|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-353 |
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: 535.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNML 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 241 EASVSEPAQNSIDLDGRQITVQeTLAHHPKGKPLTLALRPEAVSLeARKSHDTSLEATIDDVHFLGSVIRTRVILGKN-R 319
Cdd:COG3842 243 PGTVLGDEGGGVRTGGRTLEVP-ADAGLAAGGPVTVAIRPEDIRL-SPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGqE 320
|
330 340 350
....*....|....*....|....*....|....
gi 559158796 320 LSFDTFNDpTHPPPQRGDKVTVHFASHDLLVLAD 353
Cdd:COG3842 321 LVVRVPNR-AALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-350 |
6.22e-167 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 469.17 E-value: 6.22e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGT--LN 238
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 239 MLEASVSEpaqNSIDLDGRQITVQETLAHHPkGKPLTLALRPEAVSLEArkSHDTSLEATIDDVHFLGSVIRTRVILGKN 318
Cdd:COG3839 241 LLPGTVEG---GGVRLGGVRLPLPAALAAAA-GGEVTLGIRPEHLRLAD--EGDGGLEATVEVVEPLGSETLVHVRLGGQ 314
|
330 340 350
....*....|....*....|....*....|..
gi 559158796 319 RLSFDTfndPTHPPPQRGDKVTVHFASHDLLV 350
Cdd:COG3839 315 ELVARV---PGDTRLRPGDTVRLAFDPERLHL 343
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-313 |
4.55e-147 |
|
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: 419.06 E-value: 4.55e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNML 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 241 EASVSEPAQNSIDldgrQITVQETLAHHPKGKPLTLALRPEAVSLEARKSHDTSLEATIDDVHFLGSVIRTRV 313
Cdd:TIGR03265 242 PGTRGGGSRARVG----GLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRL 310
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-350 |
1.86e-145 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 414.54 E-value: 1.86e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-VNLRPNQRNIGMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 163 ALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEA 242
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 243 SVSEPAqnsIDLDGRQITVQETLAHHPKgkplTLALRPEAVSLEARKSHDTSLEATIDDVHFLGSVIRTRVILGKN---- 318
Cdd:COG1118 243 RVIGGQ---LEADGLTLPVAEPLPDGPA----VAGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLEDGegqp 315
|
330 340 350
....*....|....*....|....*....|....*
gi 559158796 319 ---RLSFDTFNDpthPPPQRGDKVTVHFASHDLLV 350
Cdd:COG1118 316 leaEVTKEAWAE---LGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
2.42e-133 |
|
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: 379.66 E-value: 2.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-341 |
1.26e-132 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 383.14 E-value: 1.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEAS 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 244 VSEPAQNS---IDLDGRQITVQETLAHHPkGKPLTLALRPEAVSLEARkSHDTSLEAT---IDDVHFLGSVIRTRVIL-- 315
Cdd:PRK09452 255 VIERLDEQrvrANVEGRECNIYVNFAVEP-GQKLHVLLRPEDLRVEEI-NDDEHAEGLigyVRERNYKGMTLDSVVELen 332
|
330 340 350
....*....|....*....|....*....|
gi 559158796 316 GKNRLSFDTFN--DPT--HPPpqrGDKVTV 341
Cdd:PRK09452 333 GKMVMVSEFFNedDPDfdHSL---GQKVAV 359
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-353 |
2.23e-125 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 364.04 E-value: 2.23e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 3 FLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQ 82
Cdd:PRK11432 6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 163 ALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEA 242
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 243 SVSepaQNSIDLDGRQITVQETLAHHPKGKPLTLALRPEAVSLEARKShdTSLEATIDDVHFLGSVIRTRVILGKNRLSF 322
Cdd:PRK11432 246 TLS---GDYVDIYGYRLPRPAAFAFNLPDGECTVGVRPEAITLSEQGE--ESQRCTIKHVAYMGPQYEVTVDWHGQELLL 320
|
330 340 350
....*....|....*....|....*....|.
gi 559158796 323 DTfnDPTHPPPQRGDKVTVHFASHDLLVLAD 353
Cdd:PRK11432 321 QV--NATQLQPDLGEHYYLEIHPYGMFLLAD 349
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-348 |
1.27e-121 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 354.53 E-value: 1.27e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGT--L 237
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 238 NMLEASVSEpAQNSIDLDGRQITVQETLAHHPKGKPLTLALRPEAVSLEarkSHDTSLEATIDDVHFLG--SVIRTRviL 315
Cdd:PRK11650 241 NLLDGRVSA-DGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALS---SAEGGVPLTVDTVELLGadNLAHGR--W 314
|
330 340 350
....*....|....*....|....*....|...
gi 559158796 316 GKNRLSFDTfndPTHPPPQRGDKVTVHFASHDL 348
Cdd:PRK11650 315 GGQPLVVRL---PHQERPAAGSTLWLHLPANQL 344
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
6.33e-121 |
|
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: 347.20 E-value: 6.33e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-351 |
2.18e-116 |
|
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: 340.24 E-value: 2.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 35 LGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 115 KEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 195 EEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEASVSEPAQNSIDLDGRQITVQE--TLAHHPKGK 272
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDiyTDVPVEKDQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 273 PLTLALRPEAVSL--EARKSHDTSLEATIDDVHFLGSVIRTRVIL---GKNRLSFDTFNDPTHPPPQRGDKVTVHFASHD 347
Cdd:TIGR01187 242 PLHVVLRPEKIVIeeEDEANSSNAIIGHVIDITYLGMTLEVHVRLetgQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPGS 321
|
....
gi 559158796 348 LLVL 351
Cdd:TIGR01187 322 EVVL 325
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-235 |
3.40e-113 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 328.91 E-value: 3.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYA 85
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 LFPNMTVAQNVSFGLRVSGKSR----SEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 162 SALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVG 235
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.57e-112 |
|
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: 326.13 E-value: 1.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-207 |
6.74e-106 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 310.87 E-value: 6.74e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSF----GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNqrn 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVM 207
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-240 |
9.47e-105 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 307.11 E-value: 9.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYA 85
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 LFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALD 165
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 166 AKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNML 240
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-306 |
5.98e-104 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 309.32 E-value: 5.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYA 85
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 LFPNMTVAQNVSFGLRV----SGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 162 SALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLE 241
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 242 ASVSepaqnsidldGRQITVQetlAHH------PKGK-PLTLALRPEAVSLEARKSHDTSLEATIDDVHFLG 306
Cdd:PRK10851 245 GTIR----------GGQFHVG---AHRwplgytPAYQgPVDLFLRPWEVDISRRTSLDSPLPVQVLEVSPKG 303
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-306 |
1.21e-101 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 304.26 E-value: 1.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGT--LN 238
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSpkMN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 239 MLEASVS--EPAQNSIDLDGRQ---ITVQETLAHhpKGKPLTLALRPEAVsLEARKShDTSLEATIDDVHFLG 306
Cdd:PRK11000 241 FLPVKVTatAIEQVQVELPNRQqvwLPVEGRGVQ--VGANMSLGIRPEHL-LPSDIA-DVTLEGEVQVVEQLG 309
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-285 |
1.81e-101 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 304.07 E-value: 1.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEAS 243
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 559158796 244 VSEPAQNSIDLDGRQITvqetlahHP----------KGKPLTLALRPEAVSL 285
Cdd:PRK11607 260 LKERQEDGLVIDSPGLV-------HPlkvdadasvvDNVPVHVALRPEKIML 304
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-235 |
1.29e-100 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 299.31 E-value: 1.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSF-GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQ 82
Cdd:COG1125 4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLD--HLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVG 235
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-221 |
5.58e-100 |
|
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: 294.38 E-value: 5.58e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNqrnIGM 79
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRAdQIGSPFDI 221
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG-RIVAEVEV 218
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-316 |
1.40e-98 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 295.45 E-value: 1.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYALFPNMTVAQNVSF 98
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 GLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRA 178
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 179 IQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEASVSEPAQ-NSIDLDGR 257
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEgTILDTGNI 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 258 QItvqeTLAHHPKGKpLTLALRPEAVSLEARK---SHDTSLEATIDDVHFLGSVIRTRVILG 316
Cdd:NF040840 256 KI----ELPEEKKGK-VRIGIRPEDITISTEKvktSARNEFKGKVEEIEDLGPLVKLTLDVG 312
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-239 |
2.32e-94 |
|
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: 280.76 E-value: 2.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGtNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNM 239
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-235 |
5.87e-93 |
|
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: 277.26 E-value: 5.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF-GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMV 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLD--HLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 159 EPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVG 235
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
7.79e-84 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 254.15 E-value: 7.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV----VNLRPNQRNIGM 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLR-VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 159 EPLSALD--------AKIRiSLREEiraiqqklGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPAS 227
Cdd:COG1126 162 EPTSALDpelvgevlDVMR-DLAKE--------GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-218 |
2.28e-83 |
|
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: 252.98 E-value: 2.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIGMV 80
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRV-SGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:COG1127 88 FQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-211 |
7.64e-82 |
|
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: 248.17 E-value: 7.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---- 75
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 --NIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEAlSISDRIVVMHEGR 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
1.48e-81 |
|
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: 245.94 E-value: 1.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV----VNLRPNQRNIGM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLrvsgksrseidatvkemlslirldhladrypyqmSGGQQQRVALARALATKPQVLLLDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
1.47e-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: 254.83 E-value: 1.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN-----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ---- 74
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 -RNIGMVFQ--AYALFPNMTVAQNVSFGLRVSGK-SRSEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQQRVALARALA 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 150 TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-211 |
5.54e-80 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 243.80 E-value: 5.54e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---- 75
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 --NIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDqEEALSISDRIVVMHEGR 211
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-259 |
2.70e-78 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 243.45 E-value: 2.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RN 76
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLL 156
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGT 236
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPT 243
|
250 260
....*....|....*....|...
gi 559158796 237 LNMLEASVSEPAQNSIDLDGRQI 259
Cdd:COG1135 244 VLNDELPEELLARLREAAGGGRL 266
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-216 |
4.02e-78 |
|
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: 238.73 E-value: 4.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVG---KGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG------KDVVNLRPNQRNIGMVFQAYALFPNMT 91
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGLRvsGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:cd03297 92 VRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 559158796 172 LREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-234 |
4.24e-78 |
|
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: 240.62 E-value: 4.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 9 LKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ------RNIGMVFQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 163 ALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFV 234
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-221 |
6.52e-77 |
|
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: 236.24 E-value: 6.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIGMV 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGK-SRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI 221
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
1.58e-75 |
|
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: 232.47 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV-----NLRPNQ 74
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 155 LLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-303 |
7.27e-75 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 234.99 E-value: 7.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 8 NLKKSFGtntvvhDFNLAV-----GKGefVSFL-GPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV------VNLRPNQR 75
Cdd:COG4148 6 DFRLRRG------GFTLDVdftlpGRG--VTALfGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 NIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEID-ATVKEMLsliRLDHLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISfDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 155 LLLDEPLSALDAKirisLREEI----RAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFV 230
Cdd:COG4148 155 LLMDEPLAALDLA----RKAEIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 231 ASFVGTLNMLEASVSEPAQN----SIDLDGRQITVQetLAHHPKGKPLTLALRPEAVSLEARKSHDTS----LEATIDDV 302
Cdd:COG4148 231 AGGEEAGSVLEATVAAHDPDygltRLALGGGRLWVP--RLDLPPGTRVRVRIRARDVSLALEPPEGSSilniLPGRVVEI 308
|
.
gi 559158796 303 H 303
Cdd:COG4148 309 E 309
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-246 |
1.03e-74 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 235.13 E-value: 1.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 11 KSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ------RNIGMVFQAY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 85 ALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 165 DAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEASV 244
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
..
gi 559158796 245 SE 246
Cdd:TIGR01186 241 AE 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-211 |
1.18e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 230.34 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 163 ALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
2.13e-74 |
|
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: 229.53 E-value: 2.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF-GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQ--AYALFpNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 159 EPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-211 |
3.68e-74 |
|
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: 228.18 E-value: 3.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN----QRNIGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLR-VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 159 EPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-236 |
5.40e-72 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 223.48 E-value: 5.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVvhDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGT 236
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
1.90e-71 |
|
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: 222.76 E-value: 1.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGT----NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN--LRPNQRNI 77
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAY--ALFPNMTVAQNVSFGLRVSGksRSEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 155 LLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPAS 227
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-211 |
2.65e-69 |
|
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: 216.60 E-value: 2.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF----GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN--- 76
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 --IGMVFQAY--ALFPNMTVAQNVSFGLRVSGKSR--SEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQQRVALARALA 149
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 150 TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-231 |
8.18e-69 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 216.27 E-value: 8.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFG----TNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQrn 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 iGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLL 156
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVM--HEGR-ADQIGSPFdiynrpASRFVA 231
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRiVERLELDF------SRRFLA 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-211 |
1.25e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.83 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTN-TVVHDFNLAVGKGEFVsFL-GPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIG 78
Cdd:COG2884 4 FENVSKRYPGGrEALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:COG2884 83 VVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 159 EPLSALDAK--IRI-SLREEIRaiqqKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG2884 163 EPTGNLDPEtsWEImELLEEIN----RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-211 |
2.59e-67 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 210.79 E-value: 2.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNT--VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVF 81
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QayalFP-----NMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLL 156
Cdd:cd03225 82 Q----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-233 |
7.95e-67 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 210.72 E-value: 7.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNI----GM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFG-LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 159 EPLSALDAKirisLREEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASF 233
Cdd:PRK09493 162 EPTSALDPE----LRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-218 |
1.35e-65 |
|
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: 207.97 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFG----LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLL 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 158 DEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
2.75e-65 |
|
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: 207.20 E-value: 2.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN---I 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNV---------------SFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRV 142
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 143 ALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR--ADqiGSPFD 220
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRviAE--GTPAE 239
|
....*.
gi 559158796 221 IYNRPA 226
Cdd:COG0411 240 VRADPR 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-232 |
1.04e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 208.50 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RN 76
Cdd:PRK11153 4 LKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLL 156
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP----ASRFVAS 232
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREFIQS 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
1.11e-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: 204.72 E-value: 1.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGF-----ETPDNGSIEIDGKDVVNLRPN----Q 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFPnMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL-DHLADR-YPYQMSGGQQQRVALARALATK 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 152 PQVLLLDEPLSALD----AKIrislrEE-IRAIQQKlgITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:cd03260 160 PEVLLLDEPTSALDpistAKI-----EElIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.15e-64 |
|
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: 213.23 E-value: 1.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF--GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFeTPDN----GSIEIDGKDVVNLRPNQR-- 75
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGgrisGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 NIGMVFQ--AYALFPnMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:COG1123 84 RIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPAS 227
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
1.04e-63 |
|
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: 202.78 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRP-NQRNIGMVFQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 163 ALDAKIRISLREEIRAIqQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-211 |
1.87e-63 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 202.17 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEI-----------DGKDVVNLRpnq 74
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIRELR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFPNMTVAQN-VSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-228 |
4.89e-63 |
|
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: 200.38 E-value: 4.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRnigMVFQAYALFPNMTVAQNVSFGL 100
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 101 R--VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRA 178
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 179 IQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI-YNRPASR 228
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
1.71e-62 |
|
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: 202.21 E-value: 1.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETP---DNGSIEIDGKDVVNLRPNQ-- 74
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 ----RNIGMVFQ-AY-ALFPNMTVAQNVSFGLRVSGK-SRSEIDATVKEMLSLIRLD---HLADRYPYQMSGGQQQRVAL 144
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
..
gi 559158796 225 PA 226
Cdd:COG0444 242 PR 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-226 |
2.14e-62 |
|
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: 199.20 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN---IGMV 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNV----------SFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALAT 150
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 151 KPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR--ADqiGSPFDIYNRPA 226
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRviAE--GTPDEVRNNPR 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-225 |
7.07e-62 |
|
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: 199.21 E-value: 7.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT-----VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-----VNLRPN 73
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 74 QRNIGMVFQ--AYALFPNmTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDH-LADRYPYQMSGGQQQRVALARALAT 150
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 151 KPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-226 |
1.95e-61 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 199.57 E-value: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF--------GTNTVVH---DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN--- 69
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 --LRPNQRNIGMVFQ-AYA-LFPNMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL--DHlADRYPYQMSGGQQQRV 142
Cdd:COG4608 88 reLRPLRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLrpEH-ADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 143 ALARALATKPQVLLLDEPLSALDAKIR---ISLREEiraIQQKLGITTVFVTHDqeeaLS----ISDRIVVMHEGRADQI 215
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQaqvLNLLED---LQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKIVEI 239
|
250
....*....|.
gi 559158796 216 GSPFDIYNRPA 226
Cdd:COG4608 240 APRDELYARPL 250
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-211 |
4.26e-61 |
|
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: 193.38 E-value: 4.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFglrvsgksrseidatvkemlslirldhladrypyqmSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 163 ALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-211 |
1.15e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 194.89 E-value: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF-GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGL--RVSG-KS------RSEIDAtVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARAL 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgRTSTwRSllglfpPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 149 ATKPQVLLLDEPLSALD---AKIRISLreeIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG3638 162 VQEPKLILADEPVASLDpktARQVMDL---LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-211 |
6.28e-60 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 192.92 E-value: 6.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG-----------KDVVNLRpnq 74
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLLR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFPNMTVAQN-VSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-209 |
1.43e-59 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 190.77 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPD---NGSIEIDGKDVVNLRPNQRNIGMV 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRvSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISdRIVVMHE 209
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-211 |
3.19e-58 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 187.62 E-value: 3.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT----VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN--- 76
Cdd:NF038007 2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 ---IGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:NF038007 82 relIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHdQEEALSISDRIVVMHEGR 211
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINMKDGK 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-211 |
8.96e-58 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 187.94 E-value: 8.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLR-------MIAGFETpdNGSIEIDGK-------DVVN 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEdiydpdvDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 LRpnqRNIGMVFQAYALFPnMTVAQNVSFGLRVSG-KSRSEIDATVKEmlSLIRL---DHLADR---YPYQMSGGQQQRV 142
Cdd:COG1117 90 LR---RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVEE--SLRKAalwDEVKDRlkkSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 143 ALARALATKPQVLLLDEPLSALD----AKIrislrEE-IRAIQQKLGIttVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDpistAKI-----EElILELKKDYTI--VIVTHNMQQAARVSDYTAFFYLGE 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-216 |
7.64e-57 |
|
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: 182.64 E-value: 7.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRnigmvfqaya 85
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 lfpnmtvAQNVSFglrvsgksrseidatVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALD 165
Cdd:cd03214 72 -------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 166 AKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-299 |
4.82e-56 |
|
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: 186.47 E-value: 4.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 8 NLKKSFGTNTVvhDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV------VNLRPNQRNIGMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFGL-RVSGKSRSEIDATVKEMLSLirlDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMkRARPSERRISFERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVA-SFVGTLNm 239
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLArEDQGSLI- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 240 lEASVSEPAQN----SIDLDGRQITVQETLAhhPKGKPLTLALRPEAVSLEARKSHDTS----LEATI 299
Cdd:TIGR02142 238 -EGVVAEHDQHygltALRLGGGHLWVPENLG--PTGARLRLRVPARDVSLALQKPEATSirniLPARV 302
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-232 |
4.88e-56 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 183.46 E-value: 4.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGkDVVNLRPNQR-------- 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG-EEIRLKPDRDgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 --------NIGMVFQAYALFPNMTVAQNVSFG-LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALAR 146
Cdd:COG4598 88 rqlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 147 ALATKPQVLLLDEPLSALDAKIrisLREEIRAIQQ--KLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPEL---VGEVLKVMRDlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 559158796 225 PAS----RFVAS 232
Cdd:COG4598 245 PKSerlrQFLSS 256
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-211 |
7.25e-56 |
|
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: 181.68 E-value: 7.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIGM 79
Cdd:TIGR02673 4 FHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 160 PLSALDAkiriSLREEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:TIGR02673 164 PTGNLDP----DLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
7.46e-56 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 182.15 E-value: 7.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---NI 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLL 157
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 158 DEPLSALDAkirISLrEEIRAIQQKL---GItTVFVT-HDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASR 228
Cdd:COG1137 161 DEPFAGVDP---IAV-ADIQKIIRHLkerGI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
8.41e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.17 E-value: 8.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNmTVAQNVSFGLRVSGKSRSEidATVKEMLSLIRLDH-LADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-234 |
1.11e-55 |
|
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: 182.11 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLR-------MIAGFETpdNGSIEIDGK-------DVVN 69
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVRI--EGKVLFDGQdiydkkiDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 LRpnqRNIGMVFQAYALFPnMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL-DHLADR---YPYQMSGGQQQRVAL 144
Cdd:TIGR00972 80 LR---RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGiKDKKELDEIVEESLKKAALwDEVKDRlhdSALGLSGGQQQRLCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLgiTTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:TIGR00972 156 ARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTN 233
|
250
....*....|
gi 559158796 225 PASRFVASFV 234
Cdd:TIGR00972 234 PKEKRTEDYI 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
5.15e-55 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 180.67 E-value: 5.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNlrPNQRNiGMVFQA 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAER-GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEG 210
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-228 |
5.77e-55 |
|
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: 179.66 E-value: 5.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---NIGMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAkirISLReEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASR 228
Cdd:cd03218 161 FAGVDP---IAVQ-DIQKIIKILkdrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-211 |
2.34e-54 |
|
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: 178.65 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVV-HDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN-----LRPNQRNI 77
Cdd:TIGR02315 2 LEVENLSKVYPNGKQAlKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGlRVSGK----------SRSEIdATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARA 147
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHG-RLGYKptwrsllgrfSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 148 LATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-211 |
2.96e-54 |
|
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: 178.15 E-value: 2.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNI 77
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFG-------LRVSGKSRSEID-ATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALA 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRSLFGLFPKEEkQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 150 TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-224 |
8.07e-54 |
|
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: 178.01 E-value: 8.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSF--GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV---NLRPNQRNIGMV 80
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeeNLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQayalfpN-------MTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:TIGR04520 83 FQ------NpdnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-205 |
1.02e-53 |
|
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: 175.88 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RN-IGM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 160 PLSALDAKIrislREEIRAIQQKL---GITTVFVTHDQEEAlSISDRIV 205
Cdd:TIGR03608 161 PTGSLDPKN----RDEVLDLLLELndeGKTIIIVTHDPEVA-KQADRVI 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-211 |
2.40e-53 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 175.54 E-value: 2.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYALFPNMTVAQNVSFGLR 101
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 102 VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIR---ISLREEIRA 178
Cdd:PRK10771 98 PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqemLTLVSQVCQ 177
|
170 180 190
....*....|....*....|....*....|...
gi 559158796 179 IQQklgITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK10771 178 ERQ---LTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-215 |
4.86e-53 |
|
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: 174.54 E-value: 4.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN---IGMV 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVsgKSRSEIDATVKEMLSLI-RLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYA--RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVM------HEGRADQI 215
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLergrvvLEGTAAEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-218 |
6.21e-53 |
|
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: 174.23 E-value: 6.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFG--TNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMV 80
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGIttVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-216 |
7.16e-53 |
|
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: 173.89 E-value: 7.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYALFPNMTVAQNVSFGLR 101
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 102 VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQ 181
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*
gi 559158796 182 KLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-211 |
8.94e-53 |
|
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: 174.16 E-value: 8.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---- 75
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 --NIGMVFQAYALFPNMTVAQNVSFGLRVSGksRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSiSDRIVVMHEGR 211
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-211 |
1.27e-52 |
|
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: 173.06 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYALFPNMTVAQNVSFGL 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 101 RVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQ 180
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|.
gi 559158796 181 QKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-211 |
1.73e-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: 170.89 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQa 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIakLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 yalfpnmtvaqnvsfglrvsgksrseidatvkemlslirldhladrypyqMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 164 LDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd00267 111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
6.82e-52 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 168.98 E-value: 6.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNIGMVFQAYALFPNMTVAQNV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 97 SFGLRVSGKSRSEIDATVKEMLSLIRLDHLADR----YPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-211 |
1.29e-51 |
|
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: 170.63 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT----VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV-NLRPNQRNIG 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 159 EPLSALDAKIRISLREEIRAiQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-211 |
1.42e-51 |
|
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: 170.67 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 7 KNLKKSFGTNTV-VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIGMV 80
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 161 LSALDAKiriSLREEIRAIQQ--KLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03292 164 TGNLDPD---TTWEIMNLLKKinKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-211 |
3.58e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 171.01 E-value: 3.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRnigMVFQA 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRvsGKSRSEidatVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLK--GQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 164 LDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-211 |
4.81e-51 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 170.32 E-value: 4.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSI-----EIDGKDVVN-----L 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 71 RPNQRNIGMVFQAYALFPNMTVAQNVSFG-LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALA 149
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 150 TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-234 |
1.08e-50 |
|
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: 169.63 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGK---------------DVV 68
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEqlyhmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 69 NLRPNQRNIGMVFQAYALFPNMTVAQNVSFG-LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARA 147
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 148 LATKPQVLLLDEPLSALDAKirisLREEIRAIQQKLG----ITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPE----LVGEVLNVIRRLAsehdLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
|
250
....*....|.
gi 559158796 224 RPASRFVASFV 234
Cdd:TIGR03005 237 QPKEERTREFL 247
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
8.52e-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: 165.73 E-value: 8.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSeiDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 559158796 163 ALDAKIRISLREEIRAiQQKLGITTVFVTHDQEEA 197
Cdd:COG4133 161 ALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
9.36e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.80 E-value: 9.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRpnqRNIGMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR---RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYAL---FPnMTVAQNVSFGL----RVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-211 |
1.16e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 167.18 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF--GT---NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR--N 76
Cdd:COG1101 2 LELKNLSKTFnpGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYAL--FPNMTVAQNVS--------FGLRvSGKSRSEIDAtVKEMLSLIRLDhLADRYPYQM---SGGQQQRVA 143
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLR-RGLTKKRREL-FRELLATLGLG-LENRLDTKVgllSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 144 LARALATKPQVLLLDEPLSALD---AKIRISLREEIraIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDpktAALVLELTEKI--VEEN-NLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-218 |
1.44e-49 |
|
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: 165.62 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV-NLRPNQRNIGMVFQAY 84
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 85 ALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 165 DAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-211 |
1.74e-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: 164.70 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDatvkEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 164 LDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-223 |
2.46e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 167.15 E-value: 2.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV----VNLRPNQRNIGMVFQ--AYALFPNmTVAQ 94
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLSDIRKKVGLVFQypEYQLFEE-TIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSFGLRVSGKSRSEIDATVKEMLSLIRLDH--LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISL 172
Cdd:PRK13637 104 DIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 173 REEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK13637 184 LNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-211 |
4.03e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 164.77 E-value: 4.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN---I 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGLRVsGKSRSEIDATVKEMLSLI-----RLDHLADrypyQMSGGQQQRVALARALATKP 152
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYA-RRDRAEVRADLERVYELFprlkeRRRQRAG----TLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 153 QVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-233 |
9.91e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 168.67 E-value: 9.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRP------NQRNIGMVFQAYALF 87
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 88 PNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 168 IRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASF 233
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-225 |
3.10e-48 |
|
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: 170.25 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF-----------GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTT----VLRMIagfetPDNGSIEIDGKDVV 68
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 69 NL-----RPNQRNIGMVFQ-AYA-LFPNMTVAQNVSFGLRV--SGKSRSEIDATVKEMLSLIRLDH-LADRYPYQMSGGQ 138
Cdd:COG4172 351 GLsrralRPLRRRMQVVFQdPFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 139 QQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDqeeaLS----ISDRIVVMHEGRADQ 214
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD----LAvvraLAHRVMVMKDGKVVE 506
|
250
....*....|.
gi 559158796 215 IGSPFDIYNRP 225
Cdd:COG4172 507 QGPTEQVFDAP 517
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-207 |
6.31e-48 |
|
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: 160.78 E-value: 6.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRpnqRNIGMVFQAYA 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 L---FPnMTVAQNVSFGL--------RVSGKSRSEIDatvkEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:cd03235 79 IdrdFP-ISVRDVVLMGLyghkglfrRLSKADKAKVD----EALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 155 LLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVM 207
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-234 |
2.77e-47 |
|
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: 161.13 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN---------TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ 74
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 -----RNIGMVFQ-AYALF-PNMTVAQNVSFGLR-VSGKSRSEIDATVKEMLSLIRL-DHLADRYPYQMSGGQQQRVALA 145
Cdd:TIGR02769 83 rrafrRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 146 RALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR--ADQIGSPFDIYN 223
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQivEECDVAQLLSFK 242
|
250
....*....|.
gi 559158796 224 RPASRFVASFV 234
Cdd:TIGR02769 243 HPAGRNLQSAV 253
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-218 |
4.52e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 169.63 E-value: 4.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFpNMTVAQN 95
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGlrvsgksRSEI-DATVKEMLSLIRLDHLADRYP--YQM---------SGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:COG2274 569 ITLG-------DPDAtDEEIIEAARLAGLHDFIEALPmgYDTvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 164 LDAKIRISLREEIRAIQQklGITTVFVTHDqEEALSISDRIVVMHEGRADQIGSP 218
Cdd:COG2274 642 LDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTH 693
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-228 |
1.02e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 159.47 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTN---------TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL- 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 71 ----RPNQRNIGMVFQ--AYALFPNMTVAQNVSFGLR-VSGKSRSEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQQRV 142
Cdd:PRK10419 81 raqrKAFRRDIQMVFQdsISAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 143 ALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR--ADQIGSPFD 220
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQivETQPVGDKL 240
|
....*...
gi 559158796 221 IYNRPASR 228
Cdd:PRK10419 241 TFSSPAGR 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-263 |
1.72e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 159.51 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNT---VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG-----KDVVNLRp 72
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 nqRNIGMVFQ-AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATK 151
Cdd:PRK13650 81 --HKIGMVFQnPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 152 PQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEaLSISDRIVVMHEGRADQIGSPFDIYNRPAS---- 227
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGNDllql 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 559158796 228 ----RFVASFVGTLNmleasvsepaQNSIDLDGRQITVQE 263
Cdd:PRK13650 238 gldiPFTTSLVQSLR----------QNGYDLPEGYLTEKE 267
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
1.89e-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: 155.62 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT--VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGM 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFpNMTVAQNVsfglrvsgksrseidatvkemlslirldhladrypyqMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 559158796 160 PLSALDAKIRISLREEIRAIQQklGITTVFVTHDqEEALSISDRIVVMHEGR 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-222 |
3.20e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 158.64 E-value: 3.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG-----KDVVNLRpnqRNIGMVFQ-AYALFPNMTV 92
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVR---RQVGMVFQnPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISL 172
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 559158796 173 REEIRAIQQKLGITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIY 222
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-230 |
1.26e-45 |
|
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: 155.90 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL---RPNQRNIGMV 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmhERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGK-SRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFV 230
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV 231
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-211 |
4.98e-45 |
|
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: 153.66 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---- 75
Cdd:TIGR02211 2 LKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 --NIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSIsDRIVVMHEGR 211
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQ 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
1.52e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 154.79 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEI------DGKDVVNLRPNQRNIGMVFQayalFPNM---- 90
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPEHqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 91 -TVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDH-LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:PRK13634 101 eTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 169 RISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPA 226
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-289 |
3.09e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 158.64 E-value: 3.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ---RNI 77
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGLRVSGK---SRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 155 LLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRadqigspfdiynrpasrfvasFV 234
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGR---------------------LV 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 235 GTLNMLEASVSEPAQNSIdldGRQITVQETLAHHPKGKP------LTLALRPEAVSLEARK 289
Cdd:COG1129 220 GTGPVAELTEDELVRLMV---GRELEDLFPKRAAAPGEVvlevegLSVGGVVRDVSFSVRA 277
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
1.29e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 151.04 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVF 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYAL-FPnMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADR-YPyQMSGGQQQRVALARALA-------TKP 152
Cdd:COG4559 82 QHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRsYQ-TLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 153 QVLLLDEPLSALD-----AKIRIsLREEIRAiqqklGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:COG4559 160 RWLFLDEPTSALDlahqhAVLRL-ARQLARR-----GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-234 |
1.76e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.89 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN---------- 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 74 -----QRNIGMVFQAYALFPNMTVAQNV-SFGLRVSGKSRSEIDATVKEMLSLIRLDHLA-DRYPYQMSGGQQQRVALAR 146
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 147 ALATKPQVLLLDEPLSALDAKirisLREEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|.
gi 559158796 224 RPASRFVASFV 234
Cdd:PRK10619 242 NPQSPRLQQFL 252
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-262 |
1.80e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 151.80 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVnlRPNQRNIGmvfqa 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 Y-----ALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:COG4152 75 YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 159 EPLSALD---AKIrisLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVasFVG 235
Cdd:COG4152 155 EPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL--RLE 228
|
250 260
....*....|....*....|....*..
gi 559158796 236 TLNMLEASVSEPAQNSIDLDGRQITVQ 262
Cdd:COG4152 229 ADGDAGWLRALPGVTVVEEDGDGAELK 255
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-218 |
4.08e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 156.86 E-value: 4.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFpNMT 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGlrvsgksRSEI-DATVKEMLSLIRLDHLADRYP--YQ---------MSGGQQQRVALARALATKPQVLLLDE 159
Cdd:COG1132 430 IRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEALPdgYDtvvgergvnLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 160 PLSALD----AKIRISLREEIRaiqqklGITTVFVTHDqeeaLS---ISDRIVVMHEGRADQIGSP 218
Cdd:COG1132 503 ATSALDteteALIQEALERLMK------GRTTIVIAHR----LStirNADRILVLDDGRIVEQGTH 558
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-302 |
4.72e-43 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 152.34 E-value: 4.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 36 GPSGCGKTTVLRMIAGFETPDNGSIEIDGK---DV---VNLRPNQRNIGMVFQAYALFPNMTVAQNVSFGlrVSGKSRSE 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG--MAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 110 IDATVkemlSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVF 189
Cdd:PRK11144 109 FDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 190 VTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEASVSEP----AQNSIDLDGRQITVQETL 265
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVLEHhphyAMTALALGDQHLWVNKLD 264
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 559158796 266 AhhPKGKPLTLALRPEAVSLEARKSHDTS----LEATIDDV 302
Cdd:PRK11144 265 A--PLGTALRIRIQASDVSLVLQPPQQSSirniLRAKVVEI 303
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-220 |
1.25e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 148.77 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGM 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYAL-FPnMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADR-YPyQMSGGQQQRVALARALA------TK 151
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRdYP-QLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 152 PQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFD 220
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-211 |
1.85e-42 |
|
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: 146.57 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVsFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 163 ALDAKIRISLREEIraiqQKLGITTVFV--THDQEEALSISDRIVVMHEGR 211
Cdd:cd03264 160 GLDPEERIRFRNLL----SELGEDRIVIlsTHIVEDVESLCNQVAVLNKGK 206
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-225 |
3.80e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 147.68 E-value: 3.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNT---------VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--N 69
Cdd:COG4167 2 SALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 LRPNQRNIGMVFQ--AYALFPNMTVAQNVSFGLRVSGK-SRSEIDATVKEMLSLIRL--DHlADRYPYQMSGGQQQRVAL 144
Cdd:COG4167 82 YKYRCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDlTAEEREERIFATLRLVGLlpEH-ANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
.
gi 559158796 225 P 225
Cdd:COG4167 241 P 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-212 |
4.35e-42 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 145.89 E-value: 4.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLrpNQRNIGMVFQA 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--ARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 164 LDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRA 212
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-221 |
9.02e-42 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 146.00 E-value: 9.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQA 83
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFGlRV---SGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:COG4604 84 NHINSRLTVRELVAFG-RFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI 221
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-211 |
1.15e-41 |
|
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: 146.00 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETP-DNGSIEIDGK-----DVVNLRpnq 74
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGErrggeDVWELR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMV--FQAYALFPNMTVAQNV------SFGL--RVSgksrSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVAL 144
Cdd:COG1119 78 KRIGLVspALQLRFPRDETVLDVVlsgffdSIGLyrEPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
1.34e-41 |
|
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: 142.95 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN---QRNIGMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 fqayalfpnmtvaqnvsfglrvsgksrseidatvkemlslirldhladrypYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:cd03216 81 ---------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-218 |
2.49e-41 |
|
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: 151.83 E-value: 2.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQAYALFPnMT 91
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWVPQNPYLFA-GT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGlrvsgksrsEIDATVKEMLSLIR---LDHLADRYP-----------YQMSGGQQQRVALARALATKPQVLLL 157
Cdd:COG4988 427 IRENLRLG---------RPDASDEELEAALEaagLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 158 DEPLSALDAKIRISLREEIRAIQQklGITTVFVTHDqEEALSISDRIVVMHEGRADQIGSP 218
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTH 555
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-218 |
3.25e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 151.84 E-value: 3.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFpNMT 91
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGlrvsgksRSEI-DATVKEMLSLIRLDHLADRYPY-----------QMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:COG4987 425 LRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 160 PLSALDAKIRISLREEIRAIQQklGITTVFVTHDqEEALSISDRIVVMHEGRADQIGSP 218
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTH 553
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
2.89e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.82 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGT--NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNIGMVF 81
Cdd:PRK13632 10 VENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 Q-AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:PRK13632 90 QnPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALsISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-217 |
3.86e-40 |
|
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: 141.52 E-value: 3.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 16 NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpNMTVA 93
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdLNLRWLRSQIGLVSQEPVLF-DGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 QNVSFGLRvsgksrseiDATVKEMLSLIRL-------DHLADRY-----PY--QMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:cd03249 95 ENIRYGKP---------DATDEEVEEAAKKanihdfiMSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 160 PLSALDAkirislrEEIRAIQQKL-----GITTVFVTHdqeeALSI---SDRIVVMHEGRADQIGS 217
Cdd:cd03249 166 ATSALDA-------ESEKLVQEALdramkGRTTIVIAH----RLSTirnADLIAVLQNGQVVEQGT 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-225 |
3.93e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 143.95 E-value: 3.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAVGKGEFVsfLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--------NLRpnqRNIGMVFQ-AYA-LFPNMT 91
Cdd:PRK11308 36 FTLERGKTLAV--VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadpeaqkLLR---QKIQIVFQnPYGsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGLRVSGK-SRSEIDATVKEMLSLI--RLDHlADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:PRK11308 111 VGQILEEPLLINTSlSAAERREKALAMMAKVglRPEH-YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 169 RISLREEIRAIQQKLGITTVFVTHDqeeaLS----ISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHD----LSvvehIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-211 |
5.05e-40 |
|
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: 140.74 E-value: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---NIGMV 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLirLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGR 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-211 |
5.72e-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: 147.91 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKT----TVLRMIAGFETPDNGSIEIDGKDVVNLRP 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 NQ------RNIGMVFQ--AYALFPNMTVAQNVSFGLRV-SGKSRSEIDATVKEMLSLIRLDHLA---DRYPYQMSGGQQQ 140
Cdd:COG4172 84 RElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 141 RVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDqeeaLSI----SDRIVVMHEGR 211
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGE 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-225 |
6.44e-40 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 143.69 E-value: 6.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFG-------------TNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL 70
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 71 RPNQR-----NIGMVFQ--AYALFPNMTVAQNVSFGLRV--SGKSRSEIDATVKEMLSLIRL-DHLADRYPYQMSGGQQQ 140
Cdd:PRK15079 89 KDDEWravrsDIQMIFQdpLASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 141 RVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFD 220
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 248
|
....*
gi 559158796 221 IYNRP 225
Cdd:PRK15079 249 VYHNP 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-218 |
3.16e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 141.10 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR-NIGMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 161 LSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-221 |
4.26e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 141.51 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-VNLRPNQRNIGMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQN-VSFGlRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:PRK13536 122 FDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 162 SALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI 221
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
4.71e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.78 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ---RNIGMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLA---DRYPYQMSGGQQQRVALARALATKPQVLLL 157
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 158 DEPLSAL-----DAKIRI--SLREEiraiqqklGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG3845 166 DEPTAVLtpqeaDELFEIlrRLAAE--------GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-234 |
4.54e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 136.51 E-value: 4.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGF-----ETPDNGSIEIDGKDVVNLRPN----Q 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpievR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFPNMTVAQNVSFGLRVSG--KSRSEIDATVKEMLSLIRL-DHLADR---YPYQMSGGQQQRVALARAL 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 149 ATKPQVLLLDEPLSALD----AKIrislrEEIrAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:PRK14267 165 AMKPKILLMDEPTANIDpvgtAKI-----EEL-LFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
250
....*....|
gi 559158796 225 PASRFVASFV 234
Cdd:PRK14267 239 PEHELTEKYV 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
7.29e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.81 E-value: 7.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGF-----ETPDNGSIEIDGKD-----VVNL 70
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDifkmdVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 71 RpnqRNIGMVFQAYALFPNMTVAQNVSFGLRVS--GKSRSEIDATVKEMLSLIRL-DHLADRY---PYQMSGGQQQRVAL 144
Cdd:PRK14247 81 R---RRVQMVFQIPNPIPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 145 ARALATKPQVLLLDEPLSALD----AKIrislreEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFD 220
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDpentAKI------ESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|....
gi 559158796 221 IYNRPASRFVASFV 234
Cdd:PRK14247 232 VFTNPRHELTEKYV 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-211 |
9.55e-38 |
|
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: 133.33 E-value: 9.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR-NIGMVF-----QAYALFPNMT 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFglrvsgksrseidatvkemlslirldhladryPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDakirIS 171
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 559158796 172 LREEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03215 139 AKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-210 |
1.25e-37 |
|
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: 133.92 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVvNLRPNQRNIGMVFQ-- 82
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNmTVAQNVSFGLRVSGKSRSEIDatvkEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03226 81 DYQLFTD-SVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 163 ALDAKIRISLREEIRAIqQKLGITTVFVTHDQEEALSISDRIVVMHEG 210
Cdd:cd03226 156 GLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-228 |
1.40e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 135.29 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGF-----ETPDNGSIEIDGK-------DVVN 69
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHniysprtDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 LRpnqRNIGMVFQAYALFPnMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL-----DHLADRyPYQMSGGQQQRVA 143
Cdd:PRK14239 84 LR---KEIGMVFQQPNPFP-MSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIwdevkDRLHDS-ALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 144 LARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLgiTTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
....*
gi 559158796 224 RPASR 228
Cdd:PRK14239 237 NPKHK 241
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-225 |
2.76e-37 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 134.35 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLrPNQR--NIGMV- 80
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiaRMGVVr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 -FQAYALFPNMT------VAQ------NVSFGL-RVSGKSRSEIDATVKEM--LSLIRLDHLADRYPYQMSGGQQQRVAL 144
Cdd:PRK11300 85 tFQHVRLFREMTvienllVAQhqqlktGLFSGLlKTPAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
.
gi 559158796 225 P 225
Cdd:PRK11300 245 P 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-236 |
2.97e-37 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 138.05 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL--RPNQRNIG 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaRAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQNVSFGlRVSGKSR-----SEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMG-RTPHRSRfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASR--FVA 231
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRaaFDA 238
|
....*.
gi 559158796 232 -SFVGT 236
Cdd:PRK09536 239 rTAVGT 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-221 |
3.21e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 134.37 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVF 81
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFG----LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLL 157
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 158 DEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI 221
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-211 |
3.55e-37 |
|
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: 133.33 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF------GTN-TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKD---------- 66
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 67 --VVNLRpnQRNIGMVFQAYALFPNMT----VAQnvsfGLRVSGKSRSEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQ 139
Cdd:COG4778 85 reILALR--RRTIGYVSQFLRVIPRVSaldvVAE----PLLERGVDREEARARARELLARLNLPeRLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 140 QRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-228 |
5.53e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 131.43 E-value: 5.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIG 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQNVSFGLRVSGKSRSEI-DATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLL 157
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 158 DEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASR 228
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-225 |
5.85e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 131.85 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPD---NGSIEIDG-----KDVVNLRpnqRNIGMVFQ-AYALFP 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGitltaKTVWDIR---EKVGIVFQnPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 89 NMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 169 RISLREEIRAIQQKLGITTVFVTHDQEEAlSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-212 |
1.09e-35 |
|
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: 127.72 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFPNmT 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVsfglrvsgksrseidatvkemlslirldhladrypyqMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:cd03246 92 IAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 559158796 172 LREEIRAIqQKLGITTVFVTHdQEEALSISDRIVVMHEGRA 212
Cdd:cd03246 135 LNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-217 |
2.08e-35 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 128.89 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpNMTVAQN 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdYTLASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRvsGKSRSEIDATVKEMLSLIRLDHLADRYP-------YQMSGGQQQRVALARALATKPQVLLLDEPLSALDAki 168
Cdd:cd03251 96 IAYGRP--GATREEVEEAARAANAHEFIMELPEGYDtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 169 rislrEEIRAIQQKL-----GITTVFVTHdqeeALSI---SDRIVVMHEGRADQIGS 217
Cdd:cd03251 172 -----ESERLVQAALerlmkNRTTFVIAH----RLSTienADRIVVLEDGKIVERGT 219
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-235 |
2.21e-35 |
|
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: 128.64 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPD----NGSIEIDGKDVVNLRPNQRNIGMVFQA--YALFPNMTV 92
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDH---LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIR 169
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 170 ISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVG 235
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-222 |
4.93e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.44 E-value: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 17 TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG---KDVVNLRPNQRNIGMVFQAyalfP-NMTV 92
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 A----QNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:PRK13633 100 AtiveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 169 RISLREEIRAIQQKLGITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIY 222
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-224 |
7.11e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 128.71 E-value: 7.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN------LRPNQRNIGMVFQayalFPNM---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 91 -TVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDH-LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 169 RISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-218 |
1.22e-34 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 126.96 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 12 SFGTNT---VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYAL 86
Cdd:cd03253 7 TFAYDPgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDSLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 87 FpNMTVAQNVSFGlrvsgksrsEIDATVKEMLSLIRLDHLAD---RYP--YQ---------MSGGQQQRVALARALATKP 152
Cdd:cd03253 87 F-NDTIGYNIRYG---------RPDATDEEVIEAAKAAQIHDkimRFPdgYDtivgerglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 153 QVLLLDEPLSALDakiriSLREeiRAIQQKL-----GITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSP 218
Cdd:cd03253 157 PILLLDEATSALD-----THTE--REIQAALrdvskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-211 |
1.71e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLkksfGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNiGMVF 81
Cdd:COG1129 257 LEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRA-GIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 -----QAYALFPNMTVAQNVSFGL--RVSGK---SRSEIDATVKEMLSL--IRLDHladryPYQ----MSGGQQQRVALA 145
Cdd:COG1129 332 vpedrKGEGLVLDLSIRENITLASldRLSRGgllDRRRERALAEEYIKRlrIKTPS-----PEQpvgnLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 146 RALATKPQVLLLDEPLSALD--AKirislrEEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDvgAK------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-222 |
3.10e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 127.13 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFN---LAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGK-----DVVNLRpnqR 75
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLR---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 NIGMVFQ-AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:PRK13642 82 KIGMVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 155 LLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIY 222
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-225 |
5.04e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 126.30 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGF-----ETPDNGSIEIDGKDV----VNLRPNQ 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyerrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFPnMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL----DHLADRYPYQMSGGQQQRVALARALA 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 150 TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMH--EGRADQI---GSPFDIYNR 224
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLvefGLTKKIFNS 246
|
.
gi 559158796 225 P 225
Cdd:PRK14258 247 P 247
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-216 |
5.83e-34 |
|
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: 131.41 E-value: 5.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFPNmT 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVS-FGlrvsgksrsEID----------ATVKEMLSlirldHLADRY-------PYQMSGGQQQRVALARALATKPQ 153
Cdd:COG4618 422 IAENIArFG---------DADpekvvaaaklAGVHEMIL-----RLPDGYdtrigegGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQeEALSISDRIVVMHEGRADQIG 216
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-223 |
6.76e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.02 E-value: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNIGMVFQ-AYALFPNMTVAQNVS 97
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRKHIGIVFQnPDNQFVGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 98 FGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIR 177
Cdd:PRK13648 107 FGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 559158796 178 AIQQKLGITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK13648 187 KVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-210 |
1.29e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.13 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNG----------SIEIDGKDVVNLRPN 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 74 QRNIGMVFQAYALFPNMTVAQNVSFGLR---------VSGKSRSEIDATVkEMLSLIRLDHLADRYPYQMSGGQQQRVAL 144
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEG 210
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-211 |
1.60e-33 |
|
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: 123.47 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 16 NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQAYALFpNMTVA 93
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 QNVSFGLRVSGksrseiDATVKEMLSLIRLDHLADRYP-----------YQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03245 96 DNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 559158796 163 ALDakiRISLREEIRAIQQKL-GITTVFVTHDQeEALSISDRIVVMHEGR 211
Cdd:cd03245 170 AMD---MNSEERLKERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGR 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-218 |
2.25e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.85 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 24 LAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNIGMVFQAY--ALFpNMTVAQNVSFG 99
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaeNEKWVRSKVGLVFQDPddQVF-SSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 100 LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLReEIRAI 179
Cdd:PRK13647 105 PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDR 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 559158796 180 QQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:PRK13647 184 LHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-211 |
3.63e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 122.68 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSflGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIGMVFQAYALFPNMTVAQN 95
Cdd:PRK10908 22 TFHMRPGEMAFLT--GHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIR---ISL 172
Cdd:PRK10908 100 VAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSegiLRL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 559158796 173 REEIraiqQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK10908 180 FEEF----NRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
3.82e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.14 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNI 77
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAY--ALFpNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVL 155
Cdd:PRK13652 81 GLVFQNPddQIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 156 LLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-216 |
4.75e-33 |
|
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: 122.26 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLrpnqrNIGMVFQa 83
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 yalfPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRyPYQM-SGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03220 97 ----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL-PVKTySSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 163 ALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-239 |
6.34e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 129.07 E-value: 6.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSF----GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--- 74
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 ---RNIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATK 151
Cdd:PRK10535 83 lrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 152 PQVLLLDEPLSALDAKIrislREEIRAIQQKL---GITTVFVTHDQEEALSiSDRIVVMHEGR----------ADQIGSP 218
Cdd:PRK10535 163 GQVILADEPTGALDSHS----GEEVMAILHQLrdrGHTVIIVTHDPQVAAQ-AERVIEIRDGEivrnppaqekVNVAGGT 237
|
250 260
....*....|....*....|...
gi 559158796 219 FDIYNRPAS--RFVASFVGTLNM 239
Cdd:PRK10535 238 EPVVNTASGwrQFVSGFREALTM 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-214 |
7.60e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.23 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL----RPNQRN--IGMVFQAYALFPNMT 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 559158796 172 LREEIRAIQQKLGITTVFVTHDQEEALSISdRIVVMHEGRADQ 214
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-234 |
8.30e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 122.97 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLR-------MIAGFETpdNGSIEIDGK-------DVVN 69
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKnlyapdvDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 LRpnqRNIGMVFQAYALFPNmTVAQNVSFGLRVSGkSRSEIDATVKEMLSLIRL-DHLADRYP---YQMSGGQQQRVALA 145
Cdd:PRK14243 89 VR---RRIGMVFQKPNPFPK-SIYDNIAYGARING-YKGDMDELVERSLRQAALwDEVKDKLKqsgLSLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 146 RALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLgiTTVFVTHDQEEALSISDrIVVMHEGRADQIGS------PF 219
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD-MTAFFNVELTEGGGrygylvEF 240
|
250
....*....|....*....
gi 559158796 220 D----IYNRPASRFVASFV 234
Cdd:PRK14243 241 DrtekIFNSPQQQATRDYV 259
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
9.74e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 9.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHD-FNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG-------KDVVNLRpnqR 75
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkKSLLEVR---K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 NIGMVFQAY--ALFPNmTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQ 153
Cdd:PRK13639 79 TVGIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-223 |
1.14e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 121.92 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDvVNLRP----NQRN 76
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDED-ISLLPlharARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDAT-VKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVL 155
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 156 LLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-222 |
1.58e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.92 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIdGKDVVN-------LRPNQRNIGMVFQayalFPNM--- 90
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSstskqkeIKPVRKKVGVVFQ----FPESqlf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 91 --TVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:PRK13643 99 eeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 168 IRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIY 222
Cdd:PRK13643 179 ARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-225 |
1.75e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 128.15 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFPNmTVAQN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLagLDVQAVRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVsgksrseidaTVKEMLSLIRLDHLAD---RYPYQM-----------SGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:TIGR03797 547 IAGGAPL----------TLDEAWEAARMAGLAEdirAMPMGMhtvisegggtlSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 162 SALDAKIRISLREEIraiqQKLGITTVFVTHdqeeALSI---SDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:TIGR03797 617 SALDNRTQAIVSESL----ERLKVTRIVIAH----RLSTirnADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-223 |
2.45e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 122.42 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 23 NLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNG-------SIEIDGKDVVNLRPNQRNIGMVFQ--AYALFPNmTVA 93
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 QNVSFGLRVSGKSRSEIDATVKEMLSLIRL-DHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISL 172
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 173 REEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK13645 190 INLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-235 |
2.54e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 122.13 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 8 NLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRM-------IAGFETpdNGSIEIDGKDVVNLR---PNQRNI 77
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSIFNYRdvlEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPnMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL-DHLADRY---PYQMSGGQQQRVALARALATKP 152
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 153 QVLLLDEPLSALDAKIRISLREEIRAIQQKLgiTTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP----ASR 228
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTAR 260
|
....*..
gi 559158796 229 FVASFVG 235
Cdd:PRK14271 261 YVAGLSG 267
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
3.57e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 126.25 E-value: 3.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQAYALFPNmT 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGLRvsGKSRSEIDATVK-----EMLSLIR--LDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:TIGR02857 412 IAENIRLARP--DASDAEIREALEragldEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 559158796 165 DAKIRISLREEIRAIQQklGITTVFVTHDqEEALSISDRIVVM 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-211 |
4.56e-32 |
|
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: 125.92 E-value: 4.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFPNmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVS-FGLRVSgkSRSEIDAT----VKEMLslIRLDHLADRY----PYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:TIGR01842 408 VAENIArFGENAD--PEKIIEAAklagVHELI--LRLPDGYDTVigpgGATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 163 ALDAKIRISLREEIRAIQQKlGITTVFVTHdQEEALSISDRIVVMHEGR 211
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGR 530
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-214 |
5.12e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 119.82 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGM 79
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNmTVAQNVSFGLRVSGKsRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQ-QPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEaLSISDRIVVM--HEGRADQ 214
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQE 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-211 |
1.05e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 121.35 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRP-NQRNIGMVF-QAYALFPNMTVAQnv 96
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKeFARRIGVVFgQRSQLWWDLPAID-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 97 SFGL--RVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLRE 174
Cdd:COG4586 116 SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 559158796 175 EIRAIQQKLGITTVFVTHDQE--EALsiSDRIVVMHEGR 211
Cdd:COG4586 196 FLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGR 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-224 |
1.17e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 10 KKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdVVNLrpnqRNIGMVFQayalfPN 89
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL----LELGAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 90 MTVAQNVSFGLRVSGKSRSEIDAtvkemlsliRLDHLAD-------------RYpyqmSGGQQQRVALARALATKPQVLL 156
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDE---------KFDEIVEfaelgdfidqpvkTY----SSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-218 |
1.68e-31 |
|
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: 118.48 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFPNmTVAQN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrdISRKSLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKSRSEIDATVKEMLSLIRldHLADRYPYQM-------SGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:cd03254 97 IRLGRPNATDEEVIEAAKEAGAHDFIM--KLPNGYDTVLgenggnlSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 559158796 169 RISLREEIRAIQQklGITTVFVTHdqeeALSI---SDRIVVMHEGRADQIGSP 218
Cdd:cd03254 175 EKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTH 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
1.87e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 120.19 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNT-----VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKD-------------- 66
Cdd:PRK13651 5 VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 67 ------------VVNLRPNQRNIGMVFQ--AYALFPNmTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLD-HLADRYP 131
Cdd:PRK13651 85 eklviqktrfkkIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 132 YQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIslreEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMH 208
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVK----EILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*
gi 559158796 209 EGRADQIGSPFDIYN 223
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
4.68e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.73 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN------LRPNQRNIGMVFQayalFPNM-- 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 91 ---TVAQNVSFGLRVSGKSRSEI-DATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDA 166
Cdd:PRK13646 99 fedTVEREIIFGPKNFKMNLDEVkNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 167 KIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYN 223
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-197 |
6.18e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR---- 75
Cdd:PRK10584 7 VEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 --NIGMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLI----RLDHLadryPYQMSGGQQQRVALARALA 149
Cdd:PRK10584 87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLglgkRLDHL----PAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 150 TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEA 197
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-222 |
7.94e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.03 E-value: 7.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-------VNLRpnqRNIGMVFQA--YALFpNMT 91
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglMKLR---ESVGMVFQDpdNQLF-SAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 172 LREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIY 222
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-234 |
1.08e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 117.07 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGK-----------DVVNLRp 72
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqiDAIKLR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 nqRNIGMVFQAYALFPNMTVAQNVSFGLRVSG-KSRSEIDATVKEMLSLIRL-DHLADRY---PYQMSGGQQQRVALARA 147
Cdd:PRK14246 90 --KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 148 LATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlgITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPAS 227
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
....*..
gi 559158796 228 RFVASFV 234
Cdd:PRK14246 246 ELTEKYV 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-211 |
1.17e-30 |
|
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: 116.28 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 17 TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVF-QAYALFPNMTVAQ 94
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLRE 174
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 559158796 175 EIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-229 |
1.19e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 121.74 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 9 LKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTT----VLRMIAGfetpdNGSIEIDGKDVVNLRPNQ-----RNIGM 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllpvrHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQ--AYALFPNMTVAQNVSFGLRVSGK--SRSEIDATVKEMLSLIRLD-HLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 155 LLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRF 229
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-213 |
1.21e-30 |
|
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: 122.67 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQAYALFpNMTVAQN 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGlrvsgkSRSEIDATVKEMLSLIRLDHLADRYP--YQM---------SGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:TIGR03375 559 IALG------APYADDEEILRAAELAGVTEFVRRHPdgLDMqigergrslSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 559158796 165 DAKiriSLREEIRAIQQKL-GITTVFVTHDQeEALSISDRIVVMHEGR--AD 213
Cdd:TIGR03375 633 DNR---SEERFKDRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRivAD 680
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-250 |
4.30e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.85 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN---LRPNQRNIGM 79
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQ-AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:PRK13644 82 VFQnPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 159 EPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEaLSISDRIVVMHEGRADQIGSPFDIYNRPASRfvasfvgTLN 238
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ-------TLG 232
|
250
....*....|..
gi 559158796 239 MLEASVSEPAQN 250
Cdd:PRK13644 233 LTPPSLIELAEN 244
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-217 |
4.69e-30 |
|
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: 114.89 E-value: 4.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQAYALFpNMTVAQN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGlrVSGKSRSEIDATVK-----EMLSLIRL--DHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAki 168
Cdd:cd03252 96 IALA--DPGMSMERVIEAAKlagahDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 169 rislrEEIRAIQQKL-----GITTVFVTHdQEEALSISDRIVVMHEGRADQIGS 217
Cdd:cd03252 172 -----ESEHAIMRNMhdicaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
5.44e-30 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.91 E-value: 5.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF-----GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEI----DGKDVVNLRPNQ 74
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RN-----IGMVFQAYALFPNMTVAQNV--SFGLrvsgksrsEIDATVKEMLSLIRL----------DHLADRYPYQMSGG 137
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGL--------ELPDELARMKAVITLkmvgfdeekaEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 138 QQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....
gi 559158796 218 PFDI 221
Cdd:TIGR03269 512 PEEI 515
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-235 |
7.47e-30 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 115.27 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT---------VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRP 72
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 NQRNIGMVFQ--AYALFPNMTVAQNVSFGLRV----SGKSRSE-IDATVKeMLSLIRlDHlADRYPYQMSGGQQQRVALA 145
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLntdlEPEQREKqIIETLR-QVGLLP-DH-ASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 146 RALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
250
....*....|....
gi 559158796 226 ----ASRFVASFVG 235
Cdd:PRK15112 242 lhelTKRLIAGHFG 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
1.82e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 115.33 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT-----VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIdgKDVVN--------- 69
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIgdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 -LRPNQRNI----------GMVFQ--AYALFPNmTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDH-LADRYPYQMS 135
Cdd:PRK13631 100 iTNPYSKKIknfkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 136 GGQQQRVALARALATKPQVLLLDEPLSALDAKiriSLREEIRAIQ--QKLGITTVFVTHDQEEALSISDRIVVMHEGRAD 213
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPK---GEHEMMQLILdaKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|...
gi 559158796 214 QIGSPFDIYNRPA 226
Cdd:PRK13631 256 KTGTPYEIFTDQH 268
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-242 |
2.85e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.42 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF----GTNTVVHDFNLAVGKGEFVSFLGPSGCGKT-TVLRMIAGFETPdNGSIEIDG-------KDVVNLR 71
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKmllrrrsRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 72 PNQR---------NIGMVFQA--YALFPNMTVAQNVSFGLRV-SGKSRSEIDATVKEMLSLIRL---DHLADRYPYQMSG 136
Cdd:PRK10261 92 EQSAaqmrhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 137 GQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....*.
gi 559158796 217 SPFDIYNRPASRFVASFVGTLNMLEA 242
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-221 |
3.18e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.54 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 7 KNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAY 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 85 ALFPNMTVAQNVSFGLR----VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:PRK10253 91 TTPGDITVQELVARGRYphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI 221
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-225 |
3.22e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.77 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV------NLRPNQRNIGMVFQ--AYALFPNmTV 92
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVSFGLRVSGKSRSEIDATVKEMLSLIRL-DHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 172 LReEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK13641 184 MM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-210 |
3.48e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 117.46 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN---QRNIGMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADrypyQMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 559158796 161 LSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEG 210
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-226 |
1.62e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 112.90 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPD---NGSIEIDGKDVVNLRPN 73
Cdd:PRK09473 10 DALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 74 QRN------IGMVFQ--AYALFPNMTVAQNVSFGLRV-SGKSRSE-IDATVKeMLSLIRLDHLADR---YPYQMSGGQQQ 140
Cdd:PRK09473 90 ELNklraeqISMIFQdpMTSLNPYMRVGEQLMEVLMLhKGMSKAEaFEESVR-MLDAVKMPEARKRmkmYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 141 RVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFD 220
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
....*.
gi 559158796 221 IYNRPA 226
Cdd:PRK09473 249 VFYQPS 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
1.86e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.25 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 12 SFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGmvfqayALFPnMT 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGL----RVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:NF040873 74 VRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 559158796 168 IRISLREEIRAIQQKlGITTVFVTHDQEEALSIsDRIVVM 207
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVRRA-DPCVLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-225 |
2.63e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.72 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 29 GEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-----RNIGMVFQ-AYA-LFPNMTVAQNVSFGLR 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQdPYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 102 VSGKSRSEIDAT-VKEMLSLIRL--DHlADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRA 178
Cdd:PRK10261 430 VHGLLPGKAAAArVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 559158796 179 IQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:PRK10261 509 LQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-192 |
3.82e-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: 108.60 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAvgKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVFQAYALFPNMTVAQNVSFG 99
Cdd:TIGR01189 20 SFTLN--AGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 100 LRVSGKSrseiDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAI 179
Cdd:TIGR01189 98 AAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|...
gi 559158796 180 QQKLGItTVFVTH 192
Cdd:TIGR01189 174 LARGGI-VLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-242 |
6.15e-28 |
|
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: 115.50 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGT--NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-VNLRPNQRNIGMVFQ 82
Cdd:TIGR01257 931 VKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 163 ALDAKIRISLREEIraIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFVASFVGTLNMLEA 242
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQS 1168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-211 |
7.49e-28 |
|
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: 107.64 E-value: 7.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 17 TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAG--FETPDNGSIEIDGKDVVNLRPNQRnIGMVFQAYALFPNMTVAQ 94
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSFGLRVSGksrseidatvkemlslirldhladrypyqMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLRE 174
Cdd:cd03213 102 TLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 559158796 175 EIRAIQQkLGITTVFVTHD-QEEALSISDRIVVMHEGR 211
Cdd:cd03213 153 LLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
8.78e-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: 8.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGkdvvNLRpnqrnIGMVFQAYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GLR-----IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 LFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLS----LIRLDHLADRY------------------------PYQ---- 133
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEELEAKLAEpdedLERLAELQEEFealggweaearaeeilsglgfpeeDLDrpvs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 134 -MSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQqklgITTVFVTHD 193
Cdd:COG0488 152 eLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
6.86e-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: 103.68 E-value: 6.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIeidgkdvvnlrpnqrnigmvfqa 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 yalfpnmTVAQNVSFGlrvsgksrseidatvkemlslirldHLAdrypyQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:cd03221 58 -------TWGSTVKIG-------------------------YFE-----QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 164 LDAKIRISLREEIRAIQQklgiTTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
8.70e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 108.29 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTV----VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGF-ETPDN---GSIEIDGKDVVNLRP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGRvmaEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 NQR------NIGMVFQ--AYALFPNMTVAQNVSFGLRV-SGKSRSEIDATVKEMLSLIRLDHLADR---YPYQMSGGQQQ 140
Cdd:PRK11022 81 KERrnlvgaEVAMIFQdpMTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 141 RVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFD 220
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*
gi 559158796 221 IYNRP 225
Cdd:PRK11022 241 IFRAP 245
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-211 |
1.35e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 110.58 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpNMTVAQN 95
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLadYTLASLRRQVALVSQDVVLF-NDTIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGlRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQ-------MSGGQQQRVALARALATKPQVLLLDEPLSALDAki 168
Cdd:TIGR02203 426 IAYG-RTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengvlLSGGQRQRLAIARALLKDAPILILDEATSALDN-- 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 169 rislrEEIRAIQQKL-----GITTVFVTHdqeeALSI---SDRIVVMHEGR 211
Cdd:TIGR02203 503 -----ESERLVQAALerlmqGRTTLVIAH----RLSTiekADRIVVMDDGR 544
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-211 |
1.59e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.35 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN---LRPNQRNI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGLRVSgkSRSEIDATVKEMLSLI-RLDHLADRYPYQMSGGQQQRVALARALATKPQVLL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 157 LDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-211 |
1.83e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 110.29 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 20 HDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpNMTVAQNVS 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdVTQASLRAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 98 FGlrvsgksrsEIDATVKEMLSLIRLDHLAD---RYP--YQ---------MSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:COG5265 454 YG---------RPDASEEEVEAAARAAQIHDfieSLPdgYDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 164 LDAkirislREEiRAIQQKL-----GITTVFVTHdqeeALSI---SDRIVVMHEGR 211
Cdd:COG5265 525 LDS------RTE-RAIQAALrevarGRTTLVIAH----RLSTivdADEILVLEAGR 569
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-211 |
2.01e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIdGKDVvnlrpnqrNIGMVFQA 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALF-PNMTVAQNVSfglRVS-GKSRSEIDATVKEML-------SLIRldhladrypyQMSGGQQQRVALARALATKPQV 154
Cdd:COG0488 387 QEELdPDKTVLDELR---DGApGGTEQEVRGYLGRFLfsgddafKPVG----------VLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 155 LLLDEPLSALDAkirislrEEIRAIQQKL----GiTTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG0488 454 LLLDEPTNHLDI-------ETLEALEEALddfpG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-216 |
2.90e-26 |
|
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: 105.30 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL------RPNQR 75
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlsEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 NI-----GMVFQAYALFPNMTVAQNVSFGLR---VSGKSRSEIDATVKEMLSLIRLDH-LADRYPYQMSGGQQQRVALAR 146
Cdd:TIGR02323 82 RLmrtewGFVHQNPRDGLRMRVSAGANIGERlmaIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 147 ALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-211 |
3.33e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.86 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAG---FETPDnGSIEIDGKDVV--NLRPNQRN-I 77
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvypHGTYE-GEIIFEGEELQasNIRDTERAgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATV---KEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQV 154
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 155 LLLDEPLSALDAK-IRIsLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK13549 165 LILDEPTASLTESeTAV-LLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
4.37e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLK-KSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ-RNIGMVF 81
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 -----QAYALFPNMTVAQNVSFGLRVSGK-------SRSEIDATVKEMLSL--IR---LDHLADrypyQMSGGQQQRVAL 144
Cdd:COG3845 338 ipedrLGRGLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEfdVRtpgPDTPAR----SLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-211 |
5.10e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.39 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN--TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRN-IGMV 80
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFpNMTVAQNVsfGLRvsgksrseidatvkemlslirldhladrypyqMSGGQQQRVALARALATKPQVLLLDEP 160
Cdd:cd03247 81 NQRPYLF-DTTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 161 LSALDAKIRISLREEIraIQQKLGITTVFVTHdQEEALSISDRIVVMHEGR 211
Cdd:cd03247 126 TVGLDPITERQLLSLI--FEVLKDKTLIWITH-HLTGIEHMDKILFLENGK 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-220 |
5.42e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.90 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpNMT 91
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrtVTRASLRRNIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNvsfgLRVsGKSrseiDATVKEML--------------SLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLL 157
Cdd:PRK13657 425 IEDN----IRV-GRP----DATDEEMRaaaeraqahdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 158 DEPLSALDAKIRISLREEIRAIQQklGITTVFVTHdqeeALSI---SDRIVVMHEGRADQIGSpFD 220
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMK--GRTTFIIAH----RLSTvrnADRILVFDNGRVVESGS-FD 554
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-211 |
5.57e-26 |
|
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: 102.93 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 10 KKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdvvnlrpnqrnIGMVFQaYALFPN 89
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQ-EPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 90 MTVAQNVSFGlrvsgksrSEIDA----TVKEMLSLIR-LDHLADRYPYQ-------MSGGQQQRVALARALATKPQVLLL 157
Cdd:cd03250 80 GTIRENILFG--------KPFDEeryeKVIKACALEPdLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 158 DEPLSALDAKIRISLREeiRAIQQKL--GITTVFVTHdQEEALSISDRIVVMHEGR 211
Cdd:cd03250 152 DDPLSAVDAHVGRHIFE--NCILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-211 |
1.31e-25 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 107.22 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPD--NGSIEIDGKDVV--NLRPNQR-NIG 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKasNIRDTERaGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQNVSFGLRVSGK-SRSEIDATV---KEMLSLIRLDHLADRYPY-QMSGGQQQRVALARALATKPQ 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPgGRMAYNAMYlraKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-211 |
2.99e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.07 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFE--TPDNGSIEIDGKDVVNLRPNQR---NIG 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQnvsFgLR--VSGKSRSEIDA-----TVKEMLSLIRLDH-LADRY-PYQMSGGQQQRVALARALA 149
Cdd:COG0396 81 LAFQYPVEIPGVSVSN---F-LRtaLNARRGEELSAreflkLLKEKMKELGLDEdFLDRYvNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 150 TKPQVLLLDEPLSALDA-KIRIsLREEIRAIQQKlGITTVFVTHdQEEALSI--SDRIVVMHEGR 211
Cdd:COG0396 157 LEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGR 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-280 |
3.43e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSF----GTNTVVHDFNLAVGKGEFVSFLGPSGCGKT-TVLRMIAGFETPD----NGSIEIDGKDVVN-- 69
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 70 ------LRPNQrnIGMVFQA--YALFPNMTVAQNVSFGLRVSGKSRSEidATVKEMLSL-----IR--LDHLADrYPYQM 134
Cdd:PRK15134 83 eqtlrgVRGNK--IAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRRE--AARGEILNCldrvgIRqaAKRLTD-YPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 135 SGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQ 214
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 215 IGSPFDIYNRPASRFvasfvgTLNMLEAS-----VSEPAQNSIDLDGRQITV---------QETLAHHPKGKPLTLALRP 280
Cdd:PRK15134 238 QNRAATLFSAPTHPY------TQKLLNSEpsgdpVPLPEPASPLLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRP 311
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-211 |
5.04e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.93 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL------RPNQRNI 77
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalsEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 -----GMVFQ--AYALFPNMTVAQNVS-----FGLRVSGKSRS---------EIDATvkemlsliRLDHLadryPYQMSG 136
Cdd:PRK11701 87 lrtewGFVHQhpRDGLRMQVSAGGNIGerlmaVGARHYGDIRAtagdwlervEIDAA--------RIDDL----PTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 137 GQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-193 |
8.26e-25 |
|
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: 105.14 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFpNMT 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGlrvsgksRSEI-DATVKEMLSLIRLDHLADRYPYQM-----------SGGQQQRVALARALATKPQVLLLDE 159
Cdd:TIGR02868 425 VRENLRLA-------RPDAtDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 559158796 160 PLSALDAKIRISLREEIRAIQQklGITTVFVTHD 193
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-192 |
1.05e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 17 TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEidgkdvvnlRPNQRNigMVF---QAYalFPNMTVA 93
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAGAR--VLFlpqRPY--LPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 QNVSFGLRVSGKSrseiDATVKEMLSLIRLDHLADRY------PYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:COG4178 444 EALLYPATAEAFS----DAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|....*.
gi 559158796 168 IRISLreeIRAIQQKL-GITTVFVTH 192
Cdd:COG4178 520 NEAAL---YQLLREELpGTTVISVGH 542
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-262 |
3.53e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 103.34 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFET--PDNGSI----------------EIDGK 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 66 --------------DVVNL-----RPNQRNIGMVFQ-AYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDH 125
Cdd:TIGR03269 81 pcpvcggtlepeevDFWNLsdklrRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 126 LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIV 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 206 VMHEGRADQIGSPFDIynrpASRFVASFVGTLNMLEASVSEPAQNSIDLDGRQITVQ 262
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV----VAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVD 293
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-166 |
5.92e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRnigmvfQA 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA------CH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 Y-----ALFPNMTVAQNVSFGLRVSGKSRSEIDATvkemLSLIRLDHLADRyPYQM-SGGQQQRVALARALATKPQVLLL 157
Cdd:PRK13539 77 YlghrnAMKPALTVAENLEFWAAFLGGEELDIAAA----LEAVGLAPLAHL-PFGYlSAGQKRRVALARLLVSNRPIWIL 151
|
....*....
gi 559158796 158 DEPLSALDA 166
Cdd:PRK13539 152 DEPTAALDA 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-193 |
7.31e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 98.65 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEidgkdvvnlRPNQRNIGMVFQAYA 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 LFPnmTVAQNVSFGLRVSGKSRSeidATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALD 165
Cdd:PRK09544 78 LDT--TLPLTVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*...
gi 559158796 166 AKIRISLREEIRAIQQKLGITTVFVTHD 193
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-217 |
8.01e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 8.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAvgKGEFVSFLGPSGCGKTTVLRMIAGFeTPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFPNmTVAQNVSF 98
Cdd:PRK11174 370 NFTLP--AGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 GlrvsgksrsEIDATVKEMLSLIR-------LDHLADRYPYQ-------MSGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:PRK11174 446 G---------NPDASDEQLQQALEnawvsefLPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 165 DAKiriSLREEIRAIQQ-KLGITTVFVTHdQEEALSISDRIVVMHEGRADQIGS 217
Cdd:PRK11174 517 DAH---SEQLVMQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-225 |
8.10e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNIGMVFQAYALFpNMTVAQN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLHRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKSrsEIDATVKEMLSLIRLDHLADRYPY-------QMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:TIGR00958 575 IAYGLTDTPDE--EIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 169 RISLREEiraiQQKLGITTVFVTHDqeeaLSI---SDRIVVMHEGRADQIGSPFDIYNRP 225
Cdd:TIGR00958 653 EQLLQES----RSRASRTVLLIAHR----LSTverADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-211 |
1.92e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.77 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVvNLRPNQ---RNIGMVFQAYALFPNmTVAQ 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKylhSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSFGLR-------VSGKSRSEIDATVKEMLSLIRLDhlADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:cd03248 107 NIAYGLQscsfecvKEAAQKAHAHSFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 559158796 168 IRISLREeirAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:cd03248 185 SEQQVQQ---ALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-242 |
2.95e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.46 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLkksfgTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNiGMVF 81
Cdd:PRK10762 258 LKVDNL-----SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglAN-GIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 -----QAYALFPNMTVAQNVSF-GLRVSGKSRSEIDATVKEML--SLIRLDHLadRYPYQ------MSGGQQQRVALARA 147
Cdd:PRK10762 332 isedrKRDGLVLGMSVKENMSLtALRYFSRAGGSLKHADEQQAvsDFIRLFNI--KTPSMeqaiglLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 148 LATKPQVLLLDEPLSALDakirISLREEI-RAIQQ--KLGITTVFVTHDQEEALSISDRIVVMHEGRadqIGSPFDIYNR 224
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVD----VGAKKEIyQLINQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGR---ISGEFTREQA 482
|
250
....*....|....*...
gi 559158796 225 PASRFVASFVGTLNMLEA 242
Cdd:PRK10762 483 TQEKLMAAAVGKLNRVNQ 500
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-211 |
5.37e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.20 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 7 KNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSI-----EIDGKDvVNLRpnqRNIGMVF 81
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGD-IATR---RRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:NF033858 346 QAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 162 SALDAKIR-------ISL-REEiraiqqklGItTVFV-THDQEEALSiSDRIVVMHEGR 211
Cdd:NF033858 426 SGVDPVARdmfwrllIELsRED--------GV-TIFIsTHFMNEAER-CDRISLMHAGR 474
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-167 |
7.22e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.49 E-value: 7.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 3 FLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVF 81
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRypyQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....*.
gi 559158796 162 SALDAK 167
Cdd:PRK13538 158 TAIDKQ 163
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-211 |
1.07e-22 |
|
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: 94.13 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFE--TPDNGSIEIDGKDVVNLRPNQR---NIG 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQ-----NVSFglrvsgksrseidatvkemlslirldhladrypyqmSGGQQQRVALARALATKPQ 153
Cdd:cd03217 81 LAFQYPPEIPGVKNADflryvNEGF------------------------------------SGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 154 VLLLDEPLSALDAKiriSLREEIRAIQQ--KLGITTVFVTHDQEEALSI-SDRIVVMHEGR 211
Cdd:cd03217 125 LAILDEPDSGLDID---ALRLVAEVINKlrEEGKSVLIITHYQRLLDYIkPDRVHVLYDGR 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-211 |
2.16e-22 |
|
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: 93.87 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFEtpDNGSIeIDGKDVVNLRPN-----QRNIGMVFQAYALFPNMTV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGT-TSGQILFNGQPRkpdqfQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVSFGLRV------SGKSRSEIDATVkeMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDA 166
Cdd:cd03234 99 RETLTYTAILrlprksSDAIRKKRVEDV--LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 167 KIRISLREEIR--AIQQKLGITTVfvtHD-QEEALSISDRIVVMHEGR 211
Cdd:cd03234 177 FTALNLVSTLSqlARRNRIVILTI---HQpRSDLFRLFDRILLLSSGE 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-192 |
2.64e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 92.94 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN-QRNIGMVFQ 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGksrseiDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 559158796 163 ALDAKIRISLREEIRAIQQKLGItTVFVTH 192
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGM-VVLTTH 183
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-211 |
1.42e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFeTPDNGSIEIDGKDVVNLRPNQ--RNIGMVFQAYALFPNMTVAQNVSFG 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 100 LRVSGkSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARAL-----ATKP--QVLLLDEPLSALDAKIRISL 172
Cdd:COG4138 94 QPAGA-SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 559158796 173 REEIRAIQQkLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:COG4138 173 DRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-202 |
1.58e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 90.78 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-VNLRPNQRNIGMVFQ 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNMTVAQNVSFGLRVSGKSRsEIDatvkEMLSLIRLDHLADrYPYQM-SGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAV-GIT----ELCRLFSLEHLID-YPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 559158796 162 SALDAKIRISLREEIRAIQQKLGitTVFVTHDQEEALSISD 202
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGG--AVLLTSHQDLPLNKAD 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-224 |
4.47e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.42 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNT-VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQ--RNIGMV 80
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQAYALFPNmTVAQNVSFGLRvSGKSRSEIDATVKemLSLIRLDHLADRYPYQ---------MSGGQQQRVALARALATK 151
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK-ENVSQDEIWAACE--IAEIKDDIENMPLGYQtelseegssISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 152 PQVLLLDEPLSALDAKIRISLREEIRAIQQKlgiTTVFVTHDQEEAlSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-235 |
5.53e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.82 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVnlRPNQRN---- 76
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAalaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 -IGMVFQAYALFPNMTVAQNVSFGlRVSGKS----RSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATK 151
Cdd:PRK11288 80 gVAIIYQELHLVPEMTVAENLYLG-QLPHKGgivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 152 PQVLLLDEPLSALDAK--------IRiSLREEIRAIqqklgittVFVTHDQEEALSISDRIVVMHEGRadQIGSPFDIYN 223
Cdd:PRK11288 159 ARVIAFDEPTSSLSAReieqlfrvIR-ELRAEGRVI--------LYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQ 227
|
250
....*....|..
gi 559158796 224 RPASRFVASFVG 235
Cdd:PRK11288 228 VDRDQLVQAMVG 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-218 |
8.50e-21 |
|
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: 89.01 E-value: 8.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN--TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGM 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFpnmtvaqnvsfglrvSGKSRSEIDatvkemlsliRLDHLADRYPYQ----------MSGGQQQRVALARALA 149
Cdd:cd03369 87 IPQDPTLF---------------SGTIRSNLD----------PFDEYSDEEIYGalrvsegglnLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 150 TKPQVLLLDEPLSAL----DAKIRISLREEIRaiqqklGITTVFVTHdQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:cd03369 142 KRPRVLVLDEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-211 |
1.06e-20 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 88.47 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNI-KNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGfETPDNGSIE-------IDGKDvvNLRP 72
Cdd:cd03233 4 LSWRNIsFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSVEgdihyngIPYKE--FAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 NQRNIGMVFQAYALFPNMTVAQNVSFGLRVSGksrseidatvkemlslirldhlaDRYPYQMSGGQQQRVALARALATKP 152
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 153 QVLLLDEPLSALDAKIRISLREEIRAIQQKLGiTTVFVTHDQ--EEALSISDRIVVMHEGR 211
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADVLK-TTTFVSLYQasDEIYDLFDKVLVLYEGR 197
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-225 |
1.10e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 91.12 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNT----VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFeTPDNGSIEID-----GKDVVNLR 71
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 72 PNQR------NIGMVFQ---AYaLFPNMTVAQNVSFGL---RVSGK------SRSEIdatVKEMLSL--IRlDHLA--DR 129
Cdd:COG4170 80 PRERrkiigrEIAMIFQepsSC-LDPSAKIGDQLIEAIpswTFKGKwwqrfkWRKKR---AIELLHRvgIK-DHKDimNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 130 YPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHE 209
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYC 234
|
250
....*....|....*.
gi 559158796 210 GRADQIGSPFDIYNRP 225
Cdd:COG4170 235 GQTVESGPTEQILKSP 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-211 |
1.66e-20 |
|
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: 92.20 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAG-FETPDNGSIEIDGKDVVNLRPNQ---RNIGMV---FQAYALFPNMT 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAQairAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVSFGL--RVSGKSRSEIDATVKEMLSLIRLDHLADRYPY----QMSGGQQQRVALARALATKPQVLLLDEPLSALD 165
Cdd:TIGR02633 356 VGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 559158796 166 AKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
2.21e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 92.31 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIdGKDVVnlrpnqrnIGMVFQA 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 Y-ALFPNMTVAQNVSFGLrvsgksrSEIDATVKEMLSLIRLDHL----ADRYPY--QMSGGQQQRVALARALATKPQVLL 156
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGL-------DIIKLGKREIPSRAYVGRFnfkgSDQQKKvgQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 559158796 157 LDEPLSALDAkirislrEEIRAIQQKL---GITTVFVTHD 193
Cdd:TIGR03719 467 LDEPTNDLDV-------ETLRALEEALlnfAGCAVVISHD 499
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-211 |
2.37e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.91 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAG-FETPDNGSIEIDGKDVVNLRPNQ---RNIGMVFQ---AYALFPNM 90
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEdrkRDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 91 TVAQNVSFGL--RVSGKSR----SEIDATVKEMLSL-IRLDHLADRYPyQMSGGQQQRVALARALATKPQVLLLDEPLSA 163
Cdd:PRK13549 357 GVGKNITLAAldRFTGGSRiddaAELKTILESIQRLkVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 164 LDakirISLREEI-RAIQQ--KLGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK13549 436 ID----VGAKYEIyKLINQlvQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-192 |
3.66e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 86.05 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 16 NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEidgkdvvnlRPNQRNIGMVFQAyalfPNMTvaqn 95
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MPEGEDLLFLPQR----PYLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 vsfglrvsgksrseiDATVKEMLSlirldhladrYPYQM--SGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLR 173
Cdd:cd03223 77 ---------------LGTLREQLI----------YPWDDvlSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 559158796 174 EEIRaiqqKLGITTVFVTH 192
Cdd:cd03223 132 QLLK----ELGITVISVGH 146
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-224 |
3.82e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV----VNLRPNQRNIGMVFQAyalfPNMTV- 92
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLALRQQVATVFQD----PEQQIf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 ----AQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRyPYQ-MSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:PRK13638 92 ytdiDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 168 IRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-221 |
4.58e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.31 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 17 TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV--NLRPNQRNIGMVFQAYALFPNMTVAQ 94
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSFGLR----VSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRI 170
Cdd:PRK10575 105 LVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 171 SLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDI 221
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-206 |
4.64e-20 |
|
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: 87.85 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEF-----VSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVvNLRPNQrnIGMVFQayalfpnMTVAQN 95
Cdd:cd03237 12 EFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQY--IKADYE-------GTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKS---RSEIdatvkemLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISL 172
Cdd:cd03237 82 LSSITKDFYTHpyfKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 559158796 173 REEIRAIQQKLGITTVFVTHDQEEALSISDRIVV 206
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-228 |
9.19e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.45 E-value: 9.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKT----TVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQA--YALFPNMTV 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVSFGLRVSGKSRSeiDATVKEMLSLIRLDH---LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALD--AK 167
Cdd:PRK10418 99 HTHARETCLALGKPAD--DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDvvAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158796 168 IRI-SLREEIRAiQQKLGIttVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASR 228
Cdd:PRK10418 177 ARIlDLLESIVQ-KRALGM--LLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-221 |
9.66e-20 |
|
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: 90.23 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 8 NLKKSFGtntvvhDFNLAVG-----KGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDgkdvvnlrpnqrnigmvfq 82
Cdd:COG1245 346 DLTKSYG------GFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 ayalfpnmtvaqnvsfgLRVSGKS---RSEIDATVKEMLS---------------LIR---LDHLADRYPYQMSGGQQQR 141
Cdd:COG1245 401 -----------------LKISYKPqyiSPDYDGTVEEFLRsantddfgssyykteIIKplgLEKLLDKNVKDLSGGELQR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 142 VALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDqeeaLS----ISDRIVVM-----HEGRA 212
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYlidyISDRLMVFegepgVHGHA 539
|
....*....
gi 559158796 213 DqigSPFDI 221
Cdd:COG1245 540 S---GPMDM 545
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-210 |
1.39e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 3 FLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN---QRNIGM 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLRVSGK-------SRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 153 QVLLLDEPLSALDAK-------IRISLREEIRAIqqklgittVFVTHDQEEALSISDRIVVMHEG 210
Cdd:PRK09700 165 KVIIMDEPTSSLTNKevdylflIMNQLRKEGTAI--------VYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-211 |
1.46e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 20 HDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV-----VNLRpnqRNIGMVFQAYALFpNMTVAQ 94
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlASLR---NQVALVSQNVHLF-NDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSFGlRVSGKSRSEIDATVK---EMLSLIRLDHLADRYPYQ----MSGGQQQRVALARALATKPQVLLLDEPLSALDAk 167
Cdd:PRK11176 436 NIAYA-RTEQYSREQIEEAARmayAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDT- 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 168 irislrEEIRAIQQKLGI----TTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11176 514 ------ESERAIQAALDElqknRTSLVIAHRLSTIEKADEILVVEDGE 555
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-221 |
1.83e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.48 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 8 NLKKSFGtntvvhDFNLAVG-----KGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDgkdvvnlrpnqrnigmvfq 82
Cdd:PRK13409 345 DLTKKLG------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 ayalfpnmtvaqnvsfgLRVSGKS---RSEIDATVKEMLSLI-----------------RLDHLADRYPYQMSGGQQQRV 142
Cdd:PRK13409 400 -----------------LKISYKPqyiKPDYDGTVEDLLRSItddlgssyykseiikplQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 143 ALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHD---QEealSISDRIVVM-----HEGRADq 214
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDiymID---YISDRLMVFegepgKHGHAS- 538
|
....*..
gi 559158796 215 igSPFDI 221
Cdd:PRK13409 539 --GPMDM 543
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-217 |
3.76e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGT-NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL--RPNQRNIGMV 80
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 81 FQ-----AYALFPNMTVAQNVSfglrvsgksrseiDATVKEMLSLIRLDHLADRYP-----------YQMSGGQQQRVAL 144
Cdd:PRK10790 421 QQdpvvlADTFLANVTLGRDIS-------------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 145 ARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlgiTTVFVTHDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-211 |
3.85e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 20 HDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdVVNLRPNQRNI--GMVF-----QAYALFPNMTV 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK-PIDIRSPRDAIraGIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVS---------FGLRVSGKSRSEidatvkemlslirldhLADRYPYQM--------------SGGQQQRVALARALA 149
Cdd:PRK11288 349 ADNINisarrhhlrAGCLINNRWEAE----------------NADRFIRSLniktpsreqlimnlSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 150 TKPQVLLLDEPLSALDakirISLREEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK11288 413 EDMKVILLDEPTRGID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-218 |
5.98e-19 |
|
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: 84.08 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSF--GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTV----LRMIagfeTPDNGSIEIDGKDVVNLRPNQ--RNI 77
Cdd:cd03244 5 FKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYALFPNmTVAQNV-SFGLrvsgKSRSEI-----DATVKEMLS--LIRLDHLADRYPYQMSGGQQQRVALARALA 149
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLdPFGE----YSDEELwqaleRVGLKEFVEslPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 150 TKPQVLLLDEPLSALD----AKIRISLREEIRaiqqklGITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSP 218
Cdd:cd03244 156 RKSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-211 |
6.14e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLkkSFG----TNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV-----NLRpnq 74
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseaALR--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 RNIGMVFQAYALFpNMTVAQNVSFGlrvsgkSRSEIDATVKEMLSLIRLDHLAD-------------RypyQMSGGQQQR 141
Cdd:PRK11160 414 QAISVVSQRVHLF-SATLRDNLLLA------APNASDEALIEVLQQVGLEKLLEddkglnawlgeggR---QLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 142 VALARALATKPQVLLLDEPLSALDAK----IRISLREEiraIQQKlgiTTVFVTHdQEEALSISDRIVVMHEGR 211
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAEterqILELLAEH---AQNK---TVLMITH-RLTGLEQFDRICVMDNGQ 550
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-211 |
1.79e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR-NIGMVF-----QAYALFPNMTVAQ 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSfGLRVSGKS---RSEIDATVKEML--SL-IRLDHlADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:PRK15439 361 NVC-ALTHNRRGfwiKPARENAVLERYrrALnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 559158796 169 RISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-210 |
2.05e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 2 AFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRP---NQRNIG 78
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAYALFPNMTVAQNV--------SFGLRVSGKSRSEIDAtvkeMLSLIRLDHLADRYPYQMSGGQQQRVALARALAT 150
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIflgrefvnRFGRIDWKKMYAEADK----LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 151 KPQVLLLDEPLSALDAKIRISLREEIRAIQ-QKLGIttVFVTHDQEEALSISDRIVVMHEG 210
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGI--VYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-215 |
4.47e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN---QRNIGMVFQAY---ALFPNMTV 92
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVS-------------FGLrVSGKSRSEIDATVKEMLSLirLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:PRK09700 359 AQNMAisrslkdggykgaMGL-FHEVDEQRTAENQRELLAL--KCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 160 PLSALDakirISLREEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGRADQI 215
Cdd:PRK09700 436 PTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-218 |
2.42e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 29 GEFVSFLGPSGCGKTTVLRMIAGFETPD---NGSIEIDGKdVVNLRPNQRNIGMVFQAYALFPNMTVAQNVSF------G 99
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM-PIDAKEMRAISAYVQQDDLFIPTLTVREHLMFqahlrmP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 100 LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQM---SGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEI 176
Cdd:TIGR00955 130 RRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVkglSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 559158796 177 RAIQQKlGITTVFVTHD-QEEALSISDRIVVMHEGRADQIGSP 218
Cdd:TIGR00955 210 KGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-165 |
2.56e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.86 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 7 KNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIdGKDVvnlrpnqrNIGMVFQAY-A 85
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQSRdA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 LFPNMTVAQNVSFGL---RVSGK---SRSEIDA----------TVKemlslirldhladrypyQMSGGQQQRVALARALA 149
Cdd:PRK11819 399 LDPNKTVWEEISGGLdiiKVGNReipSRAYVGRfnfkggdqqkKVG-----------------VLSGGERNRLHLAKTLK 461
|
170
....*....|....*.
gi 559158796 150 TKPQVLLLDEPLSALD 165
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD 477
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-226 |
1.01e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.10 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGfETPD---------NGSIEIDGKDVVNLRPNQ 74
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 75 ---RNIGMVFQAYALFPnMTVAQNVSFG----LRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARA 147
Cdd:PRK13547 81 larLRAVLPQAAQPAFA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 148 LA---------TKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:PRK13547 160 LAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
....*...
gi 559158796 219 FDIYnRPA 226
Cdd:PRK13547 240 ADVL-TPA 246
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-225 |
1.31e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.46 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTN----TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFeTPDNGSI-----EIDGKDVVNLR 71
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVtadrmRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 72 PNQR------NIGMVFQ--AYALFPNMTVAQNVSFGL-----------RVSGKSRSEIdatvkEMLSLIRL-DH--LADR 129
Cdd:PRK15093 80 PRERrklvghNVSMIFQepQSCLDPSERVGRQLMQNIpgwtykgrwwqRFGWRKRRAI-----ELLHRVGIkDHkdAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 130 YPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHE 209
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|....*.
gi 559158796 210 GRADQIGSPFDIYNRP 225
Cdd:PRK15093 235 GQTVETAPSKELVTTP 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-217 |
1.67e-16 |
|
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: 81.21 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF-GTNTVVHDfNLAVG--KGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVV-NLRPNQRNIGM 79
Cdd:TIGR01257 1938 LRLNELTKVYsGTSSPAVD-RLCVGvrPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 160 PLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-216 |
2.39e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.14 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 5 NIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQ 82
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPNmTVAQNVSFGlrvsgksrsEIDATVKEMLSLIRLDHLAD---RYP--YQ---------MSGGQQQRVALARAL 148
Cdd:PRK10789 397 TPFLFSD-TVANNIALG---------RPDATQQEIEHVARLASVHDdilRLPqgYDtevgergvmLSGGQKQRISIARAL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 149 ATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlgiTTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-210 |
9.63e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.38 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 17 TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFE--TPDNGSIEIDgkdvvnlrpnQRNIGmvfqayalfPNMTVAQ 94
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP----------DNQFG---------REASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 95 NVSfglrvsgksrseIDATVKEMLSLIRLDHLAD-----RYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIR 169
Cdd:COG2401 105 AIG------------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 559158796 170 ISLREEIRAIQQKLGITTVFVTHDQE--EALsISDRIVVMHEG 210
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATHHYDviDDL-QPDLLIFVGYG 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-217 |
1.25e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 78.45 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdvVNLRPNQrnigmvfqayALFPNMTVAQNVSF 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ----------AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 GLRVSGKS-RSEIDATVkeMLSLIRLDHLADRYP-----YQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISL 172
Cdd:TIGR00957 722 GKALNEKYyQQVLEACA--LLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 559158796 173 REEIRAIQQKL-GITTVFVTHDQeEALSISDRIVVMHEGRADQIGS 217
Cdd:TIGR00957 800 FEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGS 844
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-217 |
1.36e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 78.24 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGfETP--DNGSIEIDGKdvvnlrpnqrnIGMVFQAYALFpNMTVAQNVSF 98
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPprSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 GLRV-SGKSRSEIDAT-VKEMLSLI---RLDHLADRyPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI----- 168
Cdd:PLN03130 702 GSPFdPERYERAIDVTaLQHDLDLLpggDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrqvf 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 169 RISLREEIRaiqqklGITTVFVThDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:PLN03130 781 DKCIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-193 |
1.44e-15 |
|
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: 77.67 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTN-TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETpdngsiEIDGKdvVNLRPNqRNIGMVFQAY 84
Cdd:TIGR03719 7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFNGE--ARPQPG-IKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 85 ALFPNMTVAQNVSFGLR-----------VSGK---SRSEIDATVKEMLSLI-------------RLDHLAD--RYP---- 131
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAeikdaldrfneISAKyaePDADFDKLAAEQAELQeiidaadawdldsQLEIAMDalRCPpwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 132 --YQMSGGQQQRVALARALATKPQVLLLDEPLSALDAkirislrEEIRAIQQKL----GiTTVFVTHD 193
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLqeypG-TVVAVTHD 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-215 |
1.91e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdvvnlrpnqRNIGMVFQ- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN---------ANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 AYALFPN-MTVAQNVSfglrvSGKSRSEIDATVKEMLSliRLDHLADRYPYQ---MSGGQQQRVALARALATKPQVLLLD 158
Cdd:PRK15064 391 HAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLG--RLLFSQDDIKKSvkvLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 159 EPLSALDAkirislrEEIRAIQQKLGI---TTVFVTHDQEEALSISDRIVvmhEGRADQI 215
Cdd:PRK15064 464 EPTNHMDM-------ESIESLNMALEKyegTLIFVSHDREFVSSLATRII---EITPDGV 513
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-211 |
2.23e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDN--GSIEIDGKDVVnlRPNQRNIGMVFQA 83
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 YALFPNMTVAQNVSFG--LRV----SGKSRSEIDATVKEMLSLIRLDH--LADRYPYQMSGGQQQRVALARALATKPQVL 155
Cdd:PLN03211 149 DILYPHLTVRETLVFCslLRLpkslTKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 156 LLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHD-QEEALSISDRIVVMHEGR 211
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-217 |
2.35e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 56 DNGSIEIDGKDVV--NLRPNQRNIGMVFQAYALFpNMTVAQNVSFGLRvsgksrseiDAT---VKEMLSLIRLDH----L 126
Cdd:PTZ00265 1275 NSGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE---------DATredVKRACKFAAIDEfiesL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 127 ADRY-----PY--QMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGITTVFVTHdQEEALS 199
Cdd:PTZ00265 1345 PNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIK 1423
|
170
....*....|....*...
gi 559158796 200 ISDRIVVMHEgrADQIGS 217
Cdd:PTZ00265 1424 RSDKIVVFNN--PDRTGS 1439
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-205 |
4.27e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSflGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdvvnlrPNQRNIGMVFQAY-----ALFPNMTVAQN 95
Cdd:PRK13543 31 DFHVDAGEALLVQ--GDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGDRSRFMAYlghlpGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKSRSEIDATVkemLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKiRISLREE 175
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNR 178
|
170 180 190
....*....|....*....|....*....|
gi 559158796 176 IRAIQQKLGITTVFVTHDQEEALSISDRIV 205
Cdd:PRK13543 179 MISAHLRGGGAALVTTHGAYAAPPVRTRML 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-218 |
5.81e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFeTPDNGSIEIDGKDVVNLRPN---QRNIGMVFQAYALFpNMTVAQNVSf 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAelaRHRAYLSQQQTPPF-AMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 gLRVSGKSRSEIDATVKEML-SLIRLDHLADRYPYQMSGGQQQRVALARAL-----ATKP--QVLLLDEPLSALDAKIRI 170
Cdd:PRK03695 92 -LHQPDKTRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 171 SLREEIRAIQQkLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGSP 218
Cdd:PRK03695 171 ALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-217 |
6.79e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.52 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFetPD----NGSIEIDGKDVVNLRPNQRN--- 76
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEERAhlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYALFPNMTvaqNVSFgLRVSGKSR------SEIDA-----TVKEMLSLIRLD-HLADRYPYQ-MSGGQQQRVA 143
Cdd:CHL00131 86 IFLAFQYPIEIPGVS---NADF-LRLAYNSKrkfqglPELDPlefleIINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 144 LARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSIS-DRIVVMHEGRADQIGS 217
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGD 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-217 |
1.25e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 15 TNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETP-DNGSIEIDGkdvvnlrpnqrNIGMVFQAYALFpNMTVA 93
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG-----------SVAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 QNVSFGLRV-SGKSRSEIDATVkemlslirLDHLADRYP-----------YQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:PLN03232 697 ENILFGSDFeSERYWRAIDVTA--------LQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 162 SALDAKI-----RISLREEIRaiqqklGITTVFVThDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:PLN03232 769 SALDAHVahqvfDSCMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-192 |
1.33e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVH---DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG----KDvVNLRPNQRN 76
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKD-INLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 77 IGMVFQAYALFPNmTVAQNVSFGL--------------------------RVSGKSR----------------------- 107
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkRNSCRAKcagdlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 108 ------SEIDATVKEMLSLIRLDHLADRY-------PYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLRE 174
Cdd:PTZ00265 541 yqtikdSEVVDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250
....*....|....*...
gi 559158796 175 EIRAIQQKLGITTVFVTH 192
Cdd:PTZ00265 621 TINNLKGNENRITIIIAH 638
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-215 |
1.50e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.15 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 29 GEFVSFLGPSGCGKTTVLRMIA----GFETPDNGSIEIDGKDVVNLRPNQRniGMVF---QAYALFPNMTVAQNVSF--- 98
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYR--GDVVynaETDVHFPHLTVGETLDFaar 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 ----GLRVSGKSRSEIDATVKEM-LSLIRLDH-----LADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:TIGR00956 165 cktpQNRPDGVSREEYAKHIADVyMATYGLSHtrntkVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 559158796 169 RIslrEEIRAIQQKLGI--TTVFVTHDQ--EEALSISDRIVVMHEGRadQI 215
Cdd:TIGR00956 245 AL---EFIRALKTSANIldTTPLVAIYQcsQDAYELFDKVIVLYEGY--QI 290
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-210 |
1.44e-13 |
|
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: 68.42 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETpdNGSIEidGKDVVNLRPN----QRNIGMVFQAYALFPN 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVIT--GEILINGRPLdknfQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 90 MTVAQnvsfGLRVSGKSRSeidatvkemLSLirldhladrypyqmsgGQQQRVALARALATKPQVLLLDEPLSALDAKIR 169
Cdd:cd03232 94 LTVRE----ALRFSALLRG---------LSV----------------EQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 559158796 170 ISLreeIRAIqQKLGIT--TVFVTHDQEEALSIS--DRIVVMHEG 210
Cdd:cd03232 145 YNI---VRFL-KKLADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-193 |
2.39e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 35 LGPSGCGKTTVLRMIAGFETPDNGSieidgkdvVNLRPNQRnIGMVFQAYALFPNMTVAQNVSFGLR-----------VS 103
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAPGIK-VGYLPQEPQLDPEKTVRENVEEGVAevkaaldrfneIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 104 GK---SRSEIDATVKEMLSLI-RLDHL--------------ADRYP------YQMSGGQQQRVALARALATKPQVLLLDE 159
Cdd:PRK11819 110 AAyaePDADFDALAAEQGELQeIIDAAdawdldsqleiamdALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 559158796 160 PLSALDAkirislrEEIRAIQQKL----GiTTVFVTHD 193
Cdd:PRK11819 190 PTNHLDA-------ESVAWLEQFLhdypG-TVVAVTHD 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-205 |
2.70e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDgKDVVNLRPNQ---RNI 77
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQdppRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 -GMVF---------QAYALFPNMTVAQNVsfGLRVSGKSRSEI---------------DATVKEMLSLIRLDhlADRYPY 132
Cdd:PRK11147 80 eGTVYdfvaegieeQAEYLKRYHDISHLV--ETDPSEKNLNELaklqeqldhhnlwqlENRINEVLAQLGLD--PDAALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559158796 133 QMSGGQQQRVALARALATKPQVLLLDEPLSALDAkirislrEEIRAIQQKL----GiTTVFVTHDQEEALSISDRIV 205
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEGFLktfqG-SIIFISHDRSFIRNMATRIV 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-210 |
5.62e-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: 67.36 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 12 SFGTN-TVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN---LRPNQRNIGMVfqAYA-- 85
Cdd:cd03290 9 SWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfEATRSRNRYSV--AYAaq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 --LFPNMTVAQNVSFGLRVSgKSRSEidaTVKEMLSL---IRLDHLADRYP-----YQMSGGQQQRVALARALATKPQVL 155
Cdd:cd03290 87 kpWLLNATVEENITFGSPFN-KQRYK---AVTDACSLqpdIDLLPFGDQTEigergINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 156 LLDEPLSALDAKIRISLREE-IRAIQQKLGITTVFVTHdQEEALSISDRIVVMHEG 210
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-169 |
5.93e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 66.82 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 16 NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL-RPNQRNIGmvfQAYALFPNMTVAQ 94
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIaKPYCTYIG---HNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 95 NVSFGLRVSGKSrseidATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIR 169
Cdd:PRK13541 90 NLKFWSEIYNSA-----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-210 |
6.83e-13 |
|
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: 67.96 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 16 NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdvvnlrpnqrnIGMVFQAYALFPNmTVAQN 95
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLrvsgksrSEIDATVKEMLSLIRLDHLADRYPYQ-----------MSGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:cd03291 118 IIFGV-------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 559158796 165 DakirISLREEI------RAIQQKlgiTTVFVTHDQEEaLSISDRIVVMHEG 210
Cdd:cd03291 191 D----VFTEKEIfescvcKLMANK---TRILVTSKMEH-LKKADKILILHEG 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-193 |
7.73e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 16 NTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVvNLRPNQRNIGMVFQAYAL---FPnMTV 92
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKNLVAYVPQSEEVdwsFP-VLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNVSFGL--------RVSGKSRSEIDAtvkemlSLIRLDHLADRYPY--QMSGGQQQRVALARALATKPQVLLLDEPLS 162
Cdd:PRK15056 98 EDVVMMGRyghmgwlrRAKKRDRQIVTA------ALARVDMVEFRHRQigELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 559158796 163 ALDAKIR---ISLREEIRAiqqkLGITTVFVTHD 193
Cdd:PRK15056 172 GVDVKTEariISLLRELRD----EGKTMLVSTHN 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-208 |
7.95e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAV-GKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG--KDVVnlrpnQRNIGMVFQAYalFP-----NMTVA 93
Cdd:COG1245 91 YGLPVpKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswDEVL-----KRFRGTELQDY--FKklangEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 ---QNVSF-GLRVSGKSRSEIDAT-----VKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:COG1245 164 hkpQYVDLiPKVFKGTVRELLEKVdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 559158796 165 DAKIRISLREEIRAIQQKlGITTVFVTHDqeeaLSI----SDRIVVMH 208
Cdd:COG1245 244 DIYQRLNVARLIRELAEE-GKYVLVVEHD----LAIldylADYVHILY 286
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-210 |
8.34e-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: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKdvvnlrpnqrnIGMVFQAYALFPNmTVAQNVS 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 98 FGLRVSG-KSRSEIDA-TVKEMLSLIRLDhlaDRYPY-----QMSGGQQQRVALARALATKPQVLLLDEPLSALDakirI 170
Cdd:TIGR01271 509 FGLSYDEyRYTSVIKAcQLEEDIALFPEK---DKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD----V 581
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 559158796 171 SLREEI--RAIQQKLGITTVFVTHDQEEALSISDRIVVMHEG 210
Cdd:TIGR01271 582 VTEKEIfeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-208 |
1.01e-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: 65.67 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 26 VGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVnLRPnqrnigmvfqayalfpnmtvaQNVSfglrvsgk 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKP---------------------QYID-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 106 srseidatvkemlslirldhladrypyqMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKLGI 185
Cdd:cd03222 72 ----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|...
gi 559158796 186 TTVFVTHDQEEALSISDRIVVMH 208
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-195 |
1.18e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVnlrpnqrnigmvfqAY- 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEV--------------AYf 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 85 -----ALFPNMTVAQNVSFG---LRVSGKSRSEidatvkemlslirLDHLAD--------RYPYQ-MSGGQQQRVALARa 147
Cdd:PRK11147 388 dqhraELDPEKTVMDNLAEGkqeVMVNGRPRHV-------------LGYLQDflfhpkraMTPVKaLSGGERNRLLLAR- 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 559158796 148 LATKPQVLL-LDEPLSALDAKIrISLREEIRAIQQKlgiTTVFVTHDQE 195
Cdd:PRK11147 454 LFLKPSNLLiLDEPTNDLDVET-LELLEELLDSYQG---TVLLVSHDRQ 498
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-215 |
1.23e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVlRMIAGFETPDNGSIEIDGKD-VVNLRPNQRNIGMVFQ 82
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TwCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 83 A-YALFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:NF000106 93 Vr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 162 SALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEA------LSISDRIVVMHEGRADQI 215
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDEL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-208 |
1.26e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 67.01 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 29 GEFVSFLGPSGCGKTTVLRMIAGFETPDNGSI--EIDGKDVVN-------------LRPNQRNIGMVFQAYALFPNmtva 93
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddPPDWDEILDefrgselqnyftkLLEGDVKVIVKPQYVDLIPK---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 94 qnvsfglRVSGKSRSEIDAT-----VKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKI 168
Cdd:cd03236 102 -------AVKGKVGELLKKKdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 559158796 169 RISLREEIRAIQQKlGITTVFVTHDqeeaLSI----SDRIVVMH 208
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHD----LAVldylSDYIHCLY 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-229 |
1.30e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVN--LRPNQRNIGMVFQAYALFpnmtvAQN 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLF-----SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKSRseiDATVKEMLSLIRLDHLADRYPYQM-----------SGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:PLN03232 1326 VRFNIDPFSEHN---DADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 165 DAK----IRISLREEIRAiqqklgITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIYNRPASRF 229
Cdd:PLN03232 1403 DVRtdslIQRTIREEFKS------CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-211 |
5.09e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAG------FEtpdnGSIEIDGKdVVNLR----PN 73
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGE-VCRFKdirdSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 74 QRNIGMVFQAYALFPNMTVAQNVSFGLRVSGK---SRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALAT 150
Cdd:NF040905 77 ALGIVIIHQELALIPYLSIAENIFLGNERAKRgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 151 KPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-211 |
5.52e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAG--FETPDNGSIEIDGKDVvNLRPNQRNI--GMVF-----QAYALFP 88
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEV-DVSTVSDAIdaGLAYvtedrKGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 89 NMTVAQNVSF-GL-RVSgkSRSEIDAtVKEMLSlirldhlADRYPYQM--------------SGGQQQRVALARALATKP 152
Cdd:NF040905 354 IDDIKRNITLaNLgKVS--RRGVIDE-NEEIKV-------AEEYRKKMniktpsvfqkvgnlSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158796 153 QVLLLDEPLSALD--AKIrislreEIRAIQQKL---GITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:NF040905 424 DVLILDEPTRGIDvgAKY------EIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
276-351 |
6.14e-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: 60.33 E-value: 6.14e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 276 LALRPEAVSLEARkshDTSLEATIDDVHFLGSVIRTRVILGKNRLSFDTFNDPTHPPPQRGDKVTVHFASHDLLVL 351
Cdd:pfam08402 1 LAIRPEKIRLAAA---ANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-220 |
6.52e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGfetpdngSIEIDGKDVVNlrpnQRNIGMVFQAyALFPNMTVAQNVS 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------QFEISEGRVWA----ERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 98 F-----GLRVSGKSR-SEIDATVKEMLSliRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:PTZ00243 743 FfdeedAARLADAVRvSQLEADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 559158796 172 LREEIraIQQKL-GITTVFVTHdQEEALSISDRIVVMHEGRADQIGSPFD 220
Cdd:PTZ00243 821 VVEEC--FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-207 |
7.60e-12 |
|
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: 62.39 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 28 KGEFVSFLGPSGCGKTTVLRMIAGFETPDNGS-IEIDGkdvvnlrpnqrnigmvfqayalfpnmtvaqnvsfglrvsgks 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 107 rseidATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRA-----IQQ 181
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113
|
170 180 190
....*....|....*....|....*....|.
gi 559158796 182 KLGITTVFVTHDQEEALS-----ISDRIVVM 207
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPallrrRFDRRIVL 144
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-211 |
1.02e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.04 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFE--TPDNGSIEIDGKDVVNLRPNQRNIGMVF 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYAlFPNMTVAQNVSFGLRVSGKS-----------RSEIDATVKEMLSLIRL--DHLADRYPYQMSGGQQQRVALARAL 148
Cdd:PRK09580 82 MAFQ-YPVEIPGVSNQFFLQTALNAvrsyrgqepldRFDFQDLMEEKIALLKMpeDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 149 ATKPQVLLLDEPLSALDAK-IRI------SLREEIRAIqqklgittVFVTHDQEEALSIS-DRIVVMHEGR 211
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDaLKIvadgvnSLRDGKRSF--------IIVTHYQRILDYIKpDYVHVLYQGR 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-231 |
3.13e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVfqAYA 85
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRI--AYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 86 -------LFPNMTVAQNVSFGLRVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLD 158
Cdd:NF033858 82 pqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 159 EPLSALDAKIRI---SLREEIRAiqQKLGITTVFVTHDQEEALSIsDRIVVMHEGRADQIGSPFDIYNRPASR-----FV 230
Cdd:NF033858 162 EPTTGVDPLSRRqfwELIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGADtleaaFI 238
|
.
gi 559158796 231 A 231
Cdd:NF033858 239 A 239
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-192 |
3.29e-11 |
|
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: 64.38 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGM-VFQAYALFPnMTVAQNV 96
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 97 SFGLRvsgksrseiDATVKEMLSLIRLDHLADR---------YPYQMSGGQQQRVALARALATKPQVLLLDEPLSAldak 167
Cdd:TIGR00954 546 RRGLS---------DKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA---- 612
|
170 180
....*....|....*....|....*
gi 559158796 168 IRISLREEIRAIQQKLGITTVFVTH 192
Cdd:TIGR00954 613 VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-215 |
3.31e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 19 VHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQR-NIGMVF-----QAYALFPNMTV 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAiNHGFALvteerRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 93 AQNV----------SFGLRVSGKSRSEIDATVKEMlsliRLDHLADRYPY-QMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:PRK10982 344 GFNSlisnirnyknKVGLLDNSRMKSDTQWVIDSM----RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 162 SALDAKIRISLREEIRAIQQK-LGIttVFVTHDQEEALSISDRIVVMHEGRADQI 215
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-211 |
3.62e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVvNLRPN----QRNIGMVF 81
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkealENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFG------LRVS-GKSRSEIDATVKEM-LSLIRLDHLADrypyqMSGGQQQRVALARALATKPQ 153
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGryptkgMFVDqDKMYRDTKAIFDELdIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALSISDRIVVMHEGR 211
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-207 |
6.55e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 28 KGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDG--KDVVnlrpnQRNIGMVFQAYalFPNmtVAQNvsfGLRVSGK 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEVL-----KRFRGTELQNY--FKK--LYNG---EIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 106 SRsEIDA-------TVKEML-------------SLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALD 165
Cdd:PRK13409 166 PQ-YVDLipkvfkgKVRELLkkvdergkldevvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 559158796 166 AKIRISLREEIRAIQQklGITTVFVTHDqeeaLSI----SDRIVVM 207
Cdd:PRK13409 245 IRQRLNVARLIRELAE--GKYVLVVEHD----LAVldylADNVHIA 284
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-211 |
8.52e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 23 NLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPN--QRNIGMVFQAYALFPnmtvaqnvsfgl 100
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFD------------ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 101 RVSGKSRSEID-ATVKEMLSLIRLDH--------LADrypYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRIS 171
Cdd:PRK10522 411 QLLGPEGKPANpALVEKWLERLKMAHkleledgrISN---LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 559158796 172 LREEIRAIQQKLGITTVFVTHDqEEALSISDRIVVMHEGR 211
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-211 |
9.03e-11 |
|
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: 62.89 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 22 FNLAVGKGEFVsFL-GPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFPnmtvaqnvsf 98
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtaDNREAYRQLFSAVFSDFHLFD---------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 glRVSGKSRSEIDATVKEMLSLIRLDH--------LADRypyQMSGGQQQRVALARALATKPQVLLLDE------Plsal 164
Cdd:COG4615 420 --RLLGLDGEADPARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALLVALLEDRPILVFDEwaadqdP---- 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 165 dakiriSLRE--------EIRAiqqkLGITTVFVTHDqEEALSISDRIVVMHEGR 211
Cdd:COG4615 491 ------EFRRvfytellpELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGK 534
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-217 |
1.39e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNL--KKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDnGSIEIDGK--DVVNLRPNQRNIGM 79
Cdd:TIGR01271 1218 MDVQGLtaKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVswNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNmTVAQNVSFGLRVSGKsrsEIDATVKE--MLSLI-----RLDHLADRYPYQMSGGQQQRVALARALATKP 152
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQWSDE---EIWKVAEEvgLKSVIeqfpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559158796 153 QVLLLDEPLSALDAkirISLREEIRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:TIGR01271 1373 KILLLDEPSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-218 |
1.74e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 18 VVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpnmtvAQN 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskFGLMDLRKVLGIIPQAPVLF-----SGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 96 VSFGLRVSGKSRseiDATVKEMLSLIRLDHLADRYPYQM-----------SGGQQQRVALARALATKPQVLLLDEPLSAL 164
Cdd:PLN03130 1329 VRFNLDPFNEHN---DADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 165 ----DAKIRISLREEIRAiqqklgITTVFVTHDQEEALSiSDRIVVMHEGRADQIGSP 218
Cdd:PLN03130 1406 dvrtDALIQKTIREEFKS------CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTP 1456
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-217 |
3.59e-10 |
|
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: 59.87 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSF--GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDnGSIEIDGK--DVVNLRPNQRNIGM 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVswNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 80 VFQAYALFPNmTVAQNvsfgLRVSGKSRSEIDATVKEMLSLI--------RLDHLADRYPYQMSGGQQQRVALARALATK 151
Cdd:cd03289 82 IPQKVFIFSG-TFRKN----LDPYGKWSDEEIWKVAEEVGLKsvieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158796 152 PQVLLLDEPLSALDAKIRISLReeiRAIQQKLGITTVFVTHDQEEALSISDRIVVMHEGRADQIGS 217
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-167 |
5.70e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 29 GEFVSFLGPSGCGKTTVLRMIAGFETpdNGSIEiDGKDVVNLRPN----QRNIGMVFQAYALFPNMTVAQNVSFG--LRV 102
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT--TGVIT-GGDRLVNGRPLdssfQRSIGYVQQQDLHLPTSTVRESLRFSayLRQ 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 103 SGK-SRSEIDATVKEMLSLIRLDHLADRYPYQMSGG----QQQRVALARALATKPQVLL-LDEPLSALDAK 167
Cdd:TIGR00956 866 PKSvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-257 |
3.57e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 26 VGKGEFVSFLGPSGCGKTTVL----RMIagfETPdNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFpNMTVAQNVS-- 97
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV---EVC-GGEIRVNGREIgaYGLRELRRQFSMIPQDPVLF-DGTVRQNVDpf 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 98 --------------FGLRVSGKSRSE-IDATVKEMLSlirldhladrypyQMSGGQQQRVALARALATKPQ-VLLLDEPL 161
Cdd:PTZ00243 1408 leassaevwaalelVGLRERVASESEgIDSRVLEGGS-------------NYSVGQRQLMCMARALLKKGSgFILMDEAT 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 162 S----ALDAKIRISLREEIRAIqqklgitTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNRPASRFvasfvgtL 237
Cdd:PTZ00243 1475 AnidpALDRQIQATVMSAFSAY-------TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF-------H 1540
|
250 260
....*....|....*....|
gi 559158796 238 NMLEASVSEPAQNSIDLDGR 257
Cdd:PTZ00243 1541 SMVEALGRSEAKRFLQLVGR 1560
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-221 |
3.65e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 14 GTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDV--VNLRPNQRNIGMVFQAYALFPNmT 91
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIakIGLHDLRFKITIIPQDPVLFSG-S 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 92 VAQNVS-FGlrvsgkSRSEID-------ATVKEMLSLI--RLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPL 161
Cdd:TIGR00957 1376 LRMNLDpFS------QYSDEEvwwalelAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 162 SALDAKIRISLREEIRAiqQKLGITTVFVTHDQEEALSISdRIVVMHEGRADQIGSPFDI 221
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-197 |
4.18e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 6 IKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGfETPDNGSIEI--------DGKDVVNLRpnqRNI 77
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSNDLtlfgrrrgSGETIWDIK---KHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 78 GMVFQAYAL-FPNMTVAQNV-------SFGL--RVSGKSRSEIDatvkEMLSLIRLD-HLADRYPYQMSGGQQQRVALAR 146
Cdd:PRK10938 339 GYVSSSLHLdYRVSTSVRNVilsgffdSIGIyqAVSDRQQKLAQ----QWLDILGIDkRTADAPFHSLSWGQQRLALIVR 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 559158796 147 ALATKPQVLLLDEPLSALDAKIRISLReeiRAIQQKLG---ITTVFVTHDQEEA 197
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVR---RFVDVLISegeTQLLFVSHHAEDA 465
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-190 |
9.08e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 1 MAFLNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNL--RPNQRNIG 78
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 79 MVFQAyalfpNMTvaQNVSFGLRVSGKSRSEI------DATVKEMLS-LIRLDHLADRYPYQMSGGQQQRVALARALATK 151
Cdd:PRK10938 81 DEWQR-----NNT--DMLSPGEDDTGRTTAEIiqdevkDPARCEQLAqQFGITALLDRRFKYLSTGETRKTLLCQALMSE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 559158796 152 PQVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFV 190
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-224 |
4.04e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 32 VSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGKDVVNLRPNQRNIGMVFQAYALFPNMTVAQNV----------SFGlr 101
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVpeqklrahlgSFG-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 102 VSGksrseidatvkemlslirldHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAkirislrEEIRAIQQ 181
Cdd:PLN03073 616 VTG--------------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL-------DAVEALIQ 668
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 559158796 182 KLGI---TTVFVTHDQEEALSISDRIVVMHEGRADQIGSPFDIYNR 224
Cdd:PLN03073 669 GLVLfqgGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-216 |
8.47e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGkdvvnlrpnqrNIGMVFQAYALFPNMTVAQNVSFGL 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 101 RVSGKSRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQ 180
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 559158796 181 QKlGITTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:PRK13546 191 EQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-216 |
1.80e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 26 VGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIDGkdvvnlrpnqrNIGMVFQAYALFPNMTVAQNVSFGLRVSGK 105
Cdd:PRK13545 47 VPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNGQLTGIENIELKGLMMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 106 SRSEIDATVKEMLSLIRLDHLADRYPYQMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQKlGI 185
Cdd:PRK13545 116 TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GK 194
|
170 180 190
....*....|....*....|....*....|.
gi 559158796 186 TTVFVTHDQEEALSISDRIVVMHEGRADQIG 216
Cdd:PRK13545 195 TIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-220 |
3.74e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTNTVVHDFNLAVGKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEIdGKDVV----------NLRPN 73
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKlgyfaqhqleFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 74 QRNIGMVFQayaLFPNMTVAQNVSF--GLRVSGKSRSEIDAtvkemlslirldhladrypyQMSGGQQQRVALARALATK 151
Cdd:PRK10636 392 ESPLQHLAR---LAPQELEQKLRDYlgGFGFQGDKVTEETR--------------------RFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 152 PQVLLLDEPLSALDAKIRISLREEIRAIQQKLgittVFVTHDQEEALSISDRIVVMHEGRADqigsPFD 220
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE----PFD 509
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-167 |
1.04e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 29 GEFVSFLGPSGCGKTTVLRMIAGFETpdNGSIEIDGKdVVNLRPNQ----RNIGMVFQAYALFPNMTVAQNVSFG--LRV 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIR-ISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSafLRL 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 103 SGK-SRSEIDATVKEMLSLIRLDHLADR---YP--YQMSGGQQQRVALARALATKPQVLLLDEPLSALDAK 167
Cdd:PLN03140 983 PKEvSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
99-207 |
3.79e-06 |
|
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: 46.55 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 99 GLRVSGKSRSEIDATVKEMLSLIRLDHLA------------DRYPYQMSGGQQQRVALARALA--TKPQVLLLDEPLSAL 164
Cdd:cd03238 41 GLYASGKARLISFLPKFSRNKLIFIDQLQflidvglgyltlGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGL 120
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 559158796 165 DAKIRISLREEIRAIQQkLGITTVFVTHDqEEALSISDRIVVM 207
Cdd:cd03238 121 HQQDINQLLEVIKGLID-LGNTVILIEHN-LDVLSSADWIIDF 161
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-207 |
5.15e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 21 DFNLAVGKGEFVSFLGPSGCGKTTVL---------------------RMIAGFETPDNGSIE-------IDGKdvvNLRP 72
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEglspaiaIDQK---TTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 73 NQRN-IGMVFQAYA----LFPNMTVAQNVSFGLRVSgksrseidatvkemlslirLDHLA-DRYPYQMSGGQQQRVALAR 146
Cdd:cd03270 90 NPRStVGTVTEIYDylrlLFARVGIRERLGFLVDVG-------------------LGYLTlSRSAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158796 147 ALATKPQVLL--LDEPLSALDAKIRISLREEIRAIQQkLGITTVFVTHDqEEALSISDRIVVM 207
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHD-EDTIRAADHVIDI 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
133-195 |
5.57e-06 |
|
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: 46.45 E-value: 5.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 133 QMSGGQQQ------RVALARALATKPQVLLLDEPLSALDA-KIRISLREEIRAIQQKLGITTVFVTHDQE 195
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEE 184
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
87-227 |
3.72e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 87 FPNMTVAQNVSF--GLRVSGKSRSEIDATVKEMLSLIR------LDHLA-DRYPYQMSGGQQQRVALARALATK-PQVL- 155
Cdd:TIGR00630 433 VSELSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLGflidvgLDYLSlSRAAGTLSGGEAQRIRLATQIGSGlTGVLy 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158796 156 LLDEPLSALDAKIRISLREEIRAIqQKLGITTVFVTHDqEEALSISDRIVVM------HEGRADQIGSPFDIYNRPAS 227
Cdd:TIGR00630 513 VLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIgpgageHGGEVVASGTPEEILANPDS 588
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-224 |
7.88e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 133 QMSGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIraiqQKLGITTVFVTHDQEEALSISDRIVVMHEGRA 212
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL----LKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
90
....*....|..
gi 559158796 213 DQIGSPFDIYNR 224
Cdd:PLN03073 420 VTYKGDYDTFER 431
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-207 |
2.05e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 559158796 133 QMSGGQQQRVALARALA---TKP-QVLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDQEEALsISDRIVVM 207
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAE-LADKLIHI 153
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-236 |
2.75e-04 |
|
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: 41.82 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 4 LNIKNLKKSFGTN--TVVHDFNLAVGKGEFVSFLGPSGCGKTTV----LRMIAGFEtpdnGSIEIDGKDV--VNLRPNQR 75
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDIskLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 76 NIGMVFQAYALFpnmtvAQNVSFGLRVSGKSrseIDATVKEMLSLIRLDHLADRYP-----------YQMSGGQQQRVAL 144
Cdd:cd03288 96 RLSIILQDPILF-----SGSIRFNLDPECKC---TDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 145 ARALATKPQVLLLDEPLSALD-AKIRISLREEIRAIQQKlgiTTVFVTHDQEEALSiSDRIVVMHEGRADQIGSPFDIYN 223
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
250
....*....|...
gi 559158796 224 RPASRFvASFVGT 236
Cdd:cd03288 244 QEDGVF-ASLVRT 255
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-165 |
7.56e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 23 NLAV--GKGEFVSFLGPSGCGKTTVLRMIAGFETPDNGSIEID-GKDVVNLRPNQ------RNIGMVFQA---------- 83
Cdd:PRK15064 19 NISVkfGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQfafeefTVLDTVIMGhtelwevkqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 84 ----YALfPNMTVAQnvsfGLRVSgksrsEIDATVKEM-----------LsLIRLDHLADRYPYQMSG---GQQQRVALA 145
Cdd:PRK15064 99 rdriYAL-PEMSEED----GMKVA-----DLEVKFAEMdgytaearageL-LLGVGIPEEQHYGLMSEvapGWKLRVLLA 167
|
170 180
....*....|....*....|
gi 559158796 146 RALATKPQVLLLDEPLSALD 165
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLD 187
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
135-205 |
1.86e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559158796 135 SGGQQQRVALARALATKPQVLLLDEPLSALDAKIRISLREEIRAIQQklgiTTVFVTHDQEEALSISDRIV 205
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
82-205 |
1.99e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158796 82 QAYALFPNMTVAQNVSFGLRVSGKSRS--EIDATVKEMLS-LIRL--DHLA-DRYPYQMSGGQQQRVALARALATKPQ-- 153
Cdd:PRK00635 419 KTFAEFQQMSLQELFIFLSQLPSKSLSieEVLQGLKSRLSiLIDLglPYLTpERALATLSGGEQERTALAKHLGAELIgi 498
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 559158796 154 VLLLDEPLSALDAKIRISLREEIRAIQQKlGITTVFVTHDqEEALSISDRIV 205
Cdd:PRK00635 499 TYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-EQMISLADRII 548
|
|
|