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQfpESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDnVGYGLKMLGLPKAEIRKRVDEALELVDLAG-FADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
Cdd:PRK13643 104 KD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 175 MReKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK13643 183 MM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-236 |
1.55e-27 |
|
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: 112.59 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLE--KPTEGRM--------------------- 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 64 ---------------FIDGEDVTDRSIQQRDICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAG 128
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 129 FADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVL 208
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*...
gi 757596975 209 VMNKGKIMQLGSPQELyrqpASRFMASF 236
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV----VAVFMEGV 264
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-228 |
1.70e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 108.72 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICMVFQS 86
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YALFPHMSLGDNVGYGL----KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK10575 94 LPAAEGMTVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-222 |
1.91e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.59 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 20 TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFI-DGEDvtdrsiqqrdicMVF---QSYalFPHMSL 95
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR------------VLFlpqRPY--LPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDNVGYGLKMLGLPKAEIRkrvdEALELVDLAGFADRFvDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:COG4178 443 REALLYPATAEAFSDAELR----EALEAVGLGHLAERL-DEEadwdqvlSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 169 ANLRRSMREKIRElqQQFNITSLYVTHdQSEAFAVSDMVLVMNKGKIMQLGSPQ 222
Cdd:COG4178 518 EENEAALYQLLRE--ELPGTTVISVGH-RSTLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-215 |
3.09e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIdGEDVTdrsI----QQRDicm 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---IgyfdQHQE--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 vfqsyALFPHMSLGDNVGYGLKmlGLPKAEIRKRvdealelvdLAGF------ADRFVDQISGGQQQRVALARALILKPK 156
Cdd:COG0488 389 -----ELDPDKTVLDELRDGAP--GGTEQEVRGY---------LGRFlfsgddAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 157 VLLFDEPLSNLDANlrrsMREKIRELQQQFNITSLYVTHDqsEAF--AVSDMVLVMNKGKI 215
Cdd:COG0488 453 VLLLDEPTNHLDIE----TLEALEEALDDFPGTVLLVSHD--RYFldRVATRILEFEDGGV 507
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-237 |
3.76e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 112.26 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV---TDRSIQ--QRDICMVFQS-YA-LFPHMS 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQalRRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGYGLKMLGLPKAE-IRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFM 237
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-214 |
4.51e-27 |
|
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: 104.07 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGedvtdrsiqqrdicmvfqs 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 yalfphmslGDNVGYglkmlglpkaeirkrvdealelvdlagfadrfVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
Cdd:cd03221 62 ---------TVKIGY--------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 757596975 167 LDANlrrsMREKIRELQQQFNITSLYVTHDQseAF--AVSDMVLVMNKGK 214
Cdd:cd03221 101 LDLE----SIEALEEALKEYPGTVILVSHDR--YFldQVATKIIELEDGK 144
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-196 |
4.52e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 111.30 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 3 QHNFVELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRD 79
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSslDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYALFpHMSLGDNVgyglkMLGLPKA---EIRkrvdEALELVDLAGFADRFVD-----------QISGGQQQRV 145
Cdd:TIGR02868 411 VSVCAQDAHLF-DTTVRENL-----RLARPDAtdeELW----AALERVGLADWLRALPDgldtvlgeggaRLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFniTSLYVTHD 196
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-227 |
4.96e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.14 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSiQQRDICmvfQS 86
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR-HRRAVC---PR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 87 YA---------LFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTH---DQSEAFavsDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATaymEEAERF---DWLVAMDAGRVLATGTPAELLAR 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-224 |
5.12e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 106.69 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEK--PTEGRMFIDGEDVTDRSIQQR---DICM 82
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGD--NVGYGLKMLGLPKA-EIRKRVDEALELVDLA-GFADRFVDQ-ISGGQQQRVALARALILKPKV 157
Cdd:COG0396 82 AFQYPVEIPGVSVSNflRTALNARRGEELSArEFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQS-EAFAVSDMVLVMNKGKIMQLGSPqEL 224
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRiLDYIKPDFVHVLVDGRIVKSGGK-EL 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-237 |
7.37e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.21 E-value: 7.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICMV 83
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFpHMSLGDNVgyglkMLGLPKA---EIRkrvdEALELVDLAGFADRFVD-----------QISGGQQQRVALAR 149
Cdd:PRK13657 415 FQDAGLF-NRSIEDNI-----RVGRPDAtdeEMR----AAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQS---EAfavsDMVLVMNKGKIMQLGSPQELYr 226
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLStvrNA----DRILVFDNGRVVESGSFDELV- 557
|
250
....*....|....*
gi 757596975 227 QPASRFM----ASFM 237
Cdd:PRK13657 558 ARGGRFAallrAQGM 572
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-215 |
1.46e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRfgtnTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ---RDICMV- 83
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 --FQSYALFPHMSLGDNVGYG-LKMLG----LPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:COG1129 334 edRKGEGLVLDLSIRENITLAsLDRLSrgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-215 |
1.83e-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: 103.78 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTnTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL--EKPTEGRMFIDGEDVTDRSIQQRdICMVF 84
Cdd:cd03213 11 VTVKSSPSKSGK-QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGLKMLGlpkaeirkrvdealelvdlagfadrfvdqISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 165 SNLDANLRRSMREKIRELQQQfNITSLYVTHD-QSEAFAVSDMVLVMNKGKI 215
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-228 |
1.89e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTV-----IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT----DRSIQ- 76
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 -QRDICMVFQsyalFPHMSLGDN-----VGYGLKMLGLPKAEIRkrvDEALELVDLAGFADRFVD----QISGGQQQRVA 146
Cdd:PRK13641 83 lRKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAK---EKALKWLKKVGLSEDLISkspfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYR 226
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
..
gi 757596975 227 QP 228
Cdd:PRK13641 235 DK 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-232 |
2.23e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 17 GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTT----VLRLVAglekpTEGRMFIDGEDVTDRSIQQ-----RDICMVFQ-- 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKM--LGLPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRF 232
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-225 |
6.33e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNT-----VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIdGEDVTDRSIQQ------ 77
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKikevkr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 --RDICMVFQ--SYALFPHmSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLA-GFADRFVDQISGGQQQRVALARALI 152
Cdd:PRK13645 88 lrKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-215 |
9.81e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 102.93 E-value: 9.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT---VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDIC 81
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHmSLGDNVGYGLKmlGLPKAEIRKRVDEALELVDLAGFADRFVD-------QISGGQQQRVALARALILK 154
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKI 215
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-228 |
1.16e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 107.62 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 25 LSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLeKPTEGRMFIDGEDVTDRSIQQ--RDICMVFQSYALFpHMSLGDNVgyg 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 103 lkMLGLPKAEiRKRVDEALELVDLAGFADRFV--------DQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK11174 444 --LLGNPDAS-DEQLQQALENAWVSEFLPLLPqgldtpigDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 172 -RRSMREKIRELQQQfniTSLYVTHdQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK11174 521 eQLVMQALNAASRRQ---TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-214 |
1.42e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.94 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLeKPT---EGRMFIDGEDVTDRSI---QQRDIC 81
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIrdtERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVgyglkMLGlpkAEIRK-----------RVDEALELVDLAGFADRFVDQISGGQQQRVALARA 150
Cdd:PRK13549 86 IIHQELALVKELSVLENI-----FLG---NEITPggimdydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-224 |
1.56e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 107.52 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDICMV 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdiDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHmSLGDNVGYGLKmlglPKAEIRKrVDEALELVDLA--------GFADRFVDQ---ISGGQQQRVALARALI 152
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK----ENVSQDE-IWAACEIAEIKddienmplGYQTELSEEgssISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfniTSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-227 |
2.44e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 107.13 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD-ICMVFQ 85
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRrVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-170 |
5.50e-25 |
|
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: 100.26 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTdrsiQQRDIcmVFQSY 87
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----FQRDS--IARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSlgdnvgyGLKMLGLPKAEIR--------KRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:cd03231 76 LYLGHAP-------GIKTTLSVLENLRfwhadhsdEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170
....*....|.
gi 757596975 160 FDEPLSNLDAN 170
Cdd:cd03231 149 LDEPTTALDKA 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-196 |
5.74e-25 |
|
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: 105.40 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIdGEDVTDRSI-QQRDicmvfq 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVdQSRD------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 syALFPHMSLGDNVGYGLKMLGLPKAEIRKRVdealeLVDLAGF--AD--RFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:TIGR03719 396 --ALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFkgSDqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190
....*....|....*....|....*....|....*
gi 757596975 162 EPLSNLDANLRRSMREKIRElqqqFNITSLYVTHD 196
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLN----FAGCAVVISHD 499
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-219 |
3.81e-24 |
|
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: 103.20 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 17 GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT--DRSIQQRDICMVFQSYALFPHmS 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGyglKMLGLPKAEirkRVDEALELVD----LAGFADRFVDQI-------SGGQQQRVALARALILKPKVLLFDEP 163
Cdd:TIGR01842 408 VAENIA---RFGENADPE---KIIEAAKLAGvhelILRLPDGYDTVIgpggatlSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLG 219
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFG 535
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-219 |
3.93e-24 |
|
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: 97.00 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN--TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRD-ICMV 83
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFpHMSLGDNVGyglkmlglpkaeirkrvdealelvdlagfadrfvDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 164 LSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLG 219
Cdd:cd03247 126 TVGLDPITERQLLSLI--FEVLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-170 |
4.56e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS-------IQQRDi 80
Cdd:PRK13539 4 EGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeachyLGHRN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 cmvfqsyALFPHMSLGDNVGYGLKMLGLPKAEIrkrvDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK13539 83 -------AMKPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170
....*....|
gi 757596975 161 DEPLSNLDAN 170
Cdd:PRK13539 152 DEPTAALDAA 161
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-227 |
7.83e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.40 E-value: 7.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF-GTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICM 82
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFpHMSLGDNVGYGLKmlglpKAEIRKRVDEALELVDLAGFADRF---VDQI--------SGGQQQRVALARAL 151
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYART-----EQYSREQIEEAARMAYAMDFINKMdngLDTVigengvllSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-214 |
8.88e-24 |
|
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: 101.83 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL--EKPTEGRMFIDGEDVTDRSI---QQRDIC 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIrdtERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFAD-RFVDQISGGQQQRVALARALILKPK 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-227 |
9.40e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 96.83 E-value: 9.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLE--KPTEGRMFIDGEDVTDRSIQQR---DICM 82
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYglkmlglpkaeirkrVDEalelvdlaGFadrfvdqiSGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03217 82 AFQYPPEIPGVKNADFLRY---------------VNE--------GF--------SGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEA-FAVSDMVLVMNKGKIMQLGsPQELYRQ 227
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-170 |
1.08e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.80 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTdrsiQQRDicmVFQ 85
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALF--------PHMSLGDNVGYGLKMLGLPKAEirkRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKV 157
Cdd:PRK13538 74 QDLLYlghqpgikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170
....*....|...
gi 757596975 158 LLFDEPLSNLDAN 170
Cdd:PRK13538 151 WILDEPFTAIDKQ 163
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-224 |
1.38e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ-RD-ICM 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHmSLGDNVgyglkMLGLPKAeIRKRVDEALELVDLAGFAD-------------RfvdQISGGQQQRVALAR 149
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNL-----LLAAPNA-SDEALIEVLQQVGLEKLLEddkglnawlgeggR---QLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-213 |
1.53e-23 |
|
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: 96.73 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRF------GTN-TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFID-GEDVTD------R 73
Cdd:COG4778 6 EVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDlaqaspR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 74 SI---QQRDICMVFQsyalF----PHMSLGDNVGYGLKMLGLPKAEIRKRVDEAL-------ELVDL--AGFadrfvdqi 137
Cdd:COG4778 86 EIlalRRRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLarlnlpeRLWDLppATF-------- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKG 213
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-229 |
1.71e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.03 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKT-TVLRLVAGLEKP--TEGRMFIDGEDVTD------RS 74
Cdd:PRK09473 14 DVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNlpekelNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 75 IQQRDICMVFQS--YALFPHMSLGDNVGYGLkML--GLPKAEIRKRVDEALELVDLAGFADR---FVDQISGGQQQRVAL 147
Cdd:PRK09473 94 LRAEQISMIFQDpmTSLNPYMRVGEQLMEVL-MLhkGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
..
gi 757596975 228 PA 229
Cdd:PRK09473 253 PS 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-214 |
2.54e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.37 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIqqRD-----I 80
Cdd:PRK11288 4 YLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST--TAalaagV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQSYALFPHMSLGDNVgyglkMLG-LP-------KAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI 152
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENL-----YLGqLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 153 LKPKVLLFDEPLSNLdanlrrSMREK------IRELQQQFNITsLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:PRK11288 157 RNARVIAFDEPTSSL------SAREIeqlfrvIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-219 |
5.85e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 96.49 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 12 VTKRFGtNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDvTDRSIQQRDICMVFQSYAL-- 89
Cdd:PRK15056 14 VTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYVPQSEEVdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 90 -FPHMsLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK15056 92 sFPVL-VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 165 SNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVlVMNKGKIMQLG 219
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-216 |
7.85e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTD---RSIQQRDICMV 83
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNvgygLKMLGL--PKAEIRKRVDEALELvdLAGFADRFVDQ---ISGGQQQRVALARALILKPKVL 158
Cdd:PRK11614 86 PEGRRVFSRMTVEEN----LAMGGFfaERDQFQERIKWVYEL--FPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIM 216
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-229 |
1.42e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 18 TNTVIDDLSLSIPQGSMVTLLGPSGCGKT----TVLRLvagLEKP----TEGRMFIDGEDV------TDRSIQQRDICMV 83
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRL---LPSPpvvyPSGDIRFHGESLlhaseqTLRGVRGNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSyalfPHMSLgdNVGYGL-KML--------GLPKAEIRKRVDEALELVDLAGFADRFVD---QISGGQQQRVALARAL 151
Cdd:PRK15134 98 FQE----PMVSL--NPLHTLeKQLyevlslhrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPA 229
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-228 |
1.72e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL----EKPTEGRMFIDGEDVTDRSIQQR------DICMVFQS--YAL 89
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 90 FPHMSLGDNVGYGLKM-LGLPKAEIRKRVDEALELV---DLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-274 |
3.01e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.62 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKT----TVLRLV--AGLEKPTEG-------RMFIDGEDVTD---RSIQQRDICMVFQ 85
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKmllrrrsRQVIELSEQSAaqmRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 S--YALFPHMSLGDNVGYGLKM-LGLPKAEIRKRVDEALELV---DLAGFADRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMASFMGD 239
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
250 260 270
....*....|....*....|....*....|....*.
gi 757596975 240 ANIFPATLTHDSVNIFNY-HLPRPAQLATDNTEITV 274
Cdd:PRK10261 272 VPQLGAMKGLDYPRRFPLiSLEHPAKQEPPIEQDTV 307
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-216 |
3.27e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVT-KRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVF-- 84
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 ----QSYALFPHMSLGDNV---GYGLKMLG----LPKAEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALI 152
Cdd:COG3845 339 pedrLGRGLVPDMSVAENLilgRYRRPPFSrggfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIM 216
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-227 |
3.73e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.84 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSI------QQR----- 78
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaERRrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYA--LFPHMSLGDNVGYGLKMLGLPK-AEIRKRVDEALELVDLAgfADRFVDQ---ISGGQQQRVALARALI 152
Cdd:PRK11701 90 EWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEID--AARIDDLpttFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG-------SPQELY 225
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGltdqvldDPQHPY 247
|
..
gi 757596975 226 RQ 227
Cdd:PRK11701 248 TQ 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-214 |
2.76e-21 |
|
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: 90.22 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVT-----KRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEdvtdrsiqqrdIC 81
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPhMSLGDNVGYGLKMlglpkaeIRKRVDEALE----LVDLAGFADRfvDQ---------ISGGQQQRVALA 148
Cdd:cd03250 70 YVSQEPWIQN-GTIRENILFGKPF-------DEERYEKVIKacalEPDLEILPDG--DLteigekginLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREK-IRELQQQfNITSLYVTHdQSEAFAVSDMVLVMNKGK 214
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLN-NKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-177 |
5.19e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.03 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIdGEDVT----DrsiQQRDicm 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKlayvD---QSRD--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 vfqsyALFPHMSLGDNVGYGLKMLGLPKAEIRKRvdealelvdlaGFADRF----------VDQISGGQQQRVALARALI 152
Cdd:PRK11819 398 -----ALDPNKTVWEEISGGLDIIKVGNREIPSR-----------AYVGRFnfkggdqqkkVGVLSGGERNRLHLAKTLK 461
|
170 180
....*....|....*....|....*
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMRE 177
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVETLRALEE 486
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-185 |
6.21e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 89.24 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-TDRSIQQRDICMVFQSYALFPHMSLGDNV 99
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 100 GYGLKMlglpkAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
Cdd:PRK13540 96 LYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
....*.
gi 757596975 180 RELQQQ 185
Cdd:PRK13540 171 QEHRAK 176
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-221 |
6.61e-21 |
|
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: 89.48 E-value: 6.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTV----LRLVagleKPTEGRMFIDGEDVTDRSIQQ--R 78
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALFPhmslgdnvgyglkmlglpkAEIRKRVD-----------EALELVDLAGFADRFVDQI---------- 137
Cdd:cd03244 79 RISIIPQDPVLFS-------------------GTIRSNLDpfgeysdeelwQALERVGLKEFVESLPGGLdtvveeggen 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 138 -SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqQF-NITSLYVTHdQSEAFAVSDMVLVMNKGKI 215
Cdd:cd03244 140 lSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAH-RLDTIIDSDRILVLDKGRV 215
|
....*.
gi 757596975 216 MQLGSP 221
Cdd:cd03244 216 VEFDSP 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-217 |
1.13e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.86 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDgedVTDRSIQQRdicmvfqsy 87
Cdd:COG2401 32 EAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---VPDNQFGRE--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 alfphMSLGDNVGyglkmlglpkaeIRKRVDEALELVDLAGFAD-----RFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:COG2401 100 -----ASLIDAIG------------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQS-EAFAVSDMVLVMNKGKIMQ 217
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIFVGYGGVPE 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-224 |
1.73e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.47 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGT-NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICMV 83
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHmSLGDNVgyglkMLGLPKAEirKRVDEALELVDLAGFADRFVDQI-----------SGGQQQRVALARALI 152
Cdd:PRK10790 421 QQDPVVLAD-TFLANV-----TLGRDISE--EQVWQALETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfniTSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3-224 |
1.78e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 3 QHNFVELKNVTKRfGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVL-----RLVAGLEKptEGRMFIDGEDVTDRSIQQ 77
Cdd:TIGR00955 23 LVSRLRGCFCRER-PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAKEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RDiCMVFQSYALFPHMSLGDNVGYG--LKM-LGLPKAEIRKRVDEALELVDLAGFAD------RFVDQISGGQQQRVALA 148
Cdd:TIGR00955 100 IS-AYVQQDDLFIPTLTVREHLMFQahLRMpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-221 |
2.29e-20 |
|
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: 92.77 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGT--NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDV-TDRSIQQRDICMV 83
Cdd:TIGR01257 929 VCVKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 164 LSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSP 221
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-233 |
2.66e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 6 FVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGED---VTDRSIQQRDICM 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGL----KMLGLPK---AEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRhltkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFM 233
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-212 |
6.77e-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: 85.28 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTV-IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL--------EKPTEGRMFIdgedvtdrsIQQ 77
Cdd:cd03223 1 IELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLLF---------LPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 78 RdicmvfqSYalFPHMSLGDNVGYGLKmlglpkaeirkrvdealelvdlagfadrfvDQISGGQQQRVALARALILKPKV 157
Cdd:cd03223 72 R-------PY--LPLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 158 LLFDEPLSNLDANLRRSMREKIRELQqqfnITSLYVTHDQS-EAFAvsDMVLVMNK 212
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELG----ITVISVGHRPSlWKFH--DRVLDLDG 162
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-221 |
1.24e-19 |
|
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: 85.54 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 3 QHNFVELKNVTKRFGTN--TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QR 78
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALFphmslgdnvgyglkmlglpKAEIRKRVDEALELVDLAGFADRFV----DQISGGQQQRVALARALILK 154
Cdd:cd03369 83 SLTIIPQDPTLF-------------------SGTIRSNLDPFDEYSDEEIYGALRVseggLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDMVLVMNKGKIMQLGSP 221
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-215 |
1.55e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNT---VIDDLSLSIPQGSMVTLLGPSGCGKT-TVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ---RDI 80
Cdd:PRK13549 261 EVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQaiaQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQS---YALFPHMSLGDNVgyglKMLGLPKAEIRKRVDEALELVDLAGFADRF----------VDQISGGQQQRVAL 147
Cdd:PRK13549 341 AMVPEDrkrDGIVPVMGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRLkvktaspelaIARLSGGNQQKAVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-215 |
1.72e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 24 DLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR-DICMVF-----QSYALFPHMSLGD 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 98 NV-GYGLKMLGL---PKAE--IRKRVDEALElVDLAGfADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK15439 361 NVcALTHNRRGFwikPAREnaVLERYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 757596975 172 RRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-210 |
1.93e-19 |
|
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: 86.27 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 10 KNVTKRFGTNTvIDDLSLSIPQGSMVT-LLGPSGCGKTTVLRLVAGLEKPTEGRMfiDGEDVTDrsiqqrDICMVFQSYA 88
Cdd:cd03236 4 DEPVHRYGPNS-FKLHRLPVPREGQVLgLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPDWD------EILDEFRGSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 L---FPHMsLGDNVGYGLK---MLGLPKA------EIRKRVDE--ALELV----DLAGFADRFVDQISGGQQQRVALARA 150
Cdd:cd03236 75 LqnyFTKL-LEGDVKVIVKpqyVDLIPKAvkgkvgELLKKKDErgKLDELvdqlELRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITsLYVTHDQSEAFAVSDMVLVM 210
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDYLSDYIHCL 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-229 |
1.96e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 86.80 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 19 NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAG-LEKPTE-------GRMFIDGED---VTDRSIQQRDICMVFQSY 87
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPlaaIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPhMSLGDNVGYG----LKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARAL---------ILK 154
Cdd:PRK13547 94 PAFA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRqPA 229
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PA 246
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-227 |
2.86e-19 |
|
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: 85.65 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ-----------RD 79
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQlseaerrrlmrTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYA--LFPHMSLGDNVGYGLKMLGLPK-AEIRKRVDEALELVDL-AGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:TIGR02323 88 WGFVHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG-------SPQELYRQ 227
Cdd:TIGR02323 168 RLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGltdqvldDPQHPYTQ 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-231 |
4.43e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP----TEGRMFIDGEDVTDRSIQQRDICMVFQS--YALFPHMSL 95
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDNVGYGLKMLGLPKAEirKRVDEALELVDLAG---FADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:PRK10418 99 HTHARETCLALGKPADD--ATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-215 |
4.64e-19 |
|
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: 87.96 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVI---DDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL-EKPTEGRMFIDGEDVTDRSIQQ---RDI 80
Cdd:TIGR02633 259 EARNLTCWDVINPHRkrvDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 81 CMVFQS---YALFPHMSLGDNVgyglKMLGLPKAEIRKRVDEALELVDLAGFADRF----------VDQISGGQQQRVAL 147
Cdd:TIGR02633 339 AMVPEDrkrHGIVPILGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRLkvktaspflpIGRLSGGNQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-168 |
7.91e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 83.74 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTdRSIQQRDICMVFQSYALFPHMSLGDNVG 100
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 101 YglkMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARaLILKPKVL-LFDEPLSNLD 168
Cdd:PRK13543 105 F---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-215 |
1.02e-18 |
|
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: 83.08 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPT---EGRMFIDGEDVTD-RSIQ 76
Cdd:cd03233 2 STLSWRNISFTTGKGrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 QRDICMVFQSYALFPHMSLGDNVGYGLKMLGlpkaeirkrvdealelvdlagfaDRFVDQISGGQQQRVALARALILKPK 156
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNIT---SLYVTHDqsEAFAVSDMVLVMNKGKI 215
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtfvSLYQASD--EIYDLFDKVLVLYEGRQ 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-237 |
1.77e-18 |
|
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: 86.92 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLR-LVAGLEKpTEGRMFIDGEdvtdrsiqqrdICMVFQSyALFPHMSLGDNVg 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENI- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 101 yglkMLGLPKAEIR-KRVDEALELV---------DLAGFADRFVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
Cdd:TIGR00957 720 ----LFGKALNEKYyQQVLEACALLpdleilpsgDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 171 LRRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDMVLVMNKGKIMQLGSPQELYRQPASrfMASFM 237
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGA--FAEFL 859
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-223 |
6.73e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 25 LSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEkPTEGRMFIDGEDVTDRSIQQ--RDICM------------VFQSYALf 90
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYlsqqqsppfampVFQYLAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 91 pHMSLGdnvgyglkmlgLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI-------LKPKVLLFDEP 163
Cdd:COG4138 93 -HQPAG-----------ASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-218 |
7.19e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.64 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTV-IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICMV 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMsLGDNvgyglkmlGLPKAEirKRVD---EALELVDLAGFAD-RFVD-QISGGQQQRVALARALILKPKVL 158
Cdd:PRK10522 403 FTDFHLFDQL-LGPE--------GKPANP--ALVEkwlERLKMAHKLELEDgRISNlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSeAFAVSDMVLVMNKGKIMQL 218
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQLSEL 530
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-215 |
1.46e-17 |
|
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: 83.69 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 25 LSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ-RD-ICMVFQSYALFPHmslgdnvgyg 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQlFSAVFSDFHLFDR---------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 103 lkMLGLPKAEIRKRVDEALELVDLAG---FAD-RFVD-QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM-R 176
Cdd:COG4615 421 --LLGLDGEADPARARELLERLELDHkvsVEDgRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFyT 498
|
170 180 190
....*....|....*....|....*....|....*....
gi 757596975 177 EKIRELQQQfNITSLYVTHDQSeAFAVSDMVLVMNKGKI 215
Cdd:COG4615 499 ELLPELKAR-GKTVIAISHDDR-YFDLADRVLKMDYGKL 535
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-224 |
2.47e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS---IQQRDICMV 83
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 84 FQSYALFPHMSLGDNVgyglkMLGLPKAEIRKRVDEAL--EL---VDL---AG---FADrfvdqisggqQQRVALARALI 152
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKQLlaALgcqLDLdssAGsleVAD----------RQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-214 |
2.52e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.53 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLeKPT---EGRMFIDGEDVTDRSI---QQRDIC 81
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDIrdsEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMSLGDNVgyglkMLGLPKA--------EIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALIL 153
Cdd:NF040905 82 IIHQELALIPYLSIAENI-----FLGNERAkrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-196 |
3.13e-17 |
|
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: 82.68 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTN-TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPtegrmfIDGEDVTDRSIQqrdICMVFQSY 87
Cdd:TIGR03719 7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGIK---VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSLGDNVGYGLK--------------MLGLPKAEIRKRVDEALEL---------------VDLAGFA------DR 132
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAeikdaldrfneisaKYAEPDADFDKLAAEQAELqeiidaadawdldsqLEIAMDAlrcppwDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 133 FVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQ---QFNITSLYVTHD 196
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERhlqEYPGTVVAVTHD 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-198 |
3.29e-17 |
|
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: 82.49 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGL--------EKPTEGRMFIdgedvtdrsIQQRdicmvfqsyalfPH 92
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY---------VPQR------------PY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 93 MSLG---DNVGY-----GLKMLGLPKAEIRKrvdeALELVDLAGFADR---------FVDQISGGQQQRVALARALILKP 155
Cdd:TIGR00954 526 MTLGtlrDQIIYpdsseDMKRRGLSDKDLEQ----ILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 757596975 156 KVLLFDEPLSNLDANlrrsMREKIRELQQQFNITSLYVTHDQS 198
Cdd:TIGR00954 602 QFAILDECTSAVSVD----VEGYMYRLCREFGITLFSVSHRKS 640
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-235 |
3.75e-17 |
|
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: 79.76 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 23 DDLSLSIPQGS-----MVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVtdrSIQQRDICMVFQS--YALFphMSL 95
Cdd:cd03237 11 GEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKPQYIKADYEGtvRDLL--SSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDNVGYGLKMlglpKAEIRKrvdeALELVDLAgfaDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
Cdd:cd03237 86 TKDFYTHPYF----KTEIAK----PLQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMN--KGKIMQLGSPQELyRQPASRFMAS 235
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEgePSVNGVANPPQSL-RSGMNRFLKN 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-224 |
3.95e-17 |
|
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: 82.75 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRF-GTNT-VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDrsiqqrDICM 82
Cdd:TIGR01257 1936 DILRLNELTKVYsGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFPHMSLGDNVGYGLKML-------GLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKP 155
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLyVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-207 |
7.79e-17 |
|
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: 81.37 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 EL-KNVTKRFGTNTVidDL-SLSIPQGSMVT-LLGPSGCGKTTVLRLVAGLEKPTEGRmfIDGEDVTDRSIQQrdicmvF 84
Cdd:COG1245 74 ELeEDPVHRYGENGF--RLyGLPVPKKGKVTgILGPNGIGKSTALKILSGELKPNLGD--YDEEPSWDEVLKR------F 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMS-LGDN----------VGYGLKMLG------LPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVAL 147
Cdd:COG1245 144 RGTELQDYFKkLANGeikvahkpqyVDLIPKVFKgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDqseaFAVSDMV 207
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD----LAILDYL 278
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-220 |
9.07e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.53 E-value: 9.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 1 MTQHNFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLE--KPTEGRMFIDGEDVTDRSIQQR 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 D---ICMVFQSYALFPHMSLGD--NVGYG--LKMLGLPKA---EIRKRVDEALELVDL-AGFADRFVDQ-ISGGQQQRVA 146
Cdd:CHL00131 82 AhlgIFLAFQYPIEIPGVSNADflRLAYNskRKFQGLPELdplEFLEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNiTSLYVTHDQS-EAFAVSDMVLVMNKGKIMQLGS 220
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRlLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-218 |
1.98e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRfgTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS---IQQRDICMVF 84
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSY---ALFPHMSLGDNV---------GYGLKMLGLPKAEIRKRVDEALELVDLAGFA-DRFVDQISGGQQQRVALARAL 151
Cdd:PRK09700 345 ESRrdnGFFPNFSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQL 218
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-228 |
4.14e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 25 LSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLeKPTEGRMFIDGEDVTDRSI------------QQRD-ICM-VFQSYALf 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarhraylsqQQTPpFAMpVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 91 phmSLGDnvgyglkmlGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALI-----LKP--KVLLFDEP 163
Cdd:PRK03695 93 ---HQPD---------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-207 |
7.03e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 EL-KNVTKRFGTNTVidDL-SLSIPQGSMVT-LLGPSGCGKTTVLRLVAGLEKPTEGRMFIDG--EDVTDR--------- 73
Cdd:PRK13409 74 ELeEEPVHRYGVNGF--KLyGLPIPKEGKVTgILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEVLKRfrgtelqny 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 74 --SIQQRDICMVF--QSYALFPhMSLGDNVGYGLKmlglpKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALAR 149
Cdd:PRK13409 152 fkKLYNGEIKVVHkpQYVDLIP-KVFKGKVRELLK-----KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDqseaFAVSDMV 207
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD----LAVLDYL 277
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-198 |
1.92e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVtkRFGTNTVID-----DLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFI-DGEDVTDRSIQ--QR 78
Cdd:PTZ00265 383 IQFKNV--RFHYDTRKDveiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALFPHmSLGDNVGYGLKML---------------------------------------------GLPKAEI 113
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnELIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 114 RKRVDEALELVD----------LAGFADRF-------VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
Cdd:PTZ00265 540 NYQTIKDSEVVDvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|..
gi 757596975 177 EKIRELQQQFNITSLYVTHDQS 198
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAHRLS 641
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-231 |
2.40e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.93 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVlRLVAGLEKPTEGR------MFIDGEDVTDRSIQQR 78
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALfphmSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVL 158
Cdd:NF000106 91 RPVR*GRRESF----SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASR 231
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-196 |
7.38e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVI-DDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDgEDVTdrsiqqrdICMVFQSY 87
Cdd:PRK11819 9 MNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK--------VGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 ALFPHMSLGDNVGYGLK--------------MLGLPKAEIRKRVDEALEL---------------VDLAGFA------DR 132
Cdd:PRK11819 80 QLDPEKTVRENVEEGVAevkaaldrfneiyaAYAEPDADFDALAAEQGELqeiidaadawdldsqLEIAMDAlrcppwDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 133 FVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQ---QFNITSLYVTHD 196
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLEQflhDYPGTVVAVTHD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-214 |
8.26e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVT---DRSIQQRDICMVF 84
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALFPHMSLGDNVGYGL----KMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLF 160
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-219 |
1.91e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPT--EGRMFIDGEDVTDRSIqqRDICMVFQSYA 88
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL--KRTGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 LFPHMSLGDNVGYgLKMLGLPKAEIRK-RVDEALELVDLAGFA--------DRFVDQISGGQQQRVALARALILKPKVLL 159
Cdd:PLN03211 151 LYPHLTVRETLVF-CSLLRLPKSLTKQeKILVAESVISELGLTkcentiigNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-215 |
2.61e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQR-DICMVFQSY-----ALFPHMSL 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDNVGygLKMLG-LPKAEIRKRVDEALELVDlaGFADRF------VDQI----SGGQQQRVALARALILKPKVLLFDEPL 164
Cdd:PRK10762 348 KENMS--LTALRyFSRAGGSLKHADEQQAVS--DFIRLFniktpsMEQAigllSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 165 SNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-227 |
5.11e-14 |
|
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: 73.44 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICM 82
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdlRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFP---HMSLGDNVGYGlkmlglpkaeiRKRVDEALELVDLAGFADRFVDQI-----------SGGQQQRVALA 148
Cdd:TIGR00957 1365 IPQDPVLFSgslRMNLDPFSQYS-----------DEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHDQSEAFAVSdMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIR---TQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-236 |
8.49e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 71.37 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN----TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP----TEGRMFIDGEDVTDRSIQQR 78
Cdd:PRK15093 4 LDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 ------DICMVFQ--SYALFPHMSLGDNV-----GYGLKMLGLPKAEIRKRvdEALELVDLAGFADR------FVDQISG 139
Cdd:PRK15093 84 rklvghNVSMIFQepQSCLDPSERVGRQLmqnipGWTYKGRWWQRFGWRKR--RAIELLHRVGIKDHkdamrsFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 140 GQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260
....*....|....*....|....
gi 757596975 220 SPQEL-------YRQPASRFMASF 236
Cdd:PRK15093 242 PSKELvttphhpYTQALIRAIPDF 265
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-215 |
1.02e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 26 SLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRS----IQQRdicMVF-----QSYALFPHMSLG 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdaIRAG---IMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 97 DNVGYGLKMLGLPKAEIRKRVDEAlelvdlaGFADRFVDQ--------------ISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEA-------ENADRFIRSlniktpsreqlimnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-224 |
1.61e-13 |
|
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: 69.88 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTV----LRLVAglekpTEGRMFIDGEDVTDRSIQQ--R 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKwrK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 DICMVFQSYALFPHmSLGDNVG-YGlkmlGLPKAEIRKRVDEalelVDLAGFADRFVDQI-----------SGGQQQRVA 146
Cdd:cd03289 78 AFGVIPQKVFIFSG-TFRKNLDpYG----KWSDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMC 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSMRekiRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-224 |
1.70e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 24 DLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGlEKPTegrmfidgedVTDRSIQQR-DICMVFQSYALFpHMSLGDNVgyg 102
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPP----------RSDASVVIRgTVAYVPQVSWIF-NATVRDNI--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 103 lkMLGLPKAEIR--KRVDEA-----LELV---DLAGFADRFVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
Cdd:PLN03130 700 --LFGSPFDPERyeRAIDVTalqhdLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 173 RSMREKI--RELQQQfniTSLYVThDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:PLN03130 777 RQVFDKCikDELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-241 |
1.94e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICM 82
Cdd:PLN03232 1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFphmslGDNVGYGLKML------GLPKAEIRKRVDEALELVDLAGFADRFV--DQISGGQQQRVALARALILK 154
Cdd:PLN03232 1315 IPQSPVLF-----SGTVRFNIDPFsehndaDLWEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 155 PKVLLFDEPLSNLDANLRRSMREKIRElqqQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRF-- 232
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFfr 1466
|
....*....
gi 757596975 233 MASFMGDAN 241
Cdd:PLN03232 1467 MVHSTGPAN 1475
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-213 |
2.00e-13 |
|
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: 68.51 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDICMVFQ-SYALFPHMSLGDNVG 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 101 YGLkMLGLPKAEIR-KRVDEALEL---VDLAGFAD------RFVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
Cdd:cd03290 97 ENI-TFGSPFNKQRyKAVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 757596975 171 LRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDMVLVMNKG 213
Cdd:cd03290 175 LSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-228 |
2.61e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 18 TNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICMVFQSYALFPHmSL 95
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 96 GDNVGyglkmLGLPKAEiRKRVDEALELVDL--------AGF----ADRFVdQISGGQQQRVALARALILKPKVLLFDEP 163
Cdd:PRK10789 406 ANNIA-----LGRPDAT-QQEIEHVARLASVhddilrlpQGYdtevGERGV-MLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 164 LSNLDANLRRSMREKIRELQQQFniTSLYVTHDQSeAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-227 |
2.91e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.69 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEdvtdrsiqqrdICMVFQSYALFPHMSLGDNVGY 101
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 102 GLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 757596975 182 LQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL---YRQ 227
Cdd:PRK13545 189 FKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVvdhYDE 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-226 |
5.73e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 18 TNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEgrmfidgedvtdrsiqqrDICMVFQ-SYALFPHMS-- 94
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE------------------TSSVVIRgSVAYVPQVSwi 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 ----LGDNVGYGLKmlgLPKAEIRKRVD-----EALELV---DLAGFADRFVDqISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PLN03232 691 fnatVRENILFGSD---FESERYWRAIDvtalqHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 163 PLSNLDANLRRSMREKI--RELQQQfniTSLYVThDQSEAFAVSDMVLVMNKGKIMQLGSPQELYR 226
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCmkDELKGK---TRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-196 |
8.83e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 8 ELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMfidgedvtdRSIQQRDICMvFQSY 87
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------HCGTKLEVAY-FDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 88 --ALFPHMSLGDNVGYGlkmlglpKAEI----RKRvdEALelvdlaGFADRF----------VDQISGGQQQRVALARaL 151
Cdd:PRK11147 391 raELDPEKTVMDNLAEG-------KQEVmvngRPR--HVL------GYLQDFlfhpkramtpVKALSGGERNRLLLAR-L 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 757596975 152 ILKPKVLL-FDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHD 196
Cdd:PRK11147 455 FLKPSNLLiLDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-245 |
9.40e-13 |
|
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: 69.55 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRF--GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKpTEGRMFIDGEDVTDRSIQQ--RDICMVF 84
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTwrKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYALF---------PHMSLGDNvgyglkmlglpkaEIRKRVDEalelVDLAGFADRFVDQ-----------ISGGQQQR 144
Cdd:TIGR01271 1299 QKVFIFsgtfrknldPYEQWSDE-------------EIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQL 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 145 VALARALILKPKVLLFDEPLSNLDANLRRSMRekiRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
250 260
....*....|....*....|...
gi 757596975 225 YRQpASRFMASF--MGDANIFPA 245
Cdd:TIGR01271 1439 LNE-TSLFKQAMsaADRLKLFPL 1460
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-228 |
1.29e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP----TEGRMFIDGEDVTDRSIQQR------DICMVFQ--SYA 88
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 LFPHMSLGDNVgyglkMLGLPKAEI----------RKRvdEALELVDLAGFADR------FVDQISGGQQQRVALARALI 152
Cdd:COG4170 102 LDPSAKIGDQL-----IEAIPSWTFkgkwwqrfkwRKK--RAIELLHRVGIKDHkdimnsYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQP 228
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
61-211 |
1.62e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 61 GRMFIDGEDVTDRSIQQ-RDI-CMVFQSYALFpHMSLGDNVGYGlkmlglPKAEIRKRVDEALELVDLAGFADRFVDQ-- 136
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPNKyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 137 ---------ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHdQSEAFAVSDMV 207
Cdd:PTZ00265 1350 tnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKI 1428
|
....
gi 757596975 208 LVMN 211
Cdd:PTZ00265 1429 VVFN 1432
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-219 |
2.97e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.99 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRF--------------------GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFID 66
Cdd:PRK13546 5 VNIKNVTKEYriyrtnkermkdalipkhknKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 67 GEdvtdrsiqqrdICMVFQSYALFPHMSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVA 146
Cdd:PRK13546 85 GE-----------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLG 219
Cdd:PRK13546 154 FSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-196 |
3.63e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGtntvidDLSLS-----IPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDgEDVTDRSiQ--QRD 79
Cdd:PRK13409 341 VEYPDLTKKLG------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP-QyiKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 80 ICMVFQSYAlfphMSLGDNVG---YglkmlglpKAEIRKRvdeaLELVDLagfADRFVDQISGGQQQRVALARALILKPK 156
Cdd:PRK13409 413 YDGTVEDLL----RSITDDLGssyY--------KSEIIKP----LQLERL---LDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-241 |
5.64e-12 |
|
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: 63.36 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 29 IPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTdrsiqqrdicmvfqsyalfphmslgdnvgyglkmlgl 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 109 pkaeirkrvdealelvdlagFADRFVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNI 188
Cdd:cd03222 65 --------------------YKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 189 TSLYVTHDQSEAFAVSDMVLVM--NKGKIMQLGSPQELyRQPASRFMASFMGDAN 241
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFegEPGVYGIASQPKGT-REGINRFLRGYLITFR 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-214 |
5.96e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ---RDICMVFQ 85
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 86 SYALFPHMSLGDNV---GYGLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQISGGQQQRVALARALILKPKVLLFDE 162
Cdd:PRK10982 81 ELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGK 214
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-223 |
6.81e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 20 TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVA----GLEKPTEGRMFIDGEDVTDRSIQQR-DICMVFQSYALFPHMS 94
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 95 LGDNVGYGLKM-------LGLPKAEIRKRVDEalelVDLAGFA----------DRFVDQISGGQQQRVALARALILKPKV 157
Cdd:TIGR00956 155 VGETLDFAARCktpqnrpDGVSREEYAKHIAD----VYMATYGlshtrntkvgNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 158 LLFDEPLSNLDANlrrSMREKIRELQQQFNI--TSLYVTHDQS--EAFAVSDMVLVMNKGKIMQLGSPQE 223
Cdd:TIGR00956 231 QCWDNATRGLDSA---TALEFIRALKTSANIldTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
274-345 |
9.37e-12 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 59.94 E-value: 9.37e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 274 VGVRPEAITLSlQGDDSQRCTVTHVAYMGPQYEVTVDWHGQSMLL--QINATQLQPTVGENLYLQIHPYGMFIL 345
Cdd:pfam08402 1 LAIRPEKIRLA-AAANGLSGTVTDVEYLGDHTRYHVELAGGEELVvrVPNAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-196 |
1.37e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGtntvidDLSLSIPQGSM-----VTLLGPSGCGKTTVLRLVAGLEKPTEGRMFidgEDVTdrsI----Q- 76
Cdd:COG1245 342 VEYPDLTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK---IsykpQy 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 77 -QRDICMVFQSYalfphmsLGDNVG--YGLKMLglpKAEIRKRvdeaLELVDLAgfaDRFVDQISGGQQQRVALARALIL 153
Cdd:COG1245 410 iSPDYDGTVEEF-------LRSANTddFGSSYY---KTEIIKP----LGLEKLL---DKNVKDLSGGELQRVAIAACLSR 472
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 757596975 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
Cdd:COG1245 473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-172 |
9.41e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.27 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 19 NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIdgedvtdRSIQQRDICMVFQSYalfphmsLGDN 98
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNIAKPYCTY-------IGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 99 VGYGLKMLGLPKAEIRKRVDEALELVD-------LAGFADRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
Cdd:PRK13541 79 LGLKLEMTVFENLKFWSEIYNSAETLYaaihyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
.
gi 757596975 172 R 172
Cdd:PRK13541 159 R 159
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-198 |
1.23e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 16 FGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRsIQQ---RDIC-MVF------- 84
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVAR-LQQdppRNVEgTVYdfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 --QSYALFPHMSLGDNVG--YGLKMLG-LPKAEIR----------KRVDEALELVDLAgfADRFVDQISGGQQQRVALAR 149
Cdd:PRK11147 92 eeQAEYLKRYHDISHLVEtdPSEKNLNeLAKLQEQldhhnlwqleNRINEVLAQLGLD--PDAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 150 ALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQ---QFNITSLYVTHDQS 198
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDI-------ETIEWLEGflkTFQGSIIFISHDRS 214
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-196 |
2.16e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 5 NFVELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRM------------------FID 66
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 67 GEDVTDRSIQQR----DICMVfqsyalfpHMSLGdnvgyglKMLgLPKAEIRKRvdealelvdlagfadrfVDQISGGQQ 142
Cdd:PRK15064 398 DLTLFDWMSQWRqegdDEQAV--------RGTLG-------RLL-FSQDDIKKS-----------------VKVLSGGEK 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 143 QRVALARALILKPKVLLFDEPLSNLDanlrrsMrEKIRELQ---QQFNITSLYVTHD 196
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMD------M-ESIESLNmalEKYEGTLIFVSHD 494
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-235 |
3.61e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 24 DLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFidgedvtdrsiQQRDICMVFQSyALFPHMSLGDNVGYGl 103
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFF- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 104 kmlglpKAEIRKRVDEALEL----VDLAGFADRFVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANL- 171
Cdd:PTZ00243 745 ------DEEDAARLADAVRVsqleADLAQLGGGLETEIgekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757596975 172 RRSMREKIreLQQQFNITSLYVTHdQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRFMAS 235
Cdd:PTZ00243 819 ERVVEECF--LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAA 879
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-238 |
6.34e-10 |
|
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: 59.10 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 19 NTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEdvtdrsiqqrdICMVFQSYALFPHmSLGDN 98
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 99 VgyglkMLGLPKAEIR-KRVDEALEL-VDLAGFADRfvDQI---------SGGQQQRVALARALILKPKVLLFDEPLSNL 167
Cdd:cd03291 118 I-----IFGVSYDEYRyKSVVKACQLeEDITKFPEK--DNTvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757596975 168 DANLRRSMREK-IRELQQqfNITSLYVThDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQPASrFMASFMG 238
Cdd:cd03291 191 DVFTEKEIFEScVCKLMA--NKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLMG 258
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-200 |
1.01e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGlEKPTE--------GRMFIDGEDVTDrsIQQR 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGETIWD--IKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 79 dICMVFQSYalfpHM-----SLGDNV---GYgLKMLGLPKAEIRKRVDEALELVDLAGFADRFVDQ----ISGGQQQRVA 146
Cdd:PRK10938 338 -IGYVSSSL----HLdyrvsTSVRNVilsGF-FDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADApfhsLSWGQQRLAL 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA 200
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-224 |
2.42e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEdvtdrsiqqrdICMVFQSYALFPHmSLGDNVg 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNI- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 101 yglkMLGLPKAEIRKR-VDEALEL-VDLAGFADRfvDQI---------SGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
Cdd:TIGR01271 508 ----IFGLSYDEYRYTsVIKACQLeEDIALFPEK--DKTvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 170 NLRRSMREKIReLQQQFNITSLYVThDQSEAFAVSDMVLVMNKGKIMQLGSPQEL 224
Cdd:TIGR01271 582 VTEKEIFESCL-CKLMSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-213 |
3.03e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.10 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRfgtntVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKP--TEGRMFIDGedvtdrsiQQRDICmvF 84
Cdd:cd03232 13 VPVKGGKRQ-----LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILING--------RPLDKN--F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 85 QSYalfphmslgdnVGYGLKM-LGLPKAEIRkrvdEALEL-VDLAGfadrfvdqISGGQQQRVALARALILKPKVLLFDE 162
Cdd:cd03232 78 QRS-----------TGYVEQQdVHSPNLTVR----EALRFsALLRG--------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 757596975 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEA-FAVSDMVLVMNKG 213
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASiFEKFDRLLLLKRG 185
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-196 |
4.45e-09 |
|
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: 54.69 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 31 QGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMF-IDGEDVTDRSIQQRDICMVFQSYAlfphmslgdnvgyglkmlglp 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 110 kaeirkrvdealelvdlagfadrfvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR-----ELQQ 184
Cdd:smart00382 60 --------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKS 113
|
170
....*....|..
gi 757596975 185 QFNITSLYVTHD 196
Cdd:smart00382 114 EKNLTVILTTND 125
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-182 |
4.48e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 32 GSMVTLLGPSGCGKTTVL-----RLVAGLekPTEGRMFIDGE--DVT-DRSI---QQRDI---------CMVFQSYALFP 91
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLnvlaeRVTTGV--ITGGDRLVNGRplDSSfQRSIgyvQQQDLhlptstvreSLRFSAYLRQP 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 92 HmslgdnvgyglkmlGLPKAEIRKRVDEALELVDLAGFADRFVDQISGG----QQQRVALARALILKPKVLLF-DEPLSN 166
Cdd:TIGR00956 867 K--------------SVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLFlDEPTSG 932
|
170
....*....|....*.
gi 757596975 167 LDANLRRSMREKIREL 182
Cdd:TIGR00956 933 LDSQTAWSICKLMRKL 948
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-215 |
4.51e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 17 GTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMF--------------IDGEDVTDRSIQQRDICm 82
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNPLLYMMRC- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 vfqsyalFPhmslgdnvgyglkmlGLPKAEIRKRvdeaLELVDLAG-FADRFVDQISGGQQQRVALARALILKPKVLLFD 161
Cdd:PLN03073 599 -------FP---------------GVPEQKLRAH----LGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 757596975 162 EPLSNLDANLRRSMREKIRELQQQFnitsLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-241 |
1.12e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN--TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICM 82
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFphmslGDNVGYGLKmlglPKAEiRKRVD--EALELVDLAGFADRFV-----------DQISGGQQQRVALAR 149
Cdd:PLN03130 1318 IPQAPVLF-----SGTVRFNLD----PFNE-HNDADlwESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 150 ALILKPKVLLFDEPLSNL----DANLRRSMREKIRelqqqfNITSLYVTHdQSEAFAVSDMVLVMNKGKIMQLGSPQELY 225
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVdvrtDALIQKTIREEFK------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
250
....*....|....*...
gi 757596975 226 RQPASRF--MASFMGDAN 241
Cdd:PLN03130 1461 SNEGSAFskMVQSTGAAN 1478
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-227 |
1.45e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 9 LKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMfidgedvtdrsiqqrdicmvfqsyA 88
Cdd:PRK10636 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------------------------G 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 89 LFPHMSLGDNVGYGLKMLGL---PKAEIRKRVDEALE--LVD-LAGFA---DRFVD---QISGGQQQRVALARALILKPK 156
Cdd:PRK10636 371 LAKGIKLGYFAQHQLEFLRAdesPLQHLARLAPQELEqkLRDyLGGFGfqgDKVTEetrRFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757596975 157 VLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGSPQELYRQ 227
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-168 |
3.67e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVA-----GLEK--------------PTEGRMFIDG 67
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPKncqilhveqevvgdDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 68 EDVTDRSIQQRDICMVFQSYALFPHMSLGDnvGYGLKMLGLPKAEIRKRVDEA---LELVD-----------LAGFA--- 130
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGK--GKGANKDGVDKDAVSQRLEEIykrLELIDaytaearaasiLAGLSftp 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 757596975 131 ---DRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PLN03073 336 emqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-196 |
5.04e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.94 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 22 IDDLSLSIPQGSMVTLLGPSGCGKTTVLRlvAGLEKPTEgRMFIDGEDVTDRSIqqrdICMVFQSYALFphmslgdNVGY 101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGK-ARLISFLPKFSRNK----LIFIDQLQFLI-------DVGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 102 GLKMLGlpkaeirkrvdealelvdlagfadRFVDQISGGQQQRVALARALI--LKPKVLLFDEPLSNLDANLRRSMREKI 179
Cdd:cd03238 77 GYLTLG------------------------QKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVI 132
|
170
....*....|....*..
gi 757596975 180 RELQQQFNiTSLYVTHD 196
Cdd:cd03238 133 KGLIDLGN-TVILIEHN 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-196 |
8.29e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 11 NVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDG--------------ED--VTDRS 74
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPnerlgklrqdqfafEEftVLDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 75 I----------QQRDicmvfQSYALfPHMSLGDnvgyGLKMLGLP---------KAEIRkrvdeALELVDLAGFADRF-- 133
Cdd:PRK15064 86 ImghtelwevkQERD-----RIYAL-PEMSEED----GMKVADLEvkfaemdgyTAEAR-----AGELLLGVGIPEEQhy 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 134 --VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsmreKIRELQQ---QFNITSLYVTHD 196
Cdd:PRK15064 151 glMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN-------TIRWLEDvlnERNSTMIIISHD 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-196 |
2.05e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.68 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 35 VTLL-GPSGCGKTTVLRLVaglekptegrmfidgedvtdrsiqqrdicmvfqSYALFPHMSLGDNVGYGL-KMLGlpKAE 112
Cdd:cd03240 24 LTLIvGQNGAGKTTIIEAL---------------------------------KYALTGELPPNSKGGAHDpKLIR--EGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 113 IRKRVDEALELV-----------------------DLAGFADRFVDQISGGQQQ------RVALARALILKPKVLLFDEP 163
Cdd:cd03240 69 VRAQVKLAFENAngkkytitrslailenvifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190
....*....|....*....|....*....|....
gi 757596975 164 LSNLDA-NLRRSMREKIRELQQQFNITSLYVTHD 196
Cdd:cd03240 149 TTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-169 |
2.81e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 32 GSMVTLLGPSGCGKTTVLRLVAGLEKP--TEGRMFIDG----EDVTDR---SIQQRDIcmvfQSyalfPHMSLGDNVGYG 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpkkQETFARisgYCEQNDI----HS----PQVTVRESLIYS 977
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 103 lKMLGLPKaEIRKR-----VDEALELVDLAGFADRFV-----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
Cdd:PLN03140 978 -AFLRLPK-EVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-219 |
4.78e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLE--KPTEGRMFIDGEDVTDRSIQQR---DIC 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 82 MVFQSYALFPHMS----LGDNVGYGLKMLG---LPKAEIRKRVDEALELVDL-AGFADRFVDQ-ISGGQQQRVALARALI 152
Cdd:PRK09580 82 MAFQYPVEIPGVSnqffLQTALNAVRSYRGqepLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757596975 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQS-EAFAVSDMVLVMNKGKIMQLG 219
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-232 |
3.01e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 15 RFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQ--RDICMVFQSYALFPH 92
Cdd:PTZ00243 1319 REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 93 mSLGDNVGyglKMLGLPKAEirkrVDEALELVDL--------AGFADRFVD---QISGGQQQRVALARALILK-PKVLLF 160
Cdd:PTZ00243 1399 -TVRQNVD---PFLEASSAE----VWAALELVGLrervasesEGIDSRVLEggsNYSVGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757596975 161 DEPLSNLDANLRRSMREKIRELQQQFN-ITSLYVTHdqseAFAVSDMVLVMNKGKIMQLGSPQELYRQPASRF 232
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAYTvITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-215 |
6.58e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 6.58e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757596975 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDMVLVMNKGKI 215
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-239 |
1.54e-05 |
|
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: 45.67 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 7 VELKNVTKRFGTN--TVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQ--QRDICM 82
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 83 VFQSYALFphmslGDNVGYGLKmlglPKAEIR-KRVDEALELVDLA-------GFADRFV----DQISGGQQQRVALARA 150
Cdd:cd03288 100 ILQDPILF-----SGSIRFNLD----PECKCTdDRLWEALEIAQLKnmvkslpGGLDAVVteggENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 151 LILKPKVLLFDEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAvSDMVLVMNKGKIMQLGSPQELYRQPAS 230
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
....*....
gi 757596975 231 RFMASFMGD 239
Cdd:cd03288 248 VFASLVRTD 256
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-197 |
2.47e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 14 KRFGTNtvIDDLSLSIPQGSMVTLLGPSGCGKTTVLR---LVAGLEKPTEGRmfidgedvtdRSIQQRdicmvfqsyalf 90
Cdd:cd03227 5 GRFPSY--FVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRR----------RSGVKA------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 91 phmslGDNVGYglkmlglpkaeirkrvdEALELVdlagfadRFVDQISGGQQQRVALARALIL---KPKVL-LFDEPLSN 166
Cdd:cd03227 61 -----GCIVAA-----------------VSAELI-------FTRLQLSGGEKELSALALILALaslKPRPLyILDEIDRG 111
|
170 180 190
....*....|....*....|....*....|.
gi 757596975 167 LDANLRRSMREKIRELQQQFNITsLYVTHDQ 197
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQV-IVITHLP 141
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-168 |
2.81e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 15 RFGTNTVIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGlEKPTEGRMF--------------------------IDGe 68
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGGSYtfpgnwqlawvnqetpalpqpaleyvIDG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 69 dvtDRSIQQRDICMvfqsyalfpHMSLGDNVGYGL-----KMLGLPKAEIRKRvdeALELVDLAGFA----DRFVDQISG 139
Cdd:PRK10636 88 ---DREYRQLEAQL---------HDANERNDGHAIatihgKLDAIDAWTIRSR---AASLLHGLGFSneqlERPVSDFSG 152
|
170 180
....*....|....*....|....*....
gi 757596975 140 GQQQRVALARALILKPKVLLFDEPLSNLD 168
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-163 |
3.12e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAGLE--KPTEGRMFIDGEDVTDRSIQQ---RDICMVFQ---SYALfph 92
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDaidAGLAYVTEdrkGYGL--- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757596975 93 mSLGDNVGYGLKMLGLPKAEIRKRVDEALELVDLAGFADRF------VDQI----SGGQQQRVALARALILKPKVLLFDE 162
Cdd:NF040905 352 -NLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMniktpsVFQKvgnlSGGNQQKVVLSKWLFTDPDVLILDE 430
|
.
gi 757596975 163 P 163
Cdd:NF040905 431 P 431
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
21-87 |
7.13e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 41.08 E-value: 7.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757596975 21 VIDDLSLSIPQGSMVTLLGPSGCGKTTVLRLVAgleKPTEGRMFIDGEDVTDRSIQQRDICMVFQSY 87
Cdd:COG1373 9 ILDKLLKLLDNRKAVVITGPRQVGKTTLLKQLA---KELENILYINLDDPRLRALAEEDPDDLLEAL 72
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
31-78 |
9.75e-04 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 39.40 E-value: 9.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 757596975 31 QGSMVTLLGPSGCGKTTVLRLVA---GLEkptegrmFIDgedvTDRSIQQR 78
Cdd:PRK00131 3 KGPNIVLIGFMGAGKSTIGRLLAkrlGYD-------FID----TDHLIEAR 42
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
131-185 |
1.29e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 757596975 131 DRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQ 185
Cdd:PRK10938 130 DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
241-281 |
3.65e-03 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 35.25 E-value: 3.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 757596975 241 NIFPATLTHDSVNIFNYH----LPRPAQLAT---DNTEITVGVRPEAI 281
Cdd:pfam17912 6 NFLPATVVEDGLLVLGGGvtlpLPEGQVLALklyVGKEVILGIRPEHI 53
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
35-80 |
3.98e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 36.80 E-value: 3.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 757596975 35 VTLLGPSGCGKTTVLRLVAGLEKPTEGRMFIDGEDVTDRSIQQRDI 80
Cdd:pfam13173 5 LVITGPRQVGKTTLLLQLIKELLPPENILYINLDDPRLLKLADFEL 50
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
35-78 |
5.28e-03 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 37.03 E-value: 5.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 757596975 35 VTLLGPSGCGKTTVLRLVA---GLEkptegrmFIDgedvTDRSIQQR 78
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAkrlGLP-------FVD----TDAEIEER 36
|
|
|